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Virus-Wirt Wechselwirkungen

Virus-bedingte Erkrankungen sind eine große Bedrohung für die menschliche Gesundheit. Wir konzentrieren uns auf Proteine, die durch das humane Immundefizienz-Virus (HIV), Dengue-Virus (DENV), Hepatitis-C-Virus (HCV) bzw. SARS-Coronavirus (SARS-CoV) kodiert werden. Diese Viren sind die Erreger der erworbenen Immunschwäche (AIDS), von Dengue-Fieber, von chronischer Hepatitis, und des schweren akuten respiratorischen Syndroms (SARS). Trotz seines komplexen Immunsystems ist ein einmal infizierter Mensch nicht mehr in der Lage, Viren wie HIV-1 aus seinem Körper zu eliminieren. Auch entwickeln die meisten mit HCV infizierten Personen eine chronische Infektion. Nach wie vor ist es dringend notwendig, gegen diese und andere Viren präventive Impfstoffe sowie sicherere und hochwirksame antivirale Therapien zu entwickeln.

Viren modulieren selektiv Funktionen ihrer jeweiligen Wirtszellen, um ihre eigene Vermehrung und Persistenz zu gewährleisten. Dabei greifen virale Proteine ​​in verschiedenste zelluläre Signalwege und Prozesse wie die Apoptose und Autophagie ein. Häufig führt dies dazu, dass wichtige antivirale Abwehrmechanismen der infizierten Wirtszellen ausgeschaltet werden. Wir untersuchen die Wechselwirkung ausgewählter regulatorischer/nicht-struktureller Virusproteine mit bestimmten Wirtszellproteinen ​​oder auch Zellmembranen. Dabei wollen wir verstehen, wie diese Wechselwirkungen zu einer Steigerung der Virusreplikation führen können oder wie durch sie das Immunsystem des Wirts ausgeschaltet oder zum Nutzen des Virus missbraucht werden kann.

Unsere Forschung fokussiert sich auf individuelle virale Proteine und ihre entsprechenden zellulären Interaktionspartner. Langfristig wird ein besseres Verständnis dieser Wechselwirkungen bis auf atomarer Ebene zu neuen Konzepten für innovative antivirale Therapien führen.

Wir nutzen ein breites Spektrum an Methoden, die von der Molekularbiologie über die Zellbiologie bis hin zur Biophysik reichen.  Unser Institut ist sehr gut ausgestattet für die Expression und Reinigung von rekombinanten Proteinen, Phagendisplay-Selektion oder Yeast Two-Hybrid Screens. Struktur und Dynamik  werden mittels NMR-Spektroskopie oder Röntgenkristallisation aufgeklärt. Zusammen mit unseren externem Kooperationspartner, die z.B. an den Universitäten in Düsseldorf und Tel Aviv, Israel beheimatet sind, prüfen wir die biologische Relevanz, der untersuchten Interaktionen zwischen viralen Proteinen und Wirtsfaktoren.

Weiterführende Links:

undefinedArbeitsgruppe Hänel

undefinedArbeitsgruppe Hoffmann

undefinedArbeitsguppe König

undefinedArbeitsgruppe Schwarten

Publikationen

  • Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C 
    Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C 
    J Am Chem Soc 146, 399-409 (2024) 
    https://doi.org/10.1021/jacs.3c09586  
    https://pubs.acs.org/doi/10.1021/jacs.3c09586  
  • Sieme D, Rezaei-Ghaleh N 
    Water dynamics in eutectic solutions of sodium chloride and magnesium sulfate: implications for life in Europa's subsurface ocean and ice shell 
    Phys Chem Chem Phys 26, 105-115 (2024) 
    https://doi.org/10.1039/d3cp03455k  
    https://pubs.rsc.org/en/content/articlelanding/2024/CP/D3CP03455K  
  • Abyzov A, Mandelkow E, Zweckstetter M, Rezaei-Ghaleh N 
    Fast Motions Dominate Dynamics of Intrinsically Disordered Tau Protein at High Temperatures 
    Chem Eur J 29, e202203493 (2023) 
    https://doi.org/10.1002/chem.202203493  
  • Altendorf T, Gering I, Santiago-Schübel B, Aghabashlou Saisan S, Tamgüney G, Tusche M, Honold D, Schemmert S, Hoyer W, Mohrlüder J, Willbold D 
    Stabilization of monomeric Tau protein by all D-enantiomeric peptide ligands as therapeutic strategy for Alzheimer's disease and other tauopathies 
    Int J Mol Sci 24, 2161 (2023) 
    https://doi.org/10.3390/ijms24032161  
  • Becker C, Giller K, Sieme D, Rezaei-Ghaleh N 
    Maturation of amyloid ß fibrils alters their molecular stability 
    Phys Chem Chem Phys 25, 15099 - 15103 (2023) 
    https://doi.org/10.1039/d3cp01276j  
    https://pubs.rsc.org/en/content/articlelanding/2023/CP/D3CP01276J  
  • Borggräfe J, Gertzen CGW, Viegas A, Gohlke H, Etzkorn M 
    The architecture of the 10-23 DNAzyme and its implications for DNA-mediated catalysis  
    FEBS Journal 290, 2011-2021 (2023) 
    https://doi.org/10.1111/febs.16698  
  • Gomes CM, Hoyer W, Luo J 
    Editorial: The biochemistry of amyloids in neurodegenerative diseases, volume II 
    Front Neurosci 17, 1236518 (2023) 
    https://doi.org/10.3389/fnins.2023.1236518  
  • Heid LF, Kupreichyk T, Schützmann MP, Schneider W, Stoldt M, Hoyer W 
    Nucleation of α-Synuclein Amyloid Fibrils Induced by Cross-Interaction with β-Hairpin Peptides Derived from Immunoglobulin Light Chains 
    Int J Mol Sci 24, 16132 (2023) 
    https://doi.org/10.3390/ijms242216132  
  • Kutzsche J, Guzman GA, Willuweit A, Kletke O, Wollert E, Gering I, Jürgens D, Breitkreutz J, Stark H, Beck-Sickinge AG, Klöcker N, Hidalgo P, Willbold D. 
    An orally available N-type calcium channel inhibitor for the treatment of neuropathic pain.  
    Br J Pharmacol. , (2023) 
    https://pubmed.ncbi.nlm.nih.gov/38157867/  
  • Kutzsche J, Schemmert S, Bujnicki T, Zafiu C, Halbgebauer S, Kraemer-Schulien V, Pils M, Blömeke L, Post J, Kulawik A, Jürgens D, Rossberg WM, Hümpel M, Bannach O, Otto M, Araujo JA, Willuweit A, Willbold D. 
    Oral treatment with the all-d-peptide RD2 enhances cognition in aged beagle dogs - A model of sporadic Alzheimer's disease  
    Heliyon 29;9(8):e18443, (2023) 
    https://pubmed.ncbi.nlm.nih.gov/37609390/  
  • Matoušek J, Wüsthoff KP, Steger G 
    “Pathomorphogenic” Changes Caused by Citrus Bark Cracking Viroid and Transcription Factor TFIIIA-7ZF Variants Support Viroid Propagation in Tobacco 
    Int. J. Mol. Sci. 24, 7790 (2023) 
    https://doi.org/10.3390/ijms24097790  
  • Muschol M, Hoyer W 
    Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils 
    Front Mol Biosci 10, 1120416 (2023) 
    https://doi.org/10.3389/fmolb.2023.1120416  
  • Pils M, Dybala A, Rehn F, Blömeke L, Bujnicki T, Kraemer-Schulien V, Hoyer W, Riesner D, Willbold D, Bannach O 
    Development and implementation of an internal quality control sample to standardize oligomer-based diagnostics of Alzheimer's disease 
    Diagnostics 13, 1702 (2023) 
    https://doi.org/10.3390/diagnostics13101702  
  • Rezaei-Ghaleh N, Amininasab M, Giller K, Becker S 
    Familial Alzheimer's Disease-Related Mutations Differentially Alter Stability of Amyloid-Beta Aggregates 
    J Phys Chem Lett 14, 1427-1435 (2023) 
    https://doi.org/10.1021/acs.jpclett.2c03729  
  • Schulz CM, Pfitzer A, Hoyer W 
    Fibril core regions in engineered α-synuclein dimer are crucial for blocking of fibril elongation 
    BBA Adv 4, 100110 (2023) 
    https://doi.org/10.1016/j.bbadva.2023.100110  
  • Steger G, Riesner, D 
    Contributions of viroid research to methods for RNA purification, diagnostics, and secondary structure prediction. 
    Fundamentals of viroid biology (Adkar-Purushothama CR, Sano T, Perreault J-P, Yanjarappa SM, Di Serio F, Daròs J.-A, eds) Academic Press, Elsevier , 394–446 (2023) 
  • Steger G, Wüsthoff KP, Matoušek J, Riesner D 
    Viroids: non-coding circular RNAs are tiny pathogens provoking a broad response in host plants. 
    RNA Structure and Function, RNA Technologies 14 (Barciszewski J, ed.) Springer , 295–309 (2023) 
  • Willuweit A, Humpert S, Schöneck M, Endepols H, Burda N, Gremer L, Gering I, Kutzsche J, Shah NJ, Langen KJ, Neumaier B, Willbold D, Drzezga A. 
    Evaluation of the 18F-labeled analog of the therapeutic all-D-enantiomeric peptide RD2 for amyloid β imaging  
    Eur J Pharm Sci 184:106421, (2023) 
    https://doi.org/10.1016/j.ejps.2023.106421  
    https://pubmed.ncbi.nlm.nih.gov/36889654/  
  • Wintz K, Post J, Langen K-J, Willbold D, Willuweit A, Kutzsche J 
    Oral Treatment with d-RD2RD2 Impedes Early Disease Mechanisms in SOD1*G93A Transgenic Mice but Does Not Prolong Survival  
    Biomedicines 11(4), 995, (2023) 
    https://doi.org/10.3390/biomedicines11040995  
    https://www.mdpi.com/2227-9059/11/4/995  
  • Amariei DA, Pozhydaieva N, David B, Schneider P, Classen T, Gohlke H, Weiergräber OH, Pietruszka J 
    Enzymatic C3-Methylation of Indoles Using Methyltransferase PsmD─Crystal Structure, Catalytic Mechanism, and Preparative Applications 
    ACS Catal 12, 14130-14139 (2022) 
    https://doi.org/10.1021/acscatal.2c04240  
  • Bartl, J. and Zanini, M. and Bernardi, F. and Forget, A. and Blümel, L. and Talbot, J. and Picard D, Qin N, Cancila G, Gao Q, Nath S, Koumba IM, Wolter M, Kuonen F, Langini M, Beez, T, Munoz C, Pauck D, Marquardt V, Yu H, Souphron J, Korsch M, Mölders C, Berger D, Göbbels S, Meyer FD, Scheffler B, Rotblat B, Diederichs S, Ramaswamy V, Suzuki H, Oro A, Stühler K, Stefanski A, Fischer U, Leprivier G, Willbold D, Steger G, Buell A, Kool M, Lichter P, Pfister SM, Northcott PA, Taylor MD, Borkhardt A, Reifenberger G, Ayrault O, Remke M 
    The HHIP-AS1 lncRNA promotes tumorigenicity through stabilization of dynein complex 1 in human SHH-driven tumors. 
    Nat. Commun . 13, 4061 (2022) 
    https://doi.org/10.1038/s41467-022-31574-z  
  • Borggräfe J, Etzkorn M 
    Solution NMR Spectroscopy as a Tool to Study DNAzyme Structure and Function. 
    Methods in Molecular Biology 2439, 131-151 (2022) 
    https://doi.org/10.1007/978-1-0716-2047-2_10  
  • Borggräfe J, Victor J, Rosenbach H, Viegas A, Gertzen CGW, Wuebben C, Kovacs H, Gopalswamy M, Riesner D, Steger G, Schiemann O, Gohlke H, Span I, Etzkorn M  
    Time-resolved structural analysis of an RNA-cleaving DNA catalyst. 
    Nature 601, 144-149 (2022) 
    https://doi.org/10.1038/s41586-021-04225-4  
  • Braczynski AK, Sevenich M, Gering I, Kupreichyk T, Agerschou ED, Kronimus Y, Habib P, Stoldt M, Willbold D, Schulz JB, Bach JP, Falkenburger BH, Hoyer W 
    Alpha-synuclein-specific naturally occurring antibodies inhibit aggregation in vitro and in vivo 
    Biomolecules 12, 469 (2022) 
    https://doi.org/10.3390/biom12030469  
  • Brown H, Chung M, Üffing A, Batistatou N, Tsang T, Doskocil S, Mao W, Willbold D, Bast RC Jr, Lu Z, Weiergräber OH, Kritzer JA 
    Structure-Based Design of Stapled Peptides That Bind GABARAP and Inhibit Autophagy 
    J Am Chem Soc 144, 14687-14697 (2022) 
    https://doi.org/10.1021/jacs.2c04699  
  • Etzkorn M 
    Atomare Einblicke in die Dynamik der Membransysteme und der Biokatalyse. 
    Biospektrum 28, 30-33 (2022) 
    https://doi.org/10.1007/s12268-022-1707-8  
  • Florian Bleffert, Joachim Granzin, Muttalip Caliskan, Stephan N Schott-Verdugo, Meike Siebers, Björn Thiele, Laurence Rahme, Sebastian Felgner, Peter Dörmann, Holger Gohlke* , Renu Batra-Safferling*, Karl-Erich Jaeger, Filip Kovacic* 
    Structural, mechanistic, and physiological insights into phospholipase A-mediated membrane phospholipid degradation in Pseudomonas aeruginosa. 
    eLife 11, e72824 (2022) 
    https://doi.org/10.7554/eLife.72824  
  • Glueck D, Grethen A, Das M, Mmeka OP, Perez Patallo E, Meister A, Rajender R, Ahlhelm J, Kins S, Raeschle M, Victor J, Etzkorn M, Koeck Z, Bernhard F, Babalola JO, Vargas C, Keller S 
    Electroneutral polymer nanodiscs enable interference-free probing of membrane proteins in a lipid-bilayer environment  
    Small 18, 2202492 (2022) 
    https://doi.org/10.1002/smll.202202492  
  • Gopalswamy M, Kroeger T, Bickel D, Frieg B, Akter S, Schott-Verdugo S, Viegas A, Pauly T, Mayer M, Przibilla J, Reiners J, Nagel-Steger L, Smits SHJ, Groth G, Etzkorn M, Gohlke H 
    Biophysical and pharmacokinetic characterization of a small-molecule inhibitor of RUNX1/ETO tetramerization with anti-leukemic effects. 
    Sci Rep 12, 1-18 (2022) 
    https://doi.org/10.1038/s41598-022-17913-6  
  • Hemmer S, Schulte M, Knieps-Grünhagen E, Granzin J, Willbold D, Jaeger KE, Batra-Safferling R, Panwalkar V, Krauss U. 
    Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery. 
    Photochem Photobiol Sci , (2022) 
    https://doi.org/10.1007/s43630-022-00346-5  
  • Huwa N, Weiergräber OH, Fejzagić AV, Kirsch C, Schaffrath U, Classen T 
    The Crystal Structure of the Defense Conferring Rice Protein OsJAC1 Reveals a Carbohydrate Binding Site on the Dirigent-like Domain 
    Biomolecules 12, 1126 (2022) 
    https://doi.org/10.3390/biom12081126  
  • Kass B, Schemmert S, Zafiu C, Pils M, Bannach O, Kutzsche J, Bujnicki T, Willbold D. 
    Aβ oligomer concentration in mouse and human brain and its drug-induced reduction ex vivo. 
    Cell Rep Med. 3(5):100630, (2022) 
    https://doi.org/10.1016/j.xcrm.2022.100630  
  • Kirchgässler N, Rosenbach H, Span I 
    Stability and Activity of the 10–23 DNAzyme Under Molecular Crowding Conditions. 
    Methods in Molecular Biology 2439, 79-89 (2022) 
    https://doi.org/10.1007/978-1-0716-2047-2_6  
  • Maity D, Oh Y, Gremer L, Hoyer W, Magzoub M, Hamilton AD 
    Cucurbit[7]uril inhibits islet amyloid polypeptide aggregation by targeting N terminus hot segments and attenuates cytotoxicity 
    Chemistry , e202200456 (2022) 
    https://doi.org/10.1002/chem.202200456  
  • Matoušek J, Steger G 
    The Splicing Variant TFIIIA-7ZF of Viroid-Modulated Transcription Factor IIIA Causes Physiological Irregularities in Transgenic Tobacco and Transient Somatic Depression of “Degradome” Characteristic for Developing Pollen. 
    Cells 11, (2022) 
    https://doi.org/10.3390/cells11050784  
  • Nedaei H, Rezaei-Ghaleh N, Giller K, Becker S, Karami L, Moosavi-Movahedi AA, Griesinger C, Saboury AA 
    The calcium-free form of atorvastatin inhibits amyloid-β(1-42) aggregation in vitro 
    J Biol Chem 298, 101662 (2022) 
    https://doi.org/10.1016/j.jbc.2022.101662  
  • Pantoja CF, Zweckstetter M, Rezaei-Ghaleh N 
    Dynamical component exchange in a model phase separating system: an NMR-based approach 
    Phys Chem Chem Phys 24, 6169-6175 (2022) 
    https://doi.org/10.1039/d2cp00042c  
  • Rafiei Y, Salmani B, Mirzaei-Behbahani B, Taleb M, Meratan AA, Ramezani M, Nikfarjam N, Becker S, Rezaei-Ghaleh N 
    Polyphenols-Based Nanosheets of Propolis Modulate Cytotoxic Amyloid Fibril Assembly of α-Synuclein 
    ACS Chem Neurosci 13, 3168-3179 (2022) 
    https://doi.org/10.1021/acschemneuro.2c00465  
  • Rahban M, Zolghadri S, Salehi N, Ahmad F, Haertlé T, Rezaei-Ghaleh N, Sawyer L, Saboury AA 
    Thermal stability enhancement: Fundamental concepts of protein engineering strategies to manipulate the flexible structure 
    Int J Biol Macromol 214, 642-654 (2022) 
    https://doi.org/10.1016/j.ijbiomac.2022.06.154  
  • Rezaei-Ghaleh N 
    Water Dynamics in Highly Concentrated Salt Solutions: A Multi-Nuclear NMR Approach 
    ChemistryOpen 11, e202200080 (2022) 
    https://doi.org/10.1002/open.202200080  
  • Rezaei-Ghaleh N, Agudo-Canalejo J, Griesinger C, Golestanian R 
    Molecular Diffusivity of Click Reaction Components: The Diffusion Enhancement Question 
    J Am Chem Soc 144, 1380-1388 (2022) 
    https://doi.org/10.1021/jacs.1c11754  
  • Rezaei-Ghaleh N, Agudo-Canalejo J, Griesinger C, Golestanian R 
    Response to Comment on "Following Molecular Mobility during Chemical Reactions: No Evidence for Active Propulsion" and "Molecular Diffusivity of Click Reaction Components: The Diffusion Enhancement Question" 
    J Am Chem Soc 144, 13441-13445 (2022) 
    https://doi.org/10.1021/jacs.2c02850  
  • Rosenbach H, Span I 
    Obtaining Crystals of Nucleic Acids in Complex with the Protein U1A Using the Soaking Method 
    Methods in Molecular Biology 2439, 105-115 (2022) 
    https://doi.org/10.1007/978-1-0716-2047-2_8  
  • Rosenbach H, Steger G 
    Fluorescence-Based Kinetic Measurements for RNA-Cleaving DNAzymes 
    Methods in Molecular Biology 2439, 65-77 (2022) 
    https://doi.org/10.1007/978-1-0716-2047-2_5  
  • Sevenich M, Honold D, Willuweit A, Kutzsche J, Mohrlüder J, Willbold D. 
    Development of an α-synuclein fibril and oligomer specific tracer for diagnosis of Parkinson's disease, dementia with Lewy bodies and multiple system atrophy.  
    Neurochem Int. 161, 105422 (2022) 
    https://doi.org/10.1016/j.neuint.2022.105422  
    https://pubmed.ncbi.nlm.nih.gov/36252819/  
  • Sieme D, Griesinger C, Rezaei-Ghaleh N 
    Metal Binding to Sodium Heparin Monitored by Quadrupolar NMR 
    Int J Mol Sci 23, 13185 (2022) 
    https://doi.org/10.3390/ijms232113185  
  • Steger G 
    Predicting the Structure of a Viroid: Structure, Structure Distribution, Consensus Structure, and Structure Drawing 
    Methods in Molecular Biology 2316, 331-371 (2022) 
    https://doi.org/10.1007/978-1-0716-1464-8_26  
  • Steger G, Rosenbach H, Span I (Eds) 
    DNAzymes 
    Methods in Molecular Biology 2439, (2022) 
    https://link.springer.com/book/10.1007/978-1-0716-2047-2  
  • Steger G, Victor J 
    Design of a DNAzyme 
    Methods in Molecular Biology 2439, 47-63 (2022) 
    https://doi.org/10.1007/978-1-0716-2047-2_4  
  • Törner R, Kupreichyk T, Gremer L, Debled EC, Fenel D, Schemmert S, Gans P, Willbold D, Schoehn G, Hoyer W, Boisbouvier J 
    Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin 
    Nat Commun 13, 2363 (2022) 
    https://doi.org/10.1038/s41467-022-30042-y  
  • Törner R, Kupreichyk T, Hoyer W, Boisbouvier J 
    The role of heat shock proteins in preventing amyloid toxicity 
    Front Mol Biosci 9, 1045616 (2022) 
    https://doi.org/10.3389/fmolb.2022.1045616  
  • Weiergräber OH, Petrović D, Kislat A, Pattky M, Fabig J, Batra-Safferling R, Schulte am Esch J, Hänel K, Huhn C, Strodel B, Homey B, Willbold D 
    Structure and Dynamics of Human Chemokine CCL16—Implications for Biological Activity 
    Biomolecules 12, 1588 (2022) 
    https://doi.org/10.3390/biom12111588  
  • Wüsthoff K, Steger G 
    Conserved Motifs and Domains in Members of Pospiviroidae 
    Cells 11, 230 (2022) 
    https://doi.org/10.3390/cells11020230  
  • Agerschou ED, Schützmann MP, Reppert N, Wördehoff MM, Shaykhalishahi H, Buell AK, Hoyer W 
    β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation 
    Biophys. Chem. 269, 106519 (2021) 
    https://doi.org/10.1016/j.bpc.2020.106519  
  • Arinkin V, Granzin J, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R. 
    Structural determinants underlying the adduct lifetime in the LOV proteins of Pseudomonas putida. 
    FEBS J 288(16), 4955-4972 (2021) 
    https://doi.org/10.1111/febs.15785  
  • Bocharov, E. V., L. Gremer, A. S. Urban, I. S. Okhrimenko, P. E. Volynsky, K. D. Nadezhdin, O. V. Bocharova, D. A. Kornilov, Y. A. Zagryadskaya, A. V. Kamynina, P. K. Kuzmichev, J. Kutzsche, N. Bolakhrif, A. Müller-Schiffmann, N. A. Dencher, A. S. Arseniev, R. G. Efremov, V. I. Gordeliy and D. Willbold 
    All-d-Enantiomeric Peptide D3 Designed for Alzheimer’s Disease Treatment Dynamically Interacts with Membrane-Bound Amyloid-β Precursors. 
    Journal of Medicinal Chemistry , (2021) 
    https://doi.org/10.1021/acs.jmedchem.1c00632  
  • Camargo LC, Honold D, Bauer R, Shah NJ, Langen KJ, Willbold D, Kutzsche J, Willuweit A, Schemmert S. 
    Sex-Related Motor Deficits in the Tau-P301L Mouse Model 
    Biomedicines 9(9):1160, (2021) 
    https://pubmed.ncbi.nlm.nih.gov/34572348/  
  • Camargo LC, Schöneck M, Sangarapillai N, Honold D, Shah NJ, Langen KJ, Willbold D, Kutzsche J, Schemmert S, Willuweit A 
    PEAβ Triggers Cognitive Decline and Amyloid Burden in a Novel Mouse Model of Alzheimer's Disease 
    Int J Mol Sci. 22(13):706, (2021) 
    https://pubmed.ncbi.nlm.nih.gov/34209113/  
  • Cukkemane A, Becker N, Zielinski M, Frieg B, Lakomek NA, Heise H, SchröderGF, Willbold D, Weiergräber OH 
    Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses 
    Transl Psychiatry 11, 639 (2021) 
    https://doi.org/10.1038/s41398-021-01765-1  
  • Dubey A, Stoyanov N, Viennet T, Chhabra S, Elter S, Borggräfe J, Viegas A, Nowak RP, Burdzhiev N, Petrov O, Fischer ES, Etzkorn M, Gelev V, Arthanari H 
    Local Deuteration Enables NMR Observation of Methyl Groups in Proteins from Eukaryotic and Cell-Free Expression Systems  
    Angew. Chem. Int. Ed. 60, 13783 (2021) 
    https://doi.org/10.1002/anie.202016070  
  • Freischem S, Grimm I, López-Pérez A, Willbold D, Klenke B, Vuong C, DingleyAJ, Weiergräber OH 
    Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria 
    Biomolecules 11, 1057 (2021) 
    https://doi.org/10.3390/biom11071057  
  • Gomes CM, Hoyer W, Luo J 
    Editorial: The Biochemistry of Amyloids in Neurodegenerative Diseases, Volume I 
    Front Neurosci 15, 819481 (2021) 
    https://doi.org/10.3389/fnins.2021.819481  
  • Hasecke F, Niyangoda C, Borjas G, Pan J, Matthews G, Muschol M, Hoyer W 
    Protofibril‐fibril interactions inhibit amyloid fibril assembly by obstructing secondary nucleation 
    Angew. Chem. Int. Ed. 60, 3016-3021 (2021) 
    https://doi.org/10.1002/anie.202010098  
  • Huwa N, Weiergräber OH, Kirsch C, Schaffrath U, Classen T 
    Biochemical and Initial Structural Characterization of the Monocot Chimeric Jacalin OsJAC1 
    Int J Mol Sci 22, 5639 (2021) 
    https://doi.org/10.3390/ijms22115639  
  • Klionsky DJ, et al, Schwarten M, et al, Weiergräber OH, et al, Willbold D, et al (many co-authors) 
    Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 
    Autophagy 17, 1-382 (2021) 
    https://www.tandfonline.com/doi/full/10.1080/15548627.2020.1797280  
  • König AS, Rösener NS, Gremer L, Tusche M, Flender D, Reinartz E, Hoyer W, Neudecker P, Willbold D, Heise H 
    Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy 
    J Biol Chem 296, 100499 (2021) 
    https://doi.org/10.1016/j.jbc.2021.100499  
  • López-Pérez A, Freischem S, Grimm I, Weiergräber O, Dingley AJ, López-AlbercaMP, Waldmann H, Vollmer W, Kumar K, Vuong C 
    Discovery of Pyrrolidine-2,3-diones as Novel Inhibitors of P. aeruginosa PBP3 
    Antibiotics 10, 529 (2021) 
    https://doi.org/10.3390/antibiotics10050529  
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    Early Divergence in Misfolding Pathways of Amyloid-Beta Peptides 
    ChemPhysChem 22, 2158-2163 (2021) 
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  • Post J, Kogel V, Schaffrath A, Lohmann P, Shah NJ, Langen K-J, Willbold D, Willuweit A, Kutzsche J 
    A Novel Anti-Inflammatory d-Peptide Inhibits Disease Phenotype Progression in an ALS Mouse Model. 
    Molecules 26(6):1590, (2021) 
    https://doi.org/10.3390/molecules26061590  
  • Post J, Schaffrath A, Gering I, Hartwig S, Lehr S, Shah NJ, Langen KJ, Willbold D, Kutzsche J, Willuweit A. 
    Oral Treatment with RD2RD2 Impedes Development of Motoric Phenotype and Delays Symptom Onset in SOD1 G93A Transgenic Mice  
    Int J Mol Sci . 22(13):7066, (2021) 
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    The molecular basis of spectral tuning in blue- and red-shifted flavin-binding fluorescent proteins. 
    J Biol Chem 296, 100662 (2021) 
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    Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme 
    Biological Chemistry 402, 99-111 (2021) 
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  • Schemmert S, Camargo LC, Honold D, Gering I, Kutzsche J, Willuweit A, Willbold D 
    n Vitro and In Vivo Efficacies of the Linear and the Cyclic Version of an All-d-Enantiomeric Peptide Developed for the Treatment of Alzheimer's Disease 
    Int J Mol Sci. 22(12):6553, (2021) 
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  • Schützmann MP, Hasecke F, Bachmann S, Zielinski M, Hänsch S, Schröder GF, Zempel H, Hoyer W 
    Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting 
    Nat Commun 12, 4634 (2021) 
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    Predicting the Structure of a Viroid 
    Methods in Molecular Biology 2316, 331-371 (2021) 
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    Transformation of Seed Non-Transmissible Hop Viroids in Nicotiana benthamiana Causes Distortions in Male Gametophyte Development 
    Plants 10, 2398 (2021) 
    https://doi.org/10.3390/plants10112398  
  • Szegő EM, Boß F, Komnig D, Gärtner C, Höfs L, Shaykhalishahi H, Wördehoff MM, Saridaki T, Schulz JB, Hoyer W, Falkenburger BH 
    A β-wrapin targeting the N-terminus of α-synuclein monomers reduces fibril-induced aggregation in neurons 
    Front Neurosci 15, 696440 (2021) 
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    Combined High-Pressure and Multiquantum NMR and Molecular Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta 
    J Phys Chem Lett 12, 9933-9939 (2021) 
    https://doi.org/10.1021/acs.jpclett.1c02595  
  • Willbold D, Strodel B, Schröder GF, Hoyer W, Heise H 
    Amyloid-type protein aggregation and prion-like properties of amyloids 
    Chem Rev 121, 8285-8307 (2021) 
    https://doi.org/10.1021/acs.chemrev.1c00196  
  • Agerschou ED, Borgmann V, Wördehoff MM, Hoyer W 
    Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein 
    Chem. Sci. 11, 11331-11337 (2020) 
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  • Bernis ME and Tamgüney G 
    Bioluminescence imaging of neuroinflammation in a mouse model of Parkinson's disease 
    Methods Mol Biol 2081, 147-159 (2020) 
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  • Dobner J, Simons IM, Rufinatscha K, Hänsch S, Schwarten M, Weiergräber OH, Abdollahzadeh I, Gensch T, Bode JG, Hoffmann S, Willbold D. 
    Deficiency of GABARAP but Not Its Paralogs Causes Enhanced EGF-induced EGFR Degradation 
    Cells 9, 1296 (2020) 
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    https://www.mdpi.com/2073-4409/9/5/1296  
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    Oral absorption enhancement of the amyloid-β oligomer eliminating compound RD2 by conjugation with folic acid  
    Eur J Pharm Sci. , (2020) 
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  • Kutzsche J, Jürgens D, Willuweit A, Adermann K, Fuchs C, Simons S, Windisch M, Hümpel M, Rossberg W, Wolzt M, Willbold D. 
    Safety and Pharmacokinetics of the Orally Available Antiprionic Compound PRI-002: A Single and Multiple Ascending Dose Phase I Study 
    Alzheimers Dement (N Y) , 20;6(1):e12001 (2020) 
    https://pubmed.ncbi.nlm.nih.gov/32211506/  
  • Maity D, Kumar S, AlHussein R, Gremer L, Howarth M, Karpauskaite L, Hoyer W, Magzoubd M, Hamilton AD 
    Sub-stoichiometric inhibition of IAPP aggregation: a peptidomimetic approach to antiamyloid agents 
    RSC Chem. Biol. 1, 225-232 (2020) 
    https://doi.org/10.1039/D0CB00086H  
  • Matoušek J, Steinbachová L, Záveská Drábková L, Kocábek T, Potěšil D, Mishra KA, Honys D, Steger G 
    Elimination of Viroids from Tobacco Pollen Involves a Decrease in Propagation Rate and an Increase of the Degradation Processes 
    International Journal of Molecular Sciences 21, 3029 (2020) 
    https://doi.org/10.3390/ijms21083029  
    Special Issue "Molecular Mechanisms of Viroids and Viroid Diseases" 
  • Patricia Rodríguez-Maciá, Lisa M. Galle, Ragnar Bjornsson, Christian Lorent, Ingo Zebger, Yoshitaka Yoda, Stephen P. Cramer, Serena DeBeer, Ingrid Span and James A. Birrell 
    Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase 
    Angewandte Chemie International Edition 59, 2-11 (2020) 
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    https://onlinelibrary.wiley.com/doi/10.1002/anie.202005208  
  • Röder C, Kupreichyk T, Gremer L, Schäfer LU, Pothula KR, Ravelli RBG, Willbold D, Hoyer W, Schröder GF 
    Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils 
    Nat. Struct. Mol. Biol. 27, 660-667 (2020) 
    https://doi.org/10.1038/s41594-020-0442-4  
  • Rosenbach H, Victor J, Borggräfe J, Biehl R, Steger G, Etzkorn M, Span I. 
    Expanding crystallization tools for nucleic acid complexes using U1A protein variants 
    Journal of Structural Biology 210, 107480 (2020) 
    https://doi.org/10.1016/j.jsb.2020.107480  
  • Rosenbach H, Victor J, Etzkorn M, Steger G, Riesner D, Span I 
    Molecular Features and Metal Ions that Influence 10-23 DNAzyme Activity 
    Molecules 25, 3100 (2020) 
    https://doi.org/10.3390/molecules25133100  
    Special Issue "Advances in Catalytic DNA" 
  • Rösener NS, Gremer L, Wördehoff MM, Kupreichyk T, Etzkorn M, Neudecker P, Hoyer W 
    Clustering of human prion protein and α-synuclein oligomers requires the prion protein Nterminus 
    Commun. Biol. 3, 365 (2020) 
    https://doi.org/10.1038/s42003-020-1085-z  
  • Sanwald JL, Dobner J, Simons IM, Poschmann G, Stühler K, Üffing A, Hoffmann S, Willbold D 
    Lack of GABARAP-Type Proteins Is Accompanied by Altered Golgi Morphology and Surfaceome Composition  
    Int J Mol Sci 22(1), 85 (2020) 
    https://doi.org/10.3390/ijms22010085  
    https://www.mdpi.com/1422-0067/22/1/85  
  • Sanwald JL, Poschmann G, Stühler K, Behrends C, Hoffmanns S, Willbold D. 
    The GABARAP Co-Secretome Identified by APEX2-GABARAP Proximity Labelling of Extracellular Vesicles 
    Cells 9, 1468 (2020) 
    https://doi.org/10.3390/cells9061468  
    https://www.mdpi.com/2073-4409/9/6/1468  
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    Integrated Proteo-Transcriptomic Analyses Reveal Insights into Regulation of Pollen Development Stages and Dynamics of Cellular Response to Apple Fruit Crinkle Viroid (AFCVd)-Infection in Nicotiana tabacum 
    International Journal of Molecular Sciences 21, 8700 (2020) 
    https://doi.org/10.3390/ijms21228700  
    Special Issue "Molecular Mechanisms of Viroids and Viroid Diseases" 
  • Stadler AM, Granzin J, Cousin A, Batra-Safferling R. 
    Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin. 
    Scientific Reports 10, 10938 (2020) 
    https://doi.org/10.1038/s41598-020-67944-0  
  • Viegas A, Dollinger P, Verma N, Kubiak J, Viennet T, Seidel CAM, Gohlke H, Etzkorn M, Kovacic F, Jaeger KE 
    Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation  
    Sci Rep 10, 3578 (2020) 
    https://doi.org/10.1038/s41598-020-60093-4  
  • Viegas A, Yin DM, Borggräfe J, Viennet T, Falke M, Schmitz A, Famulok M, Etzkorn M 
    Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment 
    Structure 28, 1-9 (2020) 
    https://doi.org/10.1016/j.str.2019.11.001  
  • Abdollahzadeh I, Hendriks J, Sanwald JL, Simons IM, Hoffmann S, Weiergräber OH, Willbold D, Gensch T 
    Autophagy-Related Proteins GABARAP and LC3B Label Structures of Similar Size but Different Shape in Super-Resolution Imaging 
    Molecules 24, E1833 (2019) 
    https://doi.org/10.3390/molecules24091833  
  • Agerschou ED, Flagmeier P, Saridaki T, Galvagnion C, Komnig D, Heid L, Prasad V, Shaykhalishahi H, Willbold D, Dobson CM, Voigt A, Falkenburger B, Hoyer W, Buell AK 
    An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils 
    eLife 8, e46112 (2019) 
    https://doi.org/10.7554/eLife.46112  
  • Alvarez CE, Bovdilova A, Höppner A, Wolff CC, Saigo M, Trajtenberg F, Zhang T, Buschiazzo A, Nagel-Steger L, Drincovich MF, Lercher MJ, Maurino VG. 
    Molecular adaptations of NADP-malic enzyme for its function in C4 photosynthesis in grasses. 
    Nat Plants 5(7), 755-765 (2019) 
    https://doi.org/10.1038/s41477-019-0451-7  
    https://www.nature.com/articles/s41477-019-0451-7  
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    Pseudomonas aeruginosa esterase PA2949, a bacterial homolog of the human membrane esterase ABHD6: expression, purification and crystallization. 
    Acta Crystallography F75, 270-277 (2019) 
    https://doi.org/10.1107/S2053230X19002152  
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    Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day. 
    Plant Cell 31(10), 2525-2539 (2019) 
    https://doi.org/10.1105/tpc.19.00406  
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  • Dieter Willbold and Janine Kutzsche 
    Do We Need Anti-Prion Compounds to Treat Alzheimer’s Disease? 
    Molecules 24, 2237 (2019) 
    https://www.mdpi.com/1420-3049/24/12/2237  
  • Elfgen A, Hupert M, Bochinsky K, Tusche M, González de San Román Martin E, Gering I, Sacchi S, Pollegioni L, Huesgen PF, Hartmann R, Santiago-Schübel B, Kutzsche J, Willbold D. 
    Metabolic resistance of the D-peptide RD2 developed for direct elimination of amyloid-β oligomers 
    Sci Rep 9(1), 5715 (2019) 
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    https://www.nature.com/articles/s41598-019-41993-6  
  • Falke M, Victor J, Wördehoff MM, Peduzzo A, Zhang T, Schröder GF, Buell AK, Hoyer W, Etzkorn M 
    α-Synuclein-derived lipoparticles in the study of α-synuclein amyloid fibril formation 
    Chem Phys Lipids 220, 57-65 (2019) 
    https://doi.org/10.1016/j.chemphyslip.2019.02.009  
  • Klinker S, Stindt S, Gremer L, Bode JG, Gertzen CGW, Gohlke H, Weiergräber OH, Hoffmann S, Willbold D 
    Phosphorylated tyrosine 93 of hepatitis C virus nonstructural protein 5A is essential for interaction with host c-Src and efficient viral replication 
    J Biol Chem 294, 7388-7402 (2019) 
    https://doi.org/10.1074/jbc.RA119.007656  
  • Krichel C, Möckel C, Schillinger O, Huesgen PF, Sticht H, Strodel B, Weiergräber OH, Willbold D, Neudecker P 
    Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site 
    Sci Rep 9, 14167 (2019) 
    https://doi.org/10.1038/s41598-019-48155-8  
    https://www.nature.com/articles/s41598-019-48155-8  
  • Kukuk L, Dingley AJ, Granzin J, Nagel-Steger L, Thiagarajan-RosenkranzP, Ciupka D, Hänel K, Batra-Safferling R, Pacheco V, Stoldt M, PfefferK, Beer-Hammer S, Willbold D, Koenig BW 
    Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association 
    Scientific Reports 9, 54 (2019) 
    https://doi.org/10.1038/s41598-018-37185-3  
  • Lohmann S, Bernis ME, Babila JT, Ziemski A, Grigoletto J, Tamgüney G 
    Oral and intravenous transmission of α-synuclein prions to mice 
    Acta Neuropathol 138, 515-533 (2019) 
    https://doi.org/10.1007/s00401-019-02037-5  
  • Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM. 
    Farnesylation of human guanylate-binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. 
    FEBS J Epub ahead of print, Epub ahead of print (2019) 
    https://doi.org/10.1111/febs.15015  
    https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15015  
  • Nerius M, Doblhammer G, Tamgüney G 
    GI infections are associated with an increased risk of Parkinson’s disease 
    Gut 66, 1-2 (2019) 
    https://doi.org/10.1136/gutjnl-2019-318822  
  • Perez C, Miti T, Hasecke F, Meisl G, Hoyer W, Muschol M, Ullah G 
    Mechanism of fibril and soluble oligomer formation in amyloid β and hen egg white lysozyme proteins 
    J. Phys. Chem. B 123, 5678-5689 (2019) 
    https://doi.org/10.1021/acs.jpcb.9b02338  
  • Porta N, Zaschke-Kriesche J, Frieg J, Gopalswamy M, Zivkovic A, Etzkorn M, Stark H, Smits S, Gohlke H 
    Small-molecule inhibitors of nisin resistance protein NSR from the human pathogen Streptococcus agalactiae  
    Bioorg Med Chem 27, 115079 (2019) 
    https://doi.org/10.1016/j.bmc.2019.115079  
  • Röder C, Vettore N, Mangels LN, Gremer L, Ravelli RBG, Willbold D, Hoyer W, Buell AK, Schröder GF 
    Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy 
    Nat. Commun. 10, 3754 (2019) 
    https://doi.org/10.1038/s41467-019-11320-8  
  • Schemmert S, Schartmann E, Honold D, Zafiu C, Ziehm T, Langen KJ, Shah NJ, Kutzsche J, Willuweit A, Willbold D. 
    Deceleration of the neurodegenerative phenotype in pyroglutamate-Aβ accumulating transgenic mice by oral treatment with the Aβ oligomer eliminating compound RD2. 
    Neurobiol Dis. 124, 36-45 (2019) 
    https://www.sciencedirect.com/science/article/pii/S0969996118307320  
  • Schemmert S, Schartmann E, Zafiu C, Kass B, Hartwig S, Lehr S, Bannach O, Langen KJ, Shah NJ, Kutzsche J, Willuweit A, Willbold D. 
    Aβ Oligomer Elimination Restores Cognition in Transgenic Alzheimer's Mice with Full-blown Pathology. 
    Mol Neurobiol. 56(3):, 2211-2223 (2019) 
    https://10.1007/s12035-018-1209-3  
    https://www.ncbi.nlm.nih.gov/pubmed/30003517  
  • Schwarten M, Weiergräber OH, Petrović D, Strodel B, Willbold D 
    Structural Studies of Autophagy-Related Proteins 
    Methods Mol Biol 1880, 17-56 (2019) 
    https://link.springer.com/protocol/10.1007%2F978-1-4939-8873-0_2  
  • Simons IM, Mohrlüder J, Feederle R, Kremmer E, Zobel T, Dobner J, Bleffert N, Hoffmann S, Willbold D 
    The highly GABARAP specific rat monoclonal antibody 8H5 visualizes GABARAP in immunofluorescence imaging at endogenous levels 
    Sci Rep 9, 526 (2019) 
    https://doi.org/10.1038/s41598-018-36717-1  
  • Van Den Berge N, Ferreira N, Gram H, Mikkelsen TW, Alstrup AKO, Casadei N, Tsung-Pin P, Riess O, Nyengaard JR, Tamgüney G, Jensen PH, Borghammer P 
    Evidence for bidirectional and trans-synaptic parasympathetic and sympathetic propagation of alpha-synuclein in rats 
    Acta Neuropathol 138, 535-550 (2019) 
    https://doi.org/10.1007/s00401-019-02040-w  
  • Viennet T, Bungert-Pümke S, Elter S, Viegas A, Fahlke C, Etzkorn M 
    Reconstitution and NMR characterization of the ion-channel accessory subunit barttin in detergents and lipid-bilayer nanodiscs 
    Frontiers in Molecular Biosciences 6, 13 (2019) 
    https://doi.org/10.3389/fmolb.2019.00013  
  • Zhang T, Gering I, Kutzsche J, Nagel-Steger L, Willbold D. 
    Toward the Mode of Action of the Clinical Stage All-d-Enantiomeric Peptide RD2 on Aβ42 Aggregation. 
    ACS Chem Neurosci. 10(12), 4800-4809. (2019) 
    https://pubs.acs.org/doi/10.1021/acschemneuro.9b00458  
    https://www.ncbi.nlm.nih.gov/pubmed/31710458  
  • Zhang T, Loschwitz J, Strodel B, Nagel-Steger L, Willbold D. 
    Interference with Amyloid-β Nucleation by Transient Ligand Interaction. 
    Molecules 24(11), pii: E2129 (2019) 
    https://doi.org/10.3390/molecules24112129  
    https://www.mdpi.com/1420-3049/24/11/2129  
  • Zhang T, Nagel-Steger L, Willbold D. 
    Solution-Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies. 
    ChemistryOpen 8(7), 989-994 (2019) 
    https://doi.org/10.1002/open.201900167  
    https://onlinelibrary.wiley.com/doi/full/10.1002/open.201900167  
  • Bhatia S, Diedrich D, Frieg B, Ahlert H, Stein S, Bopp B, Lang F, Zang T, Kröger T, Ernst T, Kögler G, Krieg A, Lüdeke S, Kunkel H, Rodrigues Moita AJ, Kassack MU, Marquardt V, Opitz FV, Oldenburg M, Remke M, Babor F, Grez M, Hochhaus A, Borkhardt A, Groth G, Nagel-Steger L, Jose J, Kurz T, Gohlke H, Hansen FK, Hauer J 
    Targeting HSP90 dimerization via the C terminus is effective in imatinib-resistant CML and lacks the heat shock response. 
    Blood 132(3), 307-320 (2018) 
    https://doi.org/10.1182/blood-2017-10-810986  
    https://ashpublications.org/blood/article-lookup/doi/10.1182/blood-2017-10-810986  
  • Caruso IP, Panwalkar V, Coronado MA, Dingley AJ, Cornélio ML, Willbold D, Arni RK, Eberle RJ 
    Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y-box single-stranded DNA fragment 
    FEBS J 285, 372-390 (2018) 
    https://doi.org/10.1111/febs.14350  
  • Cavini IA, Munte CE, Erlach MB, van Groen T, Kadish I, Zhang T, Ziehm T, Nagel-Steger L, Kutzsche J, Kremer W, Willbold D, Kalbitzer HR. 
    Inhibition of amyloid Aβ aggregation by high pressures or specific d-enantiomeric peptides. 
    Chem Commun (Camb). 54(26), 3294-3297 (2018) 
    https://10.1039/c8cc01458b.  
    https://www.ncbi.nlm.nih.gov/pubmed/29537428  
  • Coronado MA, Eberle RJ, Bleffert N, Feuerstein S, Olivier DS, de Moraes FR, Willbold D, Arni RK 
    Zika virus NS2B/NS3 proteinase: A new target for an old drug - Suramin a lead compound for NS2B/NS3 proteinase inhibition. 
    Antiviral Res. 160, 118-125 (2018) 
  • Duggimpudi S, Kloetgen A, Maney SK, Münch PC, Hezaveh K, Shaykhalishahi H, Hoyer W, McHardy AC, Lang PA, Borkhardt A, Hoell JI 
    Transcriptome-wide analysis uncovers the targets of the RNA-binding protein MSI2 and effects of MSI2's RNA-binding activity on IL-6 signaling 
    J. Biol. Chem. 293, 15359-15369 (2018) 
    https://doi.org/10.1074/jbc.RA118.002243  
  • Dunkelmann T, Teichmann K, Ziehm T, Schemmert S, Frenzel D, Tusche M, Dammers C, Jürgens D, Langen KJ, Demuth HU, Shah NJ, Kutzsche J, Willuweit A, Willbold D 
    Aβ oligomer eliminating compounds interfere successfully with pEAβ (3–42) induced motor neurodegenerative phenotype in transgenic mice 
    Neuropeptides 67, 27-35 (2018) 
    https://doi.org/10.1016/j.npep.2017.11.011  
    https://www.sciencedirect.com/science/article/pii/S0143417917301531  
  • Dunkelmann T, Schemmert S, Honold D, Teichmann K, Butzküven E, Demuth HU, Shah NJ, Langen KJ, Kutzsche J, Willbold D, Willuweit A. 
    Comprehensive Characterization of the Pyroglutamate Amyloid-β Induced Motor Neurodegenerative Phenotype of TBA2.1 Mice. 
    J Alzheimers Dis. 63(1), 115-130 (2018) 
    https://10.3233/JAD-170775  
    https://www.ncbi.nlm.nih.gov/pubmed/29578479  
  • Fettweiss T, Röllen K, Granzin J, Reiners O, Endres S, Drepper T, Willbold D, Jaeger KE, Batra-Safferling R*, Krauss U* 
    Mechanistic Basis of the Fast Dark Recovery of the Short LOV Protein DsLOV from Dinoroseobacter shibae. 
    Biochemistry 57, 4833–4847 (2018) 
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  • Galle L, Cutsail III G, Nischwitz V, DeBeer S, Span I 
    Spectroscopic characterization of the Co-substituted C-terminal domain of Rubredoxin-2 
    Biological Chemistry 399, 787-798 (2018) 
    https://doi.org/10.1515/hsz-2018-0142  
    https://www.degruyter.com/view/journals/bchm/399/7/article-p787.xml  
  • Hasecke F, Miti T, Perez C, Barton J, Schölzel D, Gremer L, Grüning CSR, Matthews G, Meisl G, Knowles TPJ, Willbold D, Neudecker P, Heise H, Ullah G, Hoyer W, Muschol M 
    Origin of metastable oligomers and their effects on amyloid fibril self-assembly 
    Chem. Sci. 9, 5937-5948 (2018) 
    https://doi.org/10.1039/c8sc01479e  
  • Kulawik A,Heise H,Zafiu C,Willbold D,Bannach O. 
    Advancements of the sFIDA method for oligomer-based diagnostics of neurodegenerative diseases 
    FEBS Letters , (2018) 
    http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12983/abstract  
    CLICK  
  • Orr AA, Shaykhalishahi H, Mirecka EA, Jonnalagadda SVR, Hoyer W, Tamamis P 
    Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins 
    Comput. Chem. Eng. 116, 322-332 (2018) 
    https://doi.org/10.1016/j.compchemeng.2018.02.013  
  • Pascual-Ortiz M, Saiardi A, Walla E, Jakopec V, Künzel NA, Span I, Vangala A, Fleig U 
    Asp1 Bifunctional Activity Modulates Spindle Function via Controlling Cellular Inositol Pyrophosphate Levels in Schizosaccharomyces pombe 
    Mol. Cell. Biol. 38, e00047-18 (2018) 
    http://dx.doi.org/10.1128/MCB.00047-18  
    http://mcb.asm.org/content/38/9/e00047-18.abstract  
  • Röllen, K.; Granzin, J.; Batra-Safferling, R*.; Stadler, A.M*. 
    Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein 
    PLoS One 13(7):e0200746, (2018) 
    http://dx.doi.org/10.1371/journal.pone.0200746  
  • Rösener NS, Gremer L, Reinartz E, König A, Brener O, Heise H, Hoyer W, Neudecker P, Willbold D 
    A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein 
    J. Biol. Chem. 293, 15748-15764 (2018) 
    https://doi.org/10.1074/jbc.RA118.003116  
  • Santur K, Sevenich M, Schwarten M, Nischwitz V, Willbold D, Mohrlüder J 
    In Vitro Reconstitution of the Highly Active and Natively Folded Recombinant Human Superoxide Dismutase 1 Holoenzyme 
    ChemistrySelect 3, 7627-7632 (2018) 
    https://doi.org/10.1002/slct.201801319  
    https://onlinelibrary.wiley.com/doi/abs/10.1002/slct.201801319  
  • Schartmann E, Schemmert S, Niemietz N, Honold D, Ziehm T, Tusche M, Elfgen A, Gering I, Brener O, Shah NJ, Langen KJ, Kutzsche J, Willbold D, Willuweit A. 
    In Vitro Potency and Preclinical Pharmacokinetic Comparison of All-D-Enantiomeric Peptides Developed for the Treatment of Alzheimer's Disease. 
    J Alzheimers Dis 64(3), 859-873 (2018) 
    https://10.3233/JAD-180165  
    https://www.ncbi.nlm.nih.gov/pubmed/29966196  
  • Schulte M, Panwalkar V, Freischem S, Willbold D, Dingley, AJ 
    Proline restricts loop 1 conformation of the high affinity WW domain from human Nedd4-1 to a ligand binding-competent type 1 beta-turn 
    J Phys Chem B 122, 4219-4230 (2018) 
    https://doi.org/10.1021/acs.jpcb.7b11637  
  • Schulte M, Petrović D, Neudecker P, Hartmann R, Pietruszka J, Willbold S, Willbold D, Panwalkar V 
    Conformational sampling of the intrinsically disordered C-terminal tail of DERA is important for enzyme catalysis 
    ACS Catal 8, 3971-3984 (2018) 
    https://doi.org/10.1021/acscatal.7b04408  
  • Steger, G, Riesner, D 
    Viroid research and its significance for RNA technology and basic biochemistry. 
    Nucleic Acids Res. 46, 10563-10576 (2018) 
    http://dx.doi.org/10.1093/nar/gky903  
  • Uluca B, Viennet T, Petrovic D, Shaykhalishahi H, Weirich F, Gönülalan A, Strodel B, Etzkorn M, Hoyer W, Heise H 
    DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α-Synuclein in Different States 
    Biophys. J. 114, 1614-1623 (2018) 
    https://doi.org/10.1016/j.bpj.2018.02.011  
  • Viennet T, Wördehoff MW, Uluca B, Poojari C, Shaykhalishahi H, Willbold D, Strodel B, Heise H, Buell AK, Hoyer W, Etzkorn M: 
    Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation 
    Commun. Biol. 1, 44 (2018) 
    https://doi.org/10.1038/s42003-018-0049-z  
  • Wördehoff M, Hoyer W 
    α-Synuclein aggregation monitored by Thioflavin T fluorescence assay 
    Bio Protoc. 8, e2941 (2018) 
    https://doi.org/10.21769/BioProtoc.2941  
  • Yerabham ASK, Müller-Schiffmann A, Ziehm T, Stadler A, Köber S, Indurkhya X, Marreiros R, Trossbach SV, Bradshaw NJ, Prikulis I, Willbold D, Weiergräber OH, Korth C 
    Biophysical insights from a single chain camelid antibody directed against the disrupted in schizophrenia 1 protein 
    PLoS One 13, e0191162 (2018) 
  • Zhang T, Pauly T, Nagel-Steger L 
    Stoichiometric Zn2+ interferes with the self-association of Aβ42: Insights from size distribution analysis. 
    Int J Biol Macromol 113, 631-639 (2018) 
    https://doi.org/10.1016/j.ijbiomac.2018.02.123  
    https://www.sciencedirect.com/science/article/pii/S0141813017348365?via%3Dihub  
  • Abdollahzadeh I, Schwarten M, Gensch T, Willbold D, Weiergräber OH 
    The Atg8 Family of Proteins—Modulating Shape and Functionality of Autophagic Membranes 
    Front Genet 8, 109 (2017) 
    https://doi.org/10.3389/fgene.2017.00109  
  • Akers PW, Dingley AJ, Swift S, Nelson ARJ, Martin J, McGillivray DJ. 
    Using Neutron Reflectometry to Characterize Antimicrobial Protein Surface Coatings 
    J Phys Chem B [Epub ahead of print], (2017) 
    http://dx.doi.org/10.1021/acs.jpcb.7b02886  
    https://www.ncbi.nlm.nih.gov/pubmed/28537751  
  • Arinkin V, Granzin J, Röllen K, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R. 
    Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools 
    Scientific Reports 7(42971), (2017) 
    http://dx.doi.org/10.1038/srep42971  
  • Batra-Safferling R and Granzin J.  
    The Structure of the Polar Core Mutant R175E and Its Functional Implications.  
    The Structural Basis Of Arrestin Functions, Vsevolod V. Gurevich (Editor); Springer International Publishing Chapter 11, 143-158 (2017) 
    ISBN: 978-3-319-57552-0 
  • Boeske A, Schwarten M, Ma P, Tusche M, Mötter J, Möller C, Neudecker P, Hoffmann S, Willbold D 
    Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization 
    Scientific Reports 7, 5979 (2017) 
  • Bradshaw NJ, Yerabham ASK, Marreiros R, Zhang T, Nagel-Steger L, Korth C 
    An unpredicted aggregation-critical region of the actin-polymerizing protein TRIOBP-1/Tara, determined by elucidation of its domain structure 
    J Biol Chem 292, 9583-9598 (2017) 
    http://dx.doi.org/10.1074/jbc.M116.767939  
  • Brass JRJ, Owens RA, Matoušek J, Steger G 
    Viroid quasispecies revealed by deep sequencing 
    RNA Biology 14, 317-325 (2017) 
    http://dx.doi.org/10.1080/15476286.2016.1272745  
  • Caruso IP, Panwalkar V, Coronado MA, Dingley AJ, Cornélio ML, Willbold D, Arni RK, Eberle RJ. 
    NMR studies of cold shock protein A from Corynebacterium pseudotuberculosis: structure and interaction with Y-box single-stranded DNA fragment. 
    FEBS J. 285, 372-390 (2017) 
  • Dammers C, Reiss K, Gremer L, Lecher J, Ziehm T, Stoldt M, Schwarten M, Willbold D.  
    Pyroglutamate-modified amyloid-β(3-42) shows α-helical intermediates before amyloid formation. 
    Biophys. J. 112, 1621-1633 (2017) 
  • Dammers C, Schwarten M, Buell AK, Willbold D 
    Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways 
    Chem. Sci. 8, 4996-5004 (2017) 
    http://pubs.rsc.org/en/content/articlehtml/2017/sc/c6sc04797a  
  • Elfgen A, Santiago-Schübel B, Gremer L, Kutzsche J, Willbold, D 
    Surprisingly high stability of the Aβ oligomer eliminating all-D-enantiomeric peptide D3 in media simulating the route of orally administered drugs 
    European Journal of Pharmaceutical Sciences 107, 203-207 (2017) 
    https://doi.org/10.1016/j.ejps.2017.07.015  
    https://www.ncbi.nlm.nih.gov/pubmed/28711713  
  • Gremer L, Schölzel D, Schenk C, Reinartz E, Labahn J, Ravelli RB, Tusche M, Lopez-Iglesias C, Hoyer W, Heise H, Willbold D, Schröder GF 
    Fibril structure of amyloid-ß(1-42) by cryoelectron microscopy 
    Science 358, 116-119 (2017) 
    http://dx.doi.org/10.1126/science.aao2825  
    http://science.sciencemag.org/content/early/2017/09/06/science.aao2825  
  • Gushchin I, Melnikov I, Polovinkin V, Ishchenko A, Yuzhakova A, Buslaev P, Bourenkov G, Grudinin S, Round E, Balandin T, Borshchevskiy V, Willbold D, Leonard G, Büldt G, Popov A, Gordeliy V. 
    Mechanism of transmembrane signaling by sensor histidine kinases. 
    Science 356, eaah6345 (2017) 
  • Herrmann Y, Bujnicki T, Zafiu C, Kulawik A, Kühbach K, Peters L, Fabig J, Willbold J, Bannach O, Willbold D. 
    Nanoparticle standards for immuno-based quantitation of α-synuclein oligomers in diagnostics of Parkinson's disease and other synucleinopathies. 
    Clin Chim Acta 466, 152–159 (2017) 
    http://dx.doi.org/10.1016/j.cca.2017.01.010  
    http://www.sciencedirect.com/science/article/pii/S0009898117300104  
  • Herrmann Y, Kulawik A, Kühbach K, Hülsemann M, Peters L, Bujnicki T, Kravchenko K, Linnartz C, Willbold J, Zafiu C, Bannach O, Willbold D. 
    sFIDA automation yields sub-femtomolar limit of detection for Aβ aggregates in body liquids. 
    Clinical Biochem. 50(4-5), 244-247 (2017) 
    http://dx.doi.org/10.1016/j.clinbiochem.2016.11.001  
    http://www.sciencedirect.com/science/article/pii/S0009912016305008  
  • Hupert M, Elfgen A, Schartmann E, Schemmert S, Buscher B, Kutzsche J, Willbold D, Santiago-Schübel B 
    Development and Validation of an UHPLC-ESI-QTOF-MS method for quantification of the highly hydrophilic amyloid-β oligomer eliminating all-D-enantiomeric peptide RD2 in mouse plasma 
    Journal of Chromatography B 1073, 123-129 (2017) 
    https://doi.org/10.1016/j.jchromb.2017.12.009  
    https://www.sciencedirect.com/science/article/pii/S1570023217316562  
  • Klein AN, Ziehm T, van Groen T, Kadish I, Elfgen A, Tusche M, Thomaier M, Reiss K, Brener O, Gremer L, Kutzsche J, Willbold D 
    Optimization of D-peptides for Aβ monomer binding specificity enhances their potential to eliminate toxic Aβ oligomers 
    ACS Chem Neurosci 8, 1889-1900 (2017) 
  • Kravchenko K, Kulawik A, Hülsemann M, Kühbach K, Zafiu C, Herrmann Y, Linnartz C, Peters L, Bujnicki T, Willbold J, Bannach O, Willbold D.  
    Analysis of anticoagulants for blood-based quantitation of amyloid β oligomers in the sFIDA assay. 
    Biol. Chem. 398(4), 465-475 (2017) 
    https://dx.doi.org/10.1515/hsz-2016-0153  
    https://www.degruyter.com/view/j/bchm.ahead-of-print/hsz-2016-0153/hsz-2016-0153.xml  
  • Kroeger T, Frieg B, Zhang T, Hansen FK, Marmann A, Proksch P, Nagel-Steger L, Groth G, Smits SHJ, Gohlke H 
    EDTA aggregates induce SYPRO orange-based fluorescence in thermal shift assay 
    PLoS One 12, e0177024 (2017) 
    http://dx.doi.org/10.1371/journal.pone.0177024  
  • Kühbach K, Hülsemann M, Herrmann Y, Kravchenko K, Kulawik A, Linnartz C, Peters L, Wang K, Willbold J, Willbold D, Bannach O.  
    Application of an amyloid beta oligomer standard in the sFIDA assay. 
    In: Biomarkers of Alzheimer's Disease: The Present and the Future. Eds. Sylvain Lehmann, Charlotte Elisabeth Teunissen. , 39-44 (2017) 
    ISBN 9782889450411  
  • Kutzsche J, Schemmert S, Tusche M, Neddens J, Rabl R, Jürgens D, Brener O, Willuweit A, Hutter-Paier B, Willbold D. 
    Large-Scale Oral Treatment Study with the Four Most Promising D3-Derivatives for the Treatment of Alzheimer's Disease. 
    Molecules 22(10), (2017) 
    http://10.3390/molecules22101693  
    https://www.ncbi.nlm.nih.gov/pubmed/28994710  
  • Matoušek J, Siglová K, Jakše J, Radišek S, Brass JR, Tsushima T, Guček T, Duraisamy GS, Sano T, Steger G 
    Propagation and some physiological effects of Citrus bark cracking viroid and Apple fruit crinkle viroid in multiple infected hop (Humulus lupulus L.) 
    J. Plant Physiol. 213, 166-177 (2017) 
    http://dx.doi.org/10.1016/j.jplph.2017.02.014  
  • Nikolaev M, Round E, Gushchin I, Polovinkin V, Balandin T, Kuzmichev P, Shevchenko V, Borshchevskiy V, Kuklin A, Round A, Bernhard F, Willbold D, Büldt G, Gordeliy V.  
    Integral membrane proteins can be crystallized directly from nanodiscs. 
    Cryst. Growth Des. 17, 945-948 (2017) 
  • Panwalkar V, Neudecker P, Willbold D, Dingley AJ. 
    Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding. 
    FEBS Lett. 591(11), 1573-1583 (2017) 
    http://dx.doi.org/10.1002/1873-3468.12664  
    https://www.ncbi.nlm.nih.gov/pubmed/28471472  
  • Ricardo Gaspar, Georg Meisl, Alexander K Buell, Laurence Young, Clemens F Kaminski, Tuomas PJ Knowles, Emma Sparr, Sara Linse 
    Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification 
    Quarterly Reviews in Biophysics 50, (2017) 
    https://doi.org/10.1017/S0033583516000172  
    https://www.cambridge.org/core/journals/quarterly-reviews-of-biophysics/article/div-classtitlesecondary-nucleation-of-monomers-on-fibril-surface-dominates-span-classitalicspan-synuclein-aggregation-and-provides-autocatalytic-amyloid-amplificationdiv/36C95  
  • Ricardo Gaspar, Georg Meisl, Alexander K. Buell, Laurie Young, Clemens F. Kaminski, Tuomas P. J.Knowles, Emma Sparr and Sara Linse 
    Secondary nucleation of monomers on fibril surface dominates α- synuclein aggregation and provides autocatalytic amyloid amplification 
    Quart Rev Biophys 50, e6, 1-12 (2017) 
    https://doi.org/10.1017/S0033583516000172  
  • Schartmann E, Schemmert S, Ziehm T, Leithold LHE, Jiang N, Tusche M, Shah NJ, Langen KJ, Kutzsche J, Willbold D, Willuweit A. 
    Comparison of blood-brain barrier penetration efficiencies between linear and cyclic all-d-enantiomeric peptides developed for the treatment of Alzheimer's disease. 
    Eur J Pharm Sci. 17, 0928-0987 (2017) 
    https://doi.org/10.1016/j.ejps.2017.12.005  
    https://www.ncbi.nlm.nih.gov/pubmed/29225107  
  • Schlesinger R, Cousin A, Granzin J, Batra-Safferling R.  
    Expression and purification of arrestin in yeast Saccharomyces cerevisiae. 
    Methods Cell Biol 142, 159-172 (2017) 
    https://doi.org/10.1016/bs.mcb.2017.07.003  
  • Steger G 
    Modelling the three-dimensional structure of the right-terminal domain of pospiviroids. 
    Sci. Rep. 7, 711 (2017) 
    http://dx.doi.org/10.1038/s41598-017-00764-x  
  • Steger G, Riesner D, Maurel M-C, Perreault J-P 
    Viroid structure 
    In Viroids and Satellites; Hadidi A, Flores, R, Randles JW, Palukaitis P (eds), Oxford: Academic Press , 63-70 (2017) 
    https://www.elsevier.com/books/viroids-and-satellites/hadidi/978-0-12-801498-1  
  • van Groen T, Schemmert S, Brener O, Gremer L, Ziehm T, Tusche M, Nagel-Steger L, Kadish I, Schartmann E, Elfgen A, Jürgens D, Willuweit A, Kutzsche J, Willbold D. 
    The Aβ oligomer eliminating D-enantiomeric peptide RD2 improves cognition without changing plaque pathology. 
    Sci Rep. 7, 16275 (2017) 
    https://doi.org/10.1038/s41598-017-16565-1  
    https://www.nature.com/articles/s41598-017-16565-1  
  • Vasudevan JAA, Hofmann H, Willbold D, Häussinger D, Koenig BW, Münk C. 
    Enhancing the catalytic deamination activity of APOBEC3C is insufficient to inhibit Vif-deficient HIV-1. 
    J. Mol. Biol. 429, 1171-1191 (2017) 
  • Victor J, Steger G, Riesner D 
    Inability of DNAzymes to cleave RNA in vivo is due to limited Mg2+ concentration in cells 
    Eur Biophys J 47, 333-343 (2017) 
    https://doi.org/10.1007/s00249-017-1270-2  
  • Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Büldt G, Bamberg E, Gordeliy V 
    Structural insights into ion conduction by channelrhodopsin 2 
    Science 358, eaan8862, (2017) 
  • Weiergräber OH, Schwarten M, Strodel B, Willbold D.  
    Investigating Structure and Dynamics of Atg8 Family Proteins. 
    Methods Enzymol 587, 115-142 (2017) 
  • Wolff M, Zhang-Haagen B, Decker C, Barz B, Schneider M, Biehl R, Radulescu A, Strodel B, Willbold D, Nagel-Steger L 
    Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution 
    Sci Rep 7, 2493 (2017) 
    http://dx.doi.org/10.1038/s41598-017-02370-3  
  • Wördehoff M, Shaykhalishahi H, Groß L, Gremer L, Stoldt M, Buell AK, Willbold D, Hoyer W 
    Opposed effects of dityrosine formation in soluble and aggregated α-synuclein on fibril growth 
    J. Mol. Biol. 429, 3018-3030 (2017) 
    https://doi.org/10.1016/j.jmb.2017.09.005  
    http://www.sciencedirect.com/science/article/pii/S0022283617304278  
  • Yerabham ASK, Mas PJ, Decker C, Soares DC, Weiergräber OH, Nagel-Steger L, Willbold D, Hart DJ, Bradshaw NJ, Korth C. 
    A structural organization for Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions which are bisected by mental illness related mutations.  
    J Biol Chem 292, 6468-6477 (2017) 
    http://dx.doi.org/10.1074/jbc.M116.773903  
  • Alexander K. Buell 
    The nucleation of protein aggregates – from crystals to fibrils 
    International Review of Cell and Molecular Biology , (2016) 
    http://dx.doi.org/10.1016/bs.ircmb.2016.08.014  
  • Anđela Šarić, Alexander K. Buell, Georg Meisl, Thomas C. T. Michaels, Sara Linse, Tuomas P. J. Knowles and Daan Frenkel 
    Physical determinants for the self-replication of protein fibrils 
    Nature Physics 12, 874-880 (2016) 
    http://www.nature.com/nphys/journal/v12/n9/full/nphys3828.html  
  • Barz B and Strodel B 
    Understanding Amyloid-β oligomerization at the molecular level: the role of the fibril surface. 
    Chem. Eur. J. 22, 8768-8772 (2016) 
  • Bronder AM, Bieker A, Elter S, Etzkorn M, Haeussinger D, Oesterhelt F 
    Oriented membrane protein reconstitution into tethered lipid membranes for AFM Force Spectroscopy 
    Biophys. J. 111, 1925-1934 (2016) 
    http://dx.doi.org/10.1016/j.bpj.2016.08.051  
  • Carballo-Pacheco M and Strodel B 
    Advances in the Simulation of Protein Aggregation at the Atomistic Scale 
    J. Phys. Chem. B 120, 2991–2999 (2016) 
  • Céline Galvagnion, James Brown, Myriam M. Ouberai, Patrick Flagmeier, Michele Vendruscolo, Alexander K. Buell, Emma Sparr and Christopher M. Dobson 
    The chemical properties of lipids strongly affect the rate of the nucleation step in the membrane-induced aggregation of α-synuclein 
    PNAS 113(26), 7065-7070 (2016) 
    http://www.pnas.org/content/113/26/7065  
  • Dammers C, Yolcu D, Kukuk L, Willbold D, Pickhardt M, Mandelkow E, Horn AH, Sticht H, Malhis MN, Will N, Schuster J, Funke SA. 
    Selection and characterization of Tau binding D-enantiomeric peptides with potential for therapy of Alzheimer disease 
    PLoS One 11, e0167432 , (2016) 
    http://dx.doi.org/10.1371/journal.pone.0167432  
  • Della Corte D, Wildberg A, Schröder GF 
    Protein Structure Refinement with Adaptively Restrained Homologous Replicas  
    Proteins , (2016) 
    https://doi.org/10.1002/prot.24939  
  • Dick M, Hartmann R, Weiergräber OH, Bisterfeld C, Classen T, Schwarten M, Neudecker P, Willbold D, Pietruszka J. 
    Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies. 
    Chem. Sci. 7, 4492-4502 (2016) 
  • Donner L, Fälker K, Gremer L, Klinker S, Pagani G, Ljungberg LU, Lothmann K,Rizzi F, Schaller M, Gohlke H, Willbold D, Grenegard M, Elvers M. 
    Platelets contribute to amyloid-β aggregation in cerebral vessels through integrin αIIbβ3-induced outside-in signaling and clusterin release 
    Sci Signal 9(429), ra52 (2016) 
    http://10.1126/scisignal.aaf6240  
    http://stke.sciencemag.org/content/9/429/ra52.long  
  • Dorothea Pinotsi, Claire H. Michel, Alexander K. Buell, Christopher M. Dobson, Clemens F. Kaminski, Gabriele S. Kaminski Schierle 
    Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons 
    PNAS 113(14), 3815-3819 (2016) 
    http://www.pnas.org/content/113/14/3815  
  • Giulio Costantini, Zoe Budrikis, Alessandro Taloni, Alexander K. Buell, Stefano Zapperi and Caterina A.M. La Porta 
    Fluctuations in protein aggregation: Design of preclinical screening for early diagnosis of neurodegenerative disease 
    Phys Rev Appl 6, 034012 (2016) 
    http://journals.aps.org/prapplied/abstract/10.1103/PhysRevApplied.6.034012  
  • Hülsemann M, Zafiu C, Kühbach K, Lühmann N, Herrmann Y, Peters L, Linnartz C, Willbold J, Kravchenko K, Kulawik A, Willbold S, Bannach O, Willbold D.  
    Biofunctionalized Silica Nanoparticles: Standards in Amyloid-β Oligomer-Based Diagnosis of Alzheimer's Disease. 
    J. Alzheimers Dis. 54, 79-88 (2016) 
    https://dx.doi.org/10.3233/JAD-160253  
    http://content.iospress.com/articles/journal-of-alzheimers-disease/jad160253  
  • James Brown, Alexander K. Buell, Thomas C.T. Michaels, Georg Meisl, Jackie Carozza, Patrick Flagmeier, Michele Vendruscolo, Tuomas P.J. Knowles, Christopher M. Dobson, Céline Galvagnion 
    β-synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding 
    Scientific Reports 6, 36010 (2016) 
    http://www.nature.com/articles/srep36010  
  • Jiang N, Frenzel D, Schartmann E, van Groen T, Kadish I, Shah NJ, Langen KJ, Willbold D, Willuweit A. 
    Blood-brain barrier penetration of an Aβ-targeted, arginine-rich, D-enantiomeric peptide 
    BBA Biomembranes 1858, 2717-2724 (2016) 
  • Klein AN, Ziehm T, Tusche M, Buitenhuis J, Bartnik D, Boeddrich A, Wiglenda T, Wanker E, Funke SA, Brener O, Gremer L, Kutzsche J, Willbold D. 
    Optimization of the All-D Peptide D3 for Aβ Oligomer Elimination. 
    PLoS One 11(4), (2016) 
    http://dx.doi.org/10.1371/journal.pone.0153035  
    Erratum in: PLoS One. 2016;11(7):e0158960. http://dx.doi.org/10.1371/journal.pone.0158960 
  • Klionsky DJ, et al, Schwarten M, et al, Willbold D, et al (many co-authors) 
    Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). 
    Autophagy 12, 1-222 (2016) 
    http://www.tandfonline.com/doi/full/10.1080/15548627.2015.1100356  
  • Koch K, Hartmann R, Schröter F, Suwala AK, Maciaczyk D, Krüger AC, Willbold D, Kahlert UD, Maciaczyk J.  
    Reciprocal regulation of the cholinic phenotype and epithelial-mesenchymal transition in glioblastoma cells.  
    Oncotarget , (2016) 
  • Kovacic F, Bleffert F, Caliskan M, Wilhelm S, Granzin J, Batra-Safferling R, Jaeger KE. 
    A membrane-bound esterase PA2949 from Pseudomonas aeruginosa is expressed and purified from Escherichia coli. 
    FEBS Open Bio. Apr 19;6(5), 484-93 (2016) 
    http://dx.doi.org/10.1002/2211-5463.12061  
    http://www.ncbi.nlm.nih.gov/pubmed/27419054  
  • Kovacic F, Mandrysch A, Poojari C, Strodel B, Jaeger KE 
    Structural features determining thermal adaptation of esterases 
    Protein Eng. Des. Sel. 29, 65-76 (2016) 
  • Krichel C, Weiergräber OH, Pavlidou M, Mohrlüder J, Schwarten M, Willbold D, Neudecker P 
    Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C 
    Biomol NMR Assign 10, 41-43 (2016) 
  • Kühbach K, Hülsemann M, Herrmann Y, Kravchenko K, Kulawik A, Linnartz C, Peters L, Wang K, Willbold J, Willbold D, Bannach O. 
    Application of an Amyloid Beta Oligomer Standard in the sFIDA Assay 
    Front. Neurosci. 10:8, (2016) 
    http://dx.doi.org/10.3389/fnins.2016.00008  
    http://journal.frontiersin.org/article/10.3389/fnins.2016.00008  
  • Kynast P, Derreumaux P and Strodel B 
    Evaluation of the coarse-grained OPEP force field for protein-protein docking 
    BMC Biophysics 9, 4 (2016) 
  • Leithold LH, Jiang N, Post J, Niemietz N, Schartmann E, Ziehm T, Kutzsche J, Shah NJ, Breitkreutz J, Langen KJ, Willuweit A, Willbold D.  
    Pharmacokinetic properties of tandem D-peptides designed for treatment of Alzheimer's disease 
    Eur. J. Pharm. Sci. 89, 31-38 (2016) 
    http://dx.doi.org/10.1016/j.ejps.2016.04.016  
  • Leithold LH, Jiang N, Post J, Ziehm T, Schartmann E, Kutzsche J, Shah NJ, Breitkreutz J, Langen KJ, Willuweit A, Willbold D. 
    Pharmacokinetic Properties of a Novel D-Peptide Developed to be Therapeutically Active Against Toxic β-Amyloid Oligomers 
    Pharm Res. 33, 328-336 (2016) 
  • Luczak SE, Smits SH, Decker C, Nagel-Steger L, Schmitt L, Hegemann JH 
    The Chlamydia pneumoniae Adhesin Pmp21 Forms Oligomers with Adhesive Properties. 
    J Biol Chem 291(43), 22806-22818 (2016) 
    http://doi.10.1074/jbc.M116.728915  
    http://www.jbc.org/content/291/43/22806  
  • Lühmann N, Niu A, Allgaier J, Stellbrink J, Zorn R, Linnolahti M, Willbold S, Koenig BW, Grillo I, Richter D, Fetters LJ. 
    The initiation mechanism of butadiene polymerization in aliphatic hydrocarbons: A full mechanistic approach.  
    Macromolecules 49, 5397-5406 (2016) 
    http://doi.org/10.1021/acs.macromol.6b01115  
  • Manuel Wolff, Judith J. Mittag, Therese W. Herling, Erwin De Genst, Christopher M. Dobson, Tuomas P.J. Knowles, Dieter Braun and Alexander K. Buell 
    Quantitative thermophoretic study of disease-related protein aggregates 
    Scientific Reports 6, 22829 (2016) 
    http://www.nature.com/articles/srep22829  
  • Mirecka EA, Feuerstein S, Gremer L, Schröder GF, Stoldt M, Willbold D, Hoyer W. 
    β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor 
    Sci. Rep. 6, 33474 (2016) 
    https://dx.doi.org/10.1038/srep33474  
    http://www.nature.com/articles/srep33474  
  • Nagel-Steger L, Owen MC, and Strodel B 
    An account of amyloid oligomers: facts and figures obtained from experiments and simulations 
    ChemBioChem 17, 657-676 (2016) 
    http://dx.doi.org/10.1002/cbic.201500623  
  • Nouri K, Fansa EK, Amin E, Dvorsky R, Gremer L, Willbold D, Schmitt L, Timson DJ, Ahmadian MR. 
    IQGAP1 interaction with RHO family proteins revisited: Kinetic and equilibrium evidence for multiple distinct binding sites 
    J Biol Chem , (2016) 
    http://10.1074/jbc.M116.752121  
    http://www.jbc.org/content/early/2016/11/04/jbc.M116.752121.abstract  
    [Epub ahead of print] 
  • Orr AA, Wördehoff MM, Hoyer W, Tamamis P 
    Uncovering the binding and specificity of β-wrapins for amyloid-β and α-synuclein 
    J. Phys. Chem. B 120, 12781-12794 (2016) 
    https://dx.doi.org/10.1021/acs.jpcb.6b08485  
  • Owen MC, Strodel B, Csizmadia IG & Viskolcz B 
    Radical Formation Initiates Solvent-Dependent Unfolding and β-Sheet Formation in a Model Helical Peptide 
    J. Phys. Chem. B 120, 4878-4889 (2016) 
  • Panwalkar V, Neudecker P, Schmitz M, Lecher J, Schulte M, Medini K, Stoldt M, Brimble MA, Willbold D, Dingley AJ. 
    The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria 
    Biochemistry 55, 659-674 (2016) 
    http://pubs.acs.org/doi/full/10.1021/acs.biochem.5b01028  
  • Panwalkar V, Schulte M, Lecher J, Stoldt M, Willbold D, Dingley AJ 
    Data describing the solution structure of the WW3* domain from human Nedd4-1 
    Data Brief 22;8, 605-12 (2016) 
    http://dx.doi.org/10.1016/j.dib.2016.06.024  
    https://www.ncbi.nlm.nih.gov/pubmed/27419198  
  • Patrick Flagmeier, Georg Meisl, Michele Vendruscolo, Tuomas PJ Knowles, Christopher M. Dobson, Alexander K. Buell and Céline Galvagnion 
    Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein amyloid formation 
    PNAS 113(37), 10328-10333 (2016) 
    http://www.pnas.org/content/113/37/10328  
  • Pattky M, Barkovits K, Marcus K, Weiergräber OH, Huhn C 
    Statically Adsorbed Coatings for High Separation Efficiency and Resolution in CE-MS Peptide Analysis: Strategies and Implementation 
    Methods Mol Biol 1483, 53-75 (2016) 
    https://doi.org/10.1007/978-1-4939-6403-1_4  
  • Röllen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R. 
    Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy. 
    J Mol Biol. 428, 3721 - 3736 (2016) 
    http://dx.doi.org/10.1016/j.jmb.2016.05.027  
    http://www.ncbi.nlm.nih.gov/pubmed/27291287  
  • Rudolph S, Klein AN, Tusche M, Schlosser C, Elfgen A, Brener O, Teunissen C,Gremer L, Funke SA, Kutzsche J, Willbold D. 
    Correction: Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity 
    PLoS One 11(7), (2016) 
    http://dx.doi.org/10.1371/journal.pone.0159470  
    http://journals.plos.org/plosone/article?id=info:doi/10.1371/journal.pone.0159470  
  • Rudolph S, Klein AN, Tusche M, Schlosser C, Elfgen A, Brener O, Teunissen C, Gremer L, Funke SA, Kutzsche J, Willbold D.  
    Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and Toxicity. 
    PLoS One 11(2):e0147470., (2016) 
    http://dx.doi.org/10.1371/journal.pone.0147470  
    http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0147470  
  • Steger G, Perreault JP 
    Structure and associated biological functions of viroids 
    Adv. Virus Res. 94, 141-172 (2016) 
    http://dx.doi.org/10.1016/bs.aivir.2015.11.002  
  • Streich C, Akkari L, Decker C, Bormann J, Rehbock C, Müller-Schiffmann A, Niemeyer FC, Nagel-Steger L, Willbold D, Sacca B, Korth C, Schrader T, Barcikowski S.  
    Characterizing the Effect of Multivalent Conjugates Composed of Aβ-Specific Ligands and Metal Nanoparticles on Neurotoxic Fibrillar Aggregation. 
    ACS Nano 10, 7582-7597 (2016) 
    http://dx.doi.org10.1021/acsnano.6b02627  
  • Thakur HC, Singh M, Nagel-Steger L, Kremer J, Prumbaum D, Fansa EK, EzzahoiniH, Nouri K, Gremer L, Abts A, Schmitt L, Raunser S, Ahmadian MR, Piekorz RP 
    The centrosomal adaptor TACC3 and the microtubule polymerase chTOG interact via defined C-terminal subdomains in an Aurora-A kinase-independent manner 
    J Biol Chem 289(1), 74-88 (2016) 
    http://dx.doi.org/10.1074/jbc.M113.532333  
    http://www.jbc.org/content/289/1/74.long  
  • Thomaier M, Gremer L, Dammers C, Fabig J, Neudecker P, Willbold D. 
    High-Affinity Binding of Monomeric but Not Oligomeric Amyloid-β to Ganglioside GM1 Containing Nanodiscs 
    Biochemistry , (2016) 
    http://dx.doi.org/10.1021/acs.biochem.6b00829  
    http://pubs.acs.org/doi/ipdf/10.1021/acs.biochem.6b00829  
  • Thomas O. Mason, Thomas C.T. Michaels, Aviad Levin, Ehud Gazit, Christopher M. Dobson, Alexander K. Buell and Tuomas P. J. Knowles 
    Synthesis of non-equilibrium supra-molecular peptide polymers on a microfluidic platform 
    JACS 138(30), 9589-9596 (2016) 
    http://pubs.acs.org/doi/abs/10.1021/jacs.6b04136  
  • Týcová A, Piernikarczyk RJJ, Kugler M, Lipovová P, Podzimek T, Steger G, Matoušek J 
    A 5'P degradation hot spot influences molecular farming of anticancerogenic nuclease TBN1 in tobacco cells. 
    Plant Cell Tiss Organ Cult 127, 347-358 (2016) 
    http://dx.doi.org/10.1007/s11240-016-1054-x  
  • Viegas A, Viennet T, Etzkorn M 
    The power, pitfalls and potential of the nanodisc system for NMR-based studies  
    Biol. Chem. 397, 1335–1354 (2016) 
    https://doi.org/10.1515/hsz-2016-0224  
  • Viegas A, Viennet T, Yu TY, Schumann F, Bermel W, Wagner G, Etzkorn M 
    UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection. 
    J. Biomol. NMR 64, 9-15 (2016) 
    http://dx.doi.org/10.1007/s10858-015-0008-7  
  • Viennet T, Viegas A, Kuepper A, Arens S, Gelev V, Petrov O, Grossmann TN, Heise H, Etzkorn M 
    Selective Protein Hyperpolarization in Cell Lysates Using Targeted Dynamic Nuclear Polarization 
    Angew. Chem. Int. Ed. 55, 10746–10750 (2016) 
    http://dx.doi.org/10.1002/anie.201603205  
    (selected as inside cover article)  
  • Wallin C, Kulkarni YS, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams JP, Sholts SB, Roos PM, Kamerlin SCL, Gräslund A, Wärmländer SKTS 
    Characterization of Mn(II) ion Binding to the Amyloid-β Peptide in Alzheimer’s Disease 
    J Trace Elem Med Biol , (2016) 
    http://www.sciencedirect.com/science/article/pii/S0946672X1630030X  
  • Wang W, Ma P, Dong H, Krause HJ, Zhang Y, Willbold D, Offenhaeusser A, Gu Z A. 
    A magnetic nanoparticles relaxation sensor for protein-protein interaction detection at ultra-low magnetic field.  
    Biosens. Bioelectron. 80, 661-665 (2016) 
    http://dx.doi.org/10.1016/j.bios.2016.02.037  
  • Weirich F, Gremer L, Mirecka EA, Schiefer S, Hoyer W, Heise H 
    Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core 
    PLOS One 11, e0161243 (2016) 
    http://dx.doi.org/10.1371/journal.pone.0161243  
  • Yingbo Zhang, Alexander K. Buell, Thomas Müller, Erwin De Genst, Justin Benesch, Christopher M. Dobson and Tuomas P. J. Knowles 
    Protein aggregate-ligand binding assays based on microfluidic diffusional separation 
    ChemBioChem 17(20), 1920-1924 (2016) 
    http://onlinelibrary.wiley.com/doi/10.1002/cbic.201600384/abstract  
  • Zhang SC, Gremer L, Heise H, Janning P, Shymanets A, Cirstea IC, Krause E,Nürnberg B, Ahmadian MR 
    Liposome reconstitution and modulation of recombinant prenylated human Rac1 by GEFs, GDI1 and Pak1 
    PLoS One 9(7), (2016) 
    http://dx.doi.org/10.1371/journal.pone.0102425  
    http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0102425  
  • Zhang-Haagen B, Biehl R, Nagel-Steger L, Radulescu A, Richter D, Willbold D. 
    Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering. 
    PLoS One 11(2), e0150267 (2016) 
    http://dx.doi.org/10.1371/journal.pone.0150267  
  • Zhu J, Bailly A, Zwiewka M, Sovero V, Di Donato M, Ge P, Oehri J, Aryal B, Hao P, Linnert M, Burgardt NI, Lücke C, Weiwad M, Michel M, Weiergräber OH, Pollmann S, Azzarello E, Mancuso S, Ferro N, Fukao Y, Hoffmann C, Wedlich-Söldner R, Friml J, Thomas C, Geisler M 
    TWISTED DWARF1 Mediates the Action of Auxin Transport Inhibitors on Actin Cytoskeleton Dynamics 
    Plant Cell 28, 930-948 (2016) 
    https://doi.org/10.1105/tpc.15.00726  
  • Ziehm T, Brener O, van Groen T, Kadish I, Frenzel D, Tusche M, Kutzsche J, Reiß K, Gremer L, Nagel-Steger L, Willbold D. 
    Increase of Positive Net Charge and Conformational Rigidity Enhances the Efficacy of d-Enantiomeric Peptides Designed to Eliminate Cytotoxic Aβ Species. 
    ACS Chem Neurosci. 7 (8), 1088–1096 (2016) 
    http://pubs.acs.org/doi/abs/10.1021/acschemneuro.6b00047  
  • Börger C, Schünke S, Lecher J, Stoldt M, Winkhaus F, Kaupp UB, Willbold D 
    Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2 
    Biomol. NMR Assign. 9, 243-246 (2015) 
  • Braun T, Orlova A, Valegard K, Lindas AC, Schröder GF, Egelman EH 
    An Archaeal Actin from a Hyperthermophile Forms a Single-Stranded Filament 
    PNAS 112(30), 9340-9345 (2015) 
  • Brener O, Dunkelmann T, Gremer L, van Groen T, Mirecka EA, Kadish I, Willuweit A, Kutzsche J, Jürgens D, Rudolph S, Tusche M, Bongen P, Pietruszka J, Oesterhelt F, Langen K-J, Demuth H-U, Janssen A, Hoyer W, Funke SA, Nagel-Steger L, Willbold D 
    QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers. 
    Sci Rep 5, 13222 (2015) 
    http://dx.doi.org/10.1038/srep13222  
  • Dammers C, Gremer L, Neudecker P, Demuth HU, Schwarten M, Willbold D 
    Purification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-β Variants and Structural Analysis by Solution NMR Spectroscopy 
    PLoS One 10, e0139710 (2015) 
  • Dammers C, Gremer L, Reiß K, Klein AN, Neudecker P, Hartmann R, Sun N, Demuth HU, Schwarten M, Willbold D 
    Structural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous Trifluoroethanol  
    PLoS One 10, e0143647 (2015) 
  • Endres S, Granzin J, Circolone F, Stadler A, Krauss U, Drepper T, Svensson V, Knieps-Grünhagen E, Wirtz A, Cousin A, Tielen P, Willbold D, Jaeger K-E, Batra-Safferling R 
    Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae. 
    BMC Microbiology 15, 30 (2015) 
    http://www.biomedcentral.com/1471-2180/15/30  
  • Galkin VE, Orlova A, Vos MR, Schröder GF, Egelman EH 
    Near-Atomic Resolution for One State of F-Actin 
    Structure 23(1), 173-182 (2015) 
  • Goossens K, Prior M, Pacheco V, Willbold D, Müllen K, Enderlein J, Hofkens J, Gregor I 
    Accurate diffusion coefficients of organosoluble reference dyes in organic media measured by dual-focus fluorescence correlation spectroscopy. 
    ACS Nano 9, 7360-7373 (2015) 
  • Granzin J, Stadler A, Cousin A, Schlesinger R, Batra-Safferling R 
    Structural evidence for the role of polar core residue Arg175 in arrestin activation. 
    Scientific Reports 5, 15808 (2015) 
    http://dx.doi.org/10.1038/srep15808.  
    http://www.nature.com/articles/srep15808  
  • Gushchin I, Shevchenko V, Polovinkin V, Kovalev K, Alekseev A, Round E, Borshchevskiy V, Balandin T, Popov A, Gensch T, Fahlke C, Bamann C, Willbold D, Büldt G, Bamberg E, Gordeliy V 
    Crystal structure of a light-driven sodium pump. 
    Nat. Struct. Mol. Biol. 22, 390-395 (2015) 
  • Hung Y-F, Schwarten M, Hoffmann S, Willbold D, Sklan EH, Koenig BW 
    Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes 
    Viruses 7, 4119-4130 (2015) 
    Link  
  • Hung Y-F, Schwarten M, Schünke S, Thiagarajan-Rosenkranz P, Hoffmann S, Sklan EH, Willbold D, Koenig BW 
    Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature 
    BBA - Biomembranes 1848, 1119-1126 (2015) 
  • Jiang N, Leithold LH, Post J, Ziehm T, Mauler J, Gremer L, Cremer M, Schartmann E, Shah NJ, Kutzsche J, Langen KJ, Breitkreutz J, Willbold D, Willuweit A 
    Preclinical Pharmacokinetic Studies of the Tritium Labelled D-Enantiomeric Peptide D3 Developed for the Treatment of Alzheimer´s Disease 
    PLoS One 10, e0128553 (2015) 
  • Kahlert UD, Koch K, Hartmann R, Suwala AK, Cheng M, Maciaczyk D, Eberhart CG, Willbold D, Glunde K, Maciaczyk J 
    The effect of neurosphere culture conditions on cellular metabolism of glioma cells. 
    Folia Neuropathologica 53, 219-225 (2015) 
  • Ma P, Schillinger O, Schwarten M, Lecher J, Hartmann R, Stoldt M, Mohrlüder J, Olubiyi O, Strodel B, Willbold D, Weiergräber OH 
    Conformational Polymorphism in Autophagy-Related Protein GATE-16 
    Biochemistry 54, 5469-5479 (2015) 
  • Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P 
    Observing the overall rocking motion of a protein in a crystal. 
    Nat. Commun. 6, 8361 (2015) 
  • Mandler M, Santic R, Gruber P, Cinar Y, Pichler D, Funke SA, Willbold D, Schneeberger A, Schmidt W, Mattner F 
    Tailoring the antibody response to aggregated Aß using novel Alzheimer-vaccines. 
    PLoS ONE 10, e0115237 (2015) 
  • Matousek J, Piernikarczyk RJJ, Týcová A, Duraisamy GS, Kocábek T, Steger G 
    Expression of SANT/HTH Myb mRNA, a plant morphogenesis-regulating transcription factor, changes due to viroid infection 
    Journal of Plant Physiology 183, 85-94 (2015) 
    http://dx.doi.org/10.1016/j.jplph.2015.06.001  
  • Michel M, Schwarten M, Decker C, Nagel-Steger L, Willbold D, Weiergräber OH 
    The mammalian autophagy initiator complex contains 2 HORMA domain proteins 
    Autophagy 11, 2300-2308 (2015) 
    http://dx.doi.org/10.1080/15548627.2015.1076605  
  • Nouri K, Moll JM, Milroy LG, Hain A, Dvorsky R, Amin E, Lenders M, Nagel-Steger L, Howe S, Smits SH, Hengel H, Schmitt L, Münk C, Brunsveld L, Ahmadian MR 
    Biophysical Characterization of Nucleophosmin Interactions with Human Immunodeficiency Virus Rev and Herpes Simplex Virus US11. 
    PLoS One 10(12), e0143634 (2015) 
    http://dx.doi.org/10.1371/journal.pone.0143634  
  • Pattky M, Nicolardi S, Santiago-Schübel B, Sydes D, van der Burgt YE, Klein AN, Jiang N, Mohrlüder J, Hänel K, Kutzsche J, Funke SA, Willbold D, Willbold S, Huhn C 
    Structure characterization of unexpected covalent O-sulfonation and ion-pairing on an extremely hydrophilic peptide with CE-MS and FT-ICR-MS. 
    Anal. Bioanal. Chem. 407, 6637-6655 (2015) 
  • Sali A, Berman HM, Schwede T, Trewhella J, Kleywegt G, Burley SK, Markley J, Nakamura H, Adams P, Bonvin AMJJ, Chiu W, Dal Peraro M, DiMaio F, Ferrin TE, Grünewald K, Gutmanas A, Henderson R, Hummer G, Iwasaki K, Johnson G, Lawson CL, Meiler J, Marti-Renom MA, Montelione GT, Nilges M, Nussinov R, Patwardha A, Rappsilber J, Read RJ, Saibil H, Schröder GF, Schwieters C, Seidel CAM, Svergun D, Topf M, Ulrich EL, Velankar S, Westbrook JD 
    Outcome of the First wwPDB Hybrid / Integrative Methods Task Force Workshop 
    Structure 23(7), 1156-1167 (2015) 
  • Schröder GF 
    Hybrid methods for macromolecular structure determination: experiment with expectations 
    Curr Opin Struct Biol 31, 20-27 (2015) 
  • Shaykhalishahi H, Gauhar A, Wördehoff MM, Grüning CS, Klein A, Bannach O, Stoldt M, Willbold D, Härd T, Hoyer W 
    Contact between the beta1 and beta2 segments of alpha-synuclein that inhibits amyloid formation 
    Angew. Chem. Int. Ed. 54, 8837-8840 (2015) 
    http://dx.doi.org/10.1002/anie.201503018  
  • Shaykhalishahi H, Mirecka EA, Gauhar A, Grüning CSR, Willbold D, Härd T, Stoldt M, Hoyer W 
    A beta-hairpin-binding protein for three different disease-related amyloidogenic proteins 
    ChemBioChem 16, 411-414 (2015) 
    http://dx.doi.org/10.1002/cbic.201402552  
  • Solyom Z, Ma P, Schwarten M, Bosco M, Polidori A, Durand G, Willbold D, Brutscher B 
    The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation. 
    Biophys. J. 109, 1483-1496 (2015) 
  • Spiegel M, Duraisamy AK, Schröder GF 
    Improving the Visualisation of Cryo-EM Density Reconstructions 
    J Struct Biol 191(2), 207-213 (2015) 
  • Wildberg A, Della Corte D, Schröder GF. 
    Coupling an ensemble of homologs improves refinement of protein homology models  
    J. Chem. Theo. Comput. 11(12), 5578–5582 (2015) 
  • Wolff M, Unuchek D, Zhang B, Gordeliy V, Willbold D, Nagel-Steger L 
    Amyloid β oligomeric species present in the lag phase of amyloid formation. 
    PLoS ONE 10, e0127865 (2015) 
    http://dx.doi.org/10.1371/journal.pone.0127865  
  • Wördehoff MM, Bannach O, Shaykhalishahi H, Kulawik A, Schiefer S, Willbold D, Hoyer W, Birkmann E 
    Single fibril growth kinetics of alpha-synuclein. 
    J. Mol. Biol. 427, 1428-1435 (2015) 
    http://dx.doi.org/10.1016/j.jmb.2015.01.020  
    http://journal.frontiersin.org/article/10.3389/fnins.2016.00008/abstract  
  • Zhao H, Ghirlando R, Alfonso C, Arisaka F, Attali I, Bain DL, Bakhtina MM, Becker DF, Bedwell GJ, Bekdemir A, Besong TM, Birck C, Brautigam CA, Brennerman W, Byron O, Bzowska A, Chaires JB, Chaton CT, Cölfen H, Connaghan KD, Crowley KA, Curth U, Daviter T, Dean WL, Díez AI, Ebel C, Eckert DM, Eisele LE, Eisenstein E, England P, Escalante C, Fagan JA, Fairman R, Finn RM, Fischle W, de la Torre JG, Gor J, Gustafsson H, Hall D, Harding SE, Cifre JG, Herr AB, Howell EE, Isaac RS, Jao SC, Jose D, Kim SJ, Kokona B, Kornblatt JA, Kosek D, Krayukhina E, Krzizike D, Kusznir EA, Kwon H, Larson A, Laue TM, Le Roy A, Leech AP, Lilie H, Luger K, Luque-Ortega JR, Ma J, May CA, Maynard EL, Modrak-Wojcik A, Mok YF, Mücke N, Nagel-Steger L, Narlikar GJ, Noda M, Nourse A, Obsil T, Park CK, Park JK, Pawelek PD, Perdue EE, Perkins SJ, Perugini MA, Peterson CL, Peverelli MG, Piszczek G, Prag G, Prevelige PE, Raynal BD, Rezabkova L, Richter K, Ringel AE, Rosenberg R, Rowe AJ, Rufer AC, Scott DJ, Seravalli JG, Solovyova AS, Song R, Staunton D, Stoddard C, Stott K, Strauss HM, Streicher WW, Sumida JP, Swygert SG, Szczepanowski RH, Tessmer I, Toth RT 4th, Tripathy A, Uchiyama S, Uebel SF, Unzai S, Gruber AV, von Hippel PH, Wandrey C, Wang SH, Weitzel SE, Wielgus-Kutrowska B, Wolberger C, Wolff M, Wright E, Wu YS, Wubben JM, Schuck P 
    A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. 
    PLoS One 10(5), e0126420 (2015) 
    http://dx.doi.org/10.1371/journal.pone.0126420  
  • Aladag A, Hoffmann S, Stoldt M, Bösing C, Willbold D, Schwarten M 
    Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro 
    J. Pept. Science 20, 334-340 (2014) 
  • Arslan Z, Hermanns V, Wurm R, Wagner R, Pul U 
    Detection and characterization of spacer integration intermediates in type I-E CRISPR-Cas system 
    Nucleic Acids Res 42, 7884-7893 (2014) 
    http://dx.doi.org/10.1093/nar/gku510  
  • Borshchevskiy V, Round E, Erofeev I, Weik M, Ishchenko A, Gushchin I, Mishin A, Willbold D, Büldt G, Gordeliy V 
    Ultra-low dose X-ray radiation induces structural alterations in proteins 
    Acta Cryst. D 70, 2675-2685 (2014) 
  • Elter S, Raschle T, Arens S, Viegas A, Gelev V, Etzkorn M, Wagner G 
    The use of amphipols for NMR structural characterization of 7-TM proteins 
    J. Membr. Biol. 247, 957-964 (2014) 
    http://dx.doi.org/10.1007/s00232-014-9669-5  
  • Etzkorn M, Zoonens M, Catoire LJ, Popot JL, Hiller S 
    How Amphipols Embed Membrane Proteins: Global Solvent Accessibility and Interaction with a Flexible Protein Terminus 
    J. Membr. Biol. 247, 965-970 (2014) 
    http://dx.doi.org/10.1007/s00232-014-9657-9  
  • Frenzel D, Glück JM, Brener O, Oesterhelt F, Nagel-Steger L, Willbold D 
    Immobilization of homogeneous monomeric, oligomeric and fibrillar Aβ species for reliable SPR measurements 
    PLoS ONE 9, e89490 (2014) 
  • Frenzel D, Willbold D 
    Kinetic titration series with biolayer interferometry 
    PLoS ONE 9, e106882 (2014) 
  • Gauhar A, Shaykhalishahi H, Gremer L, Mirecka EA, Hoyer W 
    Impact of subunit linkages in an engineered homodimeric binding protein to alpha-synuclein 
    Protein Eng. Des. Sel. 27, 473-479 (2014) 
    http://dx.doi.org/10.1093/protein/gzu047  
  • Grüning CS, Mirecka EA, Klein AN, Mandelkow E, Willbold D, Marino SF, Stoldt M, Hoyer W 
    Alternative conformations of the tau repeat domain in complex with an engineered binding protein 
    J. Biol. Chem. 289, 23209-23218 (2014) 
    http://dx.doi.org/10.1074/jbc.M114.560920  
  • Hänel K, Möckel L, Brummel M, Peiris K, Hartmann R, Dingley AJ, Willbold D, Loidl-Stahlhofen A 
    Expression and purification of soluble HIV-2 viral protein R (Vpr) using a sandwich-fusion protein strategy 
    Prot. Expr. Purific. 95, 156-161 (2014) 
    http://www.sciencedirect.com/science/article/pii/S1046592813002763  
  • Hung Y-F, Valdau O, Schünke S, Stern O, Koenig BW, Willbold D, Hoffmann S 
    Recombinant production of the amino terminal cytoplasmic region of dengue virus non-structural protein 4A for structural studies 
    PLoS ONE 9, e86482 (2014) 
    Link  
  • Kowal J, Chami M, Baumgartner P, Arheit M, Chiu PL, Rangl M, Scheuring S, Schröder GF, Nimmigean CM, Stahlberg H 
    Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1 
    Nat Commun 5, 3106 (2014) 
  • Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos M, Schröder GF, Fitzgerald KA, Wu H, and Egelman EH 
    Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes 
    Cell 156, 1193-1206 (2014) 
    http://dx.doi.org/10.1016/j.cell.2014.02.008  
  • Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P 
    Probing transient conformational States of proteins by solid-state r1ρ relaxation-dispersion NMR spectroscopy. 
    Angew. Chem. Int. Ed. Engl. 53, 4312–4317 (2014) 
  • Matousek J, Piernikarczyk RJJ, Dědič P, Mertelík J, Uhlířová K, Duraisamy GS, Orctová L, Kloudová K, Ptáček J, Steger G 
    Characterization of Potato spindle tuber viroid (PSTVd) incidence and new variants from ornamentals 
    Europ J Plant Path 138, 93-101 (2014) 
    http://dx.doi.org/10.1007/s10658-013-0304-6  
  • Mirecka EA, Gremer L, Schiefer S, Oesterhelt F, Stoldt M, Willbold D, Hoyer W 
    Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide 
    J. Biotechnol. 191, 221-227 (2014) 
    http://dx.doi.org/10.1016/j.jbiotec.2014.06.006  
  • Mirecka EA, Shaykhalishahi H, Gauhar A, Akgül S, Lecher J, Willbold D, Stoldt M, Hoyer W 
    Sequestration of a beta-hairpin for control of alpha-synuclein aggregation 
    Angew. Chem. Int. Ed. 53, 4227-4230 (2014) 
    http://dx.doi.org/10.1002/anie.201309001  
    http://dx.doi.org/10.1002/ange.201309001  
  • Müller H, Brener O, Andreoletti O, Piechatzek T, Willbold D, Legname G, Heise H 
    Progress toward structural understanding of infectious sheep PrP-amyloid 
    Prion 8, 344-358 (2014) 
  • Olubiyi OO, Frenzel D, Bartnik D, Glück JM, Brener O, Nagel-Steger L, Funke SA, Willbold D, Strodel B 
    Amyloid aggregation inhibitory mechanism of arginine-rich D-peptides 
    Curr. Med. Chem. 21, 1448-1457 (2014) 
  • Patra D, Fasold M, Langenberger D, Steger G, Grosse I, Stadler, PF 
    plantDARIO: web based quantitative and qualitative analysis of small RNA-seq data in plants 
    Frontiers in Plant Science 5, (2014) 
    http://dx.doi.org/10.3389/fpls.2014.00708  
  • Polovinkin V, Balandin T, Volkov O, Round E, Borshchevskiy V, Utrobin P, von Stetten D, Royant A, Willbold D, Arzumanyan G, Chupin V, Popot JL, Gordeliy V 
    Nanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35 
    J. Membr. Biol. 247, 997-980 (2014) 
  • Polovinkin V, Gushchin I, Sintsov M, Round E, Balandin T, Chervakov P, Schevchenko V, Utrobin P, Popov A, Borshchevskiy V, Mishin A, Kuklin A, Willbold D, Chupin V, Popot JL, Gordeliy V 
    High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase 
    J. Membr. Biol. 247, 997-1004 (2014) 
  • Pul U 
    Chemical and enzymatic footprint analyses of R-Loop formation by Cascade-crRNA complex 
    Meth. Mol. Biol. 1311, 293-305 (2014) 
  • Riesner D, Steger G 
    Temperature-gradient gel-electrophoresis. 
    In Bindereif, A., Hartmann, R., Schön, A. & Westhof, E. (eds), Handbook of RNA Biochemistry, Part II, 2nd edition, Wiley-VCH , 427-444 (2014) 
    http://dx.doi.org/10.1002/9783527647064.ch21  
  • Schröder GF, Levitt M, Brunger AT 
    Deformable elastic network refinement for low-resolution macromolecular crystallography 
    Acta Cryst. D D70, 2241-2255 (2014) 
  • Steger G 
    Secondary Structure Prediction. 
    In Bindereif, A., Hartmann, R., Schön, A. & Westhof, E. (eds), Handbook of RNA Biochemistry, Part III, 2nd edition, Wiley-VCH , 547-578 (2014) 
    http://dx.doi.org/10.1002/9783527647064.ch26  
  • Widera M, Klein NA, Cinar Y, Funke SA, Willbold D, Schaal H 
    The D-amino acid peptide D3 reduces amyloid fibril boosted HIV-1 infectivity 
    AIDS Res. Therapy 11, 1 (2014) 
  • Yi T, Zhai B, Yu Y, Kiyotsugu Y, Raschle T, Etzkorn M, Seo HC, Nagiec M, Luna RE, Reinherz EL, Blenis J, Gygi SP, Wagner G 
    Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/CXCR4 in breast cancer stem cells 
    PNAS 111(21), E2182-E2190 (2014) 
    http://dx.doi.org/10.1073/pnas.1404943111  
    http://dx.doi.org/10.1073/pnas.1405991111  
    See also PNAS highlight commentary (follow second link) 
  • Amin E, Dubey BN, Zhang SC, Gremer L, Dvorsky R, Moll JM, Taha MS, Nagel-Steger L, Piekorz RP, Somlyo AV, Ahmadian MR 
    Rho-kinase: regulation, (dys)function, and inhibition 
    Biol Chem. 394, 1399-1410 (2013) 
    full text  
  • Arslan Z, Stratmann T, Wurm R, Wagner R, Schnetz K, Pul U 
    RcsB-BglJ mediated activation of Cascade operon does not induce the maturation of CRISPR RNAs in E. coli K12 
    RNA Biol. 10, 708-715 (2013) 
    full text  
  • Arslan Z, Westra ER, Wagner R, Pul U 
    Regulation of CRISPR-based immune responses 
    In: CRISPR-Cas systems: RNA-mediated Adaptive Immunity in Bacteria and Archaea, Barrangou, Rodolphe; van der Oost, John (Eds.) , Springer-Verlag X, 93-113 (2013) 
    full text  
  • Arslan Z, Wurm R, Brener O, Ellinger P, Nagel-Steger L, Oesterhelt F, Schmitt L, Willbold D, Wagner R, Gohlke H, Smits S, Pul U 
    Double-strand DNA end-binding and sliding of the toroidal CRISPR-associated protein Csn2. 
    Nucl Acids Res 41, 6347-6359 (2013) 
    open access  
  • Bannach O, Reinartz E, Henke F, Dreßen F, Oelschlegel A, Kaatz M, Groschup M H, Willbold D, Riesner D and Birkmann E 
    Analysis of prion protein aggregates in blood and brain from pre-clinical and clinical BSE cases 
    Vet Microbiol 166, 102-108 (2013) 
    http://dx.doi.org/10.1016/j.vetmic.2013.05.021  
  • Bannach O, Riesner D 
    Prions Overview 
    In: The Encyclopedia of Biological Chemistry. William J. Lennarz, M. Daniel Lane (eds.), Elsevier Inc. 3, 571-575 (2013) 
  • Bier D, Hartmann R, Holschbach M 
    Collision-induced dissociation studies of caffeine in positive electrospray ionisation mass spectrometry using six deuterated isotopomers and one N1-ethylated homologue 
    Rapid communications in mass spectrometry 27, 885-895 (2013) 
  • Bobby R, Medini K, Neudecker P, Lee TV, Brimble MA, McDonald FJ, Lott JS, Dingley AJ 
    Structure and dynamics of human Nedd4-1 WW3 in complex with the αENaC PY motif 
    Biochim Biophys Acta 1834, 1632-41 (2013) 
    http://dx.doi.org/10.1016/j.bbapap.2013.04.031  
  • Bock LV, C Blau, GF Schröder, II Davydov, N Fischer, H Stark, MV Rodnina, AC Vaiana, and H Grubmüller 
    Energy barriers and driving forces in tRNA translocation through the ribosome 
    Nat. Struct. Mol. Biol. 20, 1390-1396 (2013) 
    http://www.nature.com/nsmb/journal/vaop/ncurrent/abs/nsmb.2690.html  
  • Chen D-H, Madan D, Weaver J, Lin Z, Schröder GF, Chiu W, Rye HS 
    Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein 
    Cell 153, 1354-1365 (2013) 
  • Chen DH, Madan D, Weaver J, Lin Z, Schröder GF, Chiu W, Rye HS 
    Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein 
    Cell 153, 1354–1365 (2013) 
  • Chien T-H, Chiang Y-L, Chen C-P, Henklein P, Hänel K, Hwang I-S, Willbold D, Fischer WB 
    Assembling an ion channel: ORF 3a from SARS-CoV 
    Biopolymers 99, 628-635 (2013) 
    http://dx.doi.org/10.1002/bip.22230  
  • Deng X, J Morris, C Chaton, GF Schröder, WS Davidson and TB Thompson 
    Small-angle X-ray Scattering of Apolipoprotein A-IV Reveals the Importance of Its Termini for Structural Stability 
    J. Biol. Chem. 288, 4854 (2013) 
  • Dioletis E, Dingley AJ, Driscoll PC 
    Structural and functional characterization of the recombinant death domain from death-associated protein kinase 
    PLoS One 8, e70095 (2013) 
    full text  
  • Do H, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H 
    Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR. 
    Biol. Chem. 394, 1453-1463 (2013) 
  • Dornieden S, Müller-Schiffmann A, Sticht H, Cinar Y, Wördehoff M, Korth C, Funke SA, Willbold D 
    Characterization of a single-chain variable fragment recognizing a linear epitope of Aß: A biotechnical tool for studies on Alzheimer's disease? 
    PLoS ONE 8, e59820 (2013) 
  • Eichhorn T, Winter D, Büchele B, Dirdjaja N, Frank M, Lehmann WD, Mertens R, Krauth-Siegel RL, Simmet T, Granzin J, Efferth T 
    Molecular interaction of artemisinin with translationally controlled tumor protein (TCTP) of Plasmodium falciparum. 
    Biochem Pharmacol. 85, 38-45 (2013) 
    http://dx.doi.org/10.1016/j.bcp.2012.10.006  
  • Falkner B and Schröder GF 
    Cross-validation in cryo-electron microscopy based structural modeling 
    PNAS 110, 8930 (2013) 
  • Falkner B, Schröder GF 
    Cross-validation in cryo-electron microscopy based structural modeling 
    PNAS 110(22), 8930-8935 (2013) 
  • Grüning CS, Klinker S, Wolff M, Schneider M, Toksöz K, Klein AN, Nagel-Steger L, Willbold D, Hoyer W 
    The off-rate of monomers dissociating from amyloid-beta protofibrils 
    J. Biol. Chem. 288, 37104-37111 (2013) 
    http://dx.doi.org/10.1074/jbc.M113.513432  
  • Kalisman N, GF Schröder, M Levitt 
    The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal its Functional Partitioning 
    Structure 21, 540 (2013) 
  • Kovacic F, Granzin J, Wilhelm S, Kojic-Prodic B, Batra-Safferling R, Jaeger KE 
    Structural and Functional Characterisation of TesA - A Novel Lysophospholipase A from Pseudomonas aeruginosa. 
    PLoS One 8, e69125 (2013) 
    http://dx.doi.org/10.1371/journal.pone.0069125  
    http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0069125  
  • Kruse C, Willbold D, Schmitt L 
    Highlight: NRW Research School BioStruct - Biological Structures in Molecular Medicine and Biotechnology. 
    Biol. Chem. 394, 1353-1355 (2013) 
  • Luers, L, Bannach, O, Stöhr, J, Wördehoff, MM, Wolff M, Nagel-Steger, L, Riesner, D, Willbold, D, Birkmann E 
    Seeded Fibrillation as Molecular Basis of the Species Barrier in Human Prion Diseases 
    PloS ONE 8, e72623 (2013) 
  • Ma P, Schwarten M, Schneider L, Boeske A, Henke N, Lisak D, Weber S, Mohrlüder J, Stoldt M, Strodel B, Methner A, Hoffmann S, Weiergräber OH, Willbold D 
    Interaction of Bcl-2 with the autophagy-related GABAA receptor-associated protein (GABARAP): Biophysical characterization and functional implications 
    J Biol Chem 288, 37204-37215 (2013) 
  • Marbach, J; Zentis, P; Ellinger, P; Müller, H; Birkmann, E 
    Expression and characterization of fully posttranslational modified cellular prion protein in Pichia pastoris 
    Biol. Chem. 394, 1475-1483 (2013) 
  • Marchfelder A, Maier L-K, Heidrich N, Pul U 
    Das Immunsystem der Prokaryoten: CRISPR-Cas 
    BiuZ 43(3), 158-165 (2013) 
    full text (Cover article)  
  • Pavlidou M, Hänel K, Möckel L, Willbold D 
    Nanodiscs allow phage display selection for ligands to non-linear epitopes on membrane proteins 
    PLoS ONE 9, e72272 (2013) 
  • Pham C, Hartmann R, Müller WEG, de Voogd N, Lai D, Proksch P 
    Aaptamine Derivates from the Indonesian Sponge Aaptos suberitoides 
    Journal of natural products 76(1), 103-106 (2013) 
  • Pham C, Weber H, Hartmann R, Wray V, Lin W, Lai D, Proksch P 
    New Cytotoxic 1,2,4.Thiadiazole Alkaloids fromthe Ascidian Polycarpa aurata 
    Organic letters 15, 2230-2233 (2013) 
    http://dx.doi.org/10.1016/j.bbamem.2012.09.001  
  • Rani R, Jentzsch K, Lecher L, Hartmann R, Willbold D, Jaeger K-E, Krauss U 
    Conservation of dark recovery kinetic parameters and structural features in the Pseudomonadaceae “short” LOV protein family – implications for the design of LOV-based optogenetic tools. 
    Biochemistry 52, 4460-4473 (2013) 
  • Reinauer C, Censarek P, Kaber G, Weber AA, Steger G, Klamp T, Schrör K 
    Expression and translation of the COX-1b gene in human cells--no evidence of generation of COX-1b protein 
    Biol Chem 394, 753-760 (2013) 
    http://dx.doi.org/10.1515/hsz-2012-0309  
  • Schünke S, Stoldt M 
    Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels 
    Biol Chem. 394, 1439-1451 (2013) 
    http://www.ncbi.nlm.nih.gov/pubmed/24021595  
  • Schwarten M, Solyom Z, Feuerstein S, Aladag A, Hoffmann S, Willbold D, Brutscher B 
    Interaction of non-structural protein 5A of hepatitis C virus with SH3 domains using non-canonical binding sites 
    Biochemistry 52, 6160-6168 (2013) 
  • Solyom Z, Schwarten M, Geist L, Konrat R, Willbold D, Brutscher B 
    BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins 
    J. Biomol. NMR 55, 311-221 (2013) 
  • Steger G, Giegerich R 
    RNA structure prediction 
    in "RNA Structure and Folding: Biophysical Techniques and Prediction Methods" (Klostermeier D, Hammann C) de Gruyter, 335-362 (2013) 
    http://dx.doi.org/10.1515/9783110284959.335  
  • Stern O, Hung Y-F, Valdau O, Yaffe Y, Harris E, Hoffmann S, Willbold D, Sklan E 
    An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. 
    J. Virol. 87, 4080-4085 (2013) 
  • Steuten B, Setney P, Zacharias M, Wagner R 
    Mapping the Spatial Neighborhood of the Regulatory 6S RNA Bound to Escherichia coli RNA Polymerase Holoenzyme 
    J. Mol. Biol. 425, 3649-3661 (2013) 
  • Thakur HC, Singh M, Nagel-Steger L, Prumbaum D, Kalawy Fansa E, Gremer L, Ezzahoini H, Abts A, Schmitt L, Raunser S, Ahmadian MR, Piekorz RP 
    Role of centrosomal adaptor proteins of the TACC family in the regulation of microtubule dynamics during mitotic cell division 
    Biol Chem 394, 1411-1423 (2013) 
    full text  
  • van Groen T, Kadish I, Funke SA, Bartnik D, Willbold D 
    Treatment with D3 removes amyloid deposits, reduces inflammation, and improves cognition in old AβPP/PS1 double transgenic mice. 
    J Alzheimer's Dis. 34, 609-620 (2013) 
    open access  
  • Vasudevan AA, Smits SH, Hoeppner A, Haeussinger D, Koenig BW, Muenk C 
    Structural features of antiviral DNA cytidine deaminases 
    Biological Chemistry 394, 1357 - 1370 (2013) 
  • Wang-Dietrich L, Funke SA, Kühbach K, Wang K, Besmehn A, Willbold S, Cinar Y, Bannach O, Birkmann E, Willbold D 
    The Aβ oligomer count in CSF is a biomarker for Alzheimer’s disease. 
    J. Alzheimers Dis. 34, 985-994 (2013) 
  • Weiergräber OH, Mohrlüder J, Willbold D 
    Atg8 family proteins –- autophagy and beyond 
    in: Autophagy - A double-edged sword - Cell survival or death? ISBN 978-953-51-1062-0, Editor: Yannick Bailly (2013) 
    open access  
  • Aigner K, Dreßen F, Steger G 
    Methods for Predicting RNA Secondary Structure 
    In "Nucleic Acids and Molecular Biology: RNA 3D Structure Analysis and Prediction" (Leontis N, Westhof E) 27, 19-42 (2012) 
    http://dx.doi.org/10.1007/978-3-642-25740-7_3  
  • Bannach O, Birkmann E, Reinartz E, Jaeger K-E, Langeveld JP, Rohwer RG, Gregory L, Terry LA, Willbold D, Riesner D 
    Detection of Prion Protein Particles in Blood Plasma of Scrapie Infected Sheep 
    PLoS ONE 7, e36620 (2012) 
    http://dx.doi.org/10.1371/journal.pone.0036620  
    full text open access  
  • Brunger AT, D Das, AM Deacon, J Grant, TC Terwilliger, RJ Read, PD Adams, M Levitt and GF Schröder 
    Application of DEN-Refinement And Automated Model-Building To A Difficult Case Of Molecular Replacement Phasing: The Structure Of A Putative Succinyl-Diaminopimelate Desuccinylase From Corynebacterium Glutamicum. 
    Acta Cryst. D 68, 391 (2012) 
  • Brunger AT, PD Adams, P Fromme, R Fromme, M Levitt, and GF Schröder 
    Improving the accuracy of macromolecular structure refinement at 7 Å resolution. 
    Structure 20(6), 957 (2012) 
  • Circolone F, Granzin J, Jentzsch K, Drepper T, Jaeger K-E, Willbold D, Krauss U, Batra-Safferling R 
    Structural basis for the slow dark recovery of a full-length LOV protein from Pseudomonas putida. 
    J. Mol. Biol. 417, 362–374 (2012) 
  • Ellinger P, Arslan Z, Wurm R, Ries B, MacKenzie C, Pfeffer K, Panjikar S, Wagner R, Schmitt L, Gohlke H, Pul U, Smits SHJ 
    The crystal structure of the CRISPR-associated protein Csn2 from Streptococcus agalactiae 
    J. Struct. Biol. 178 (3), 350-62 (2012) 
    full text  
  • Feuerstein S, Plevin MJ, Willbold D, Brutscher B 
    iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered protein. 
    J. Magn. Res. 214, 329-334 (2012) 
  • Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B 
    Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. 
    J. Mol. Biol. 420, 310-323 (2012) 
  • Funke SA, Bartnik D, Glück JM, Pirkowska K, Wiesehan K, Weber U, Gulyas B, Halldin C, Pfeifer A, Spenger C, Muhs A, Willbold D 
    Development of a small D-enantiomeric Alzheimer's amyloid-beta binding peptide ligand for future in vivo imaging applications. 
    PLoS ONE 7, e41457 (2012) 
  • Funke SA, Liu H, Sehl T, Bartnik D, Brener O, Nagel-Steger L, Wiesehan K, Willbold D 
    Identification and characterization of an Aβ oligomer precipitating peptide that may be useful to explore gene therapeutic approaches to Alzheimer’s disease. 
    Rejuv. Res. 15, 144-147 (2012) 
  • Funke SA, Willbold D 
    Peptides for Therapy and Diagnosis of Alzheimer’s Disease. 
    Curr. Pharm. Design 18, 755-767 (2012) 
  • Granzin J, Cousin A, Weirauch M, Schlesinger R, Büldt G, Batra-Safferling R 
    Crystal structure of p44, a constitutively active splice variant of visual arrestin. 
    J Mol Biol. 416(5), 611-8 (2012) 
    http://dx.doi.org/10.1016/j.jmb.2012.01.028  
  • Gulyás B, Spenger C, Beliczai Z, Gulya K, Kása P, Jahan M, Jia Z, Weber U, Pfeifer A, Muhs A, Willbold D, Halldin C 
    Distribution and binding of (18)F-labeled and (125)I-labeled analogues of ACI-80, a prospective molecular imaging biomarker of disease: A whole hemisphere post mortem autoradiography study in human brains obtained from Alzheimer's disease patients. 
    Neurochem. Intern. 60, 153-162 (2012) 
  • Hammann C, Steger G 
    Viroid-specific small RNA in plant disease 
    RNA Biology 9, 809-819 (2012) 
    http://dx.doi.org/10.4161/rna.19810  
  • Henderson R, A Sali, ML Baker, B Carragher, B Devkota, KH Downing, EH Egelman, Z Feng, J Frank, N Grigorieff, W Jiang, SJ Ludtke, O Medalia, PA Penczek, PB Rosenthal, MG Rossmann, MF Schmid, GF Schröder, AC Steven, DL Stokes, JD Westbrook, W Wriggers, H Yang, J Young, HM Berman, W Chiu, GJ Kleywegt, CL Lawson 
    Outcome of the First Electron Microscopy Validation Task Force Meeting. 
    Structure 20, 205 (2012) 
  • Holze R, Jacob T, Schünke S, Neudecker P, Willbold D 
    Physical Chemistry 2011 
    Nachr. Chemie 60, 313-322 (2012) 
  • Hübinger S, Bannach O, Funke SA, Willbold D, Birkmann E 
    Detection of alpha-synuclein aggregates by fluorescence microscopy 
    Rejuvenation Res. 15, 213-216 (2012) 
  • Jahan M, Nag S, Krasikova R, Weber U, Muhs A, Pfeifer A, Spenger C, Willbold D, Gulyás B, Halldin C 
    Fluorine-18 labeling of three novel d-peptides by conjugation with N-succinimidyl-4-[(18)F]fluorobenzoate and preliminary examination by postmortem whole-hemisphere human brain autoradiography. 
    Nucl. Med. Biol. 392, 315-323 (2012) 
  • Kammula E, Moetter J, Gorgels A, Jonas E, Hoffmann S, Willbold D 
    Brain transcriptome-wide screen for HIV-1 Nef protein interaction partners reveals various membrane-associated proteins. 
    PLoS ONE 7, e51578 (2012) 
    http://dx.doi.org/10.1371/journal.pone.0051578  
    full text open access  
  • Klionsky DJ, et al, Willbold D, et al (many co-authors) 
    Guidelines for the use and interpretation of assays for monitoring autophagy. 
    Autophagy 8, 445-544 (2012) 
  • Koenig BW, Schünke S, Stoldt M, Willbold D 
    NMR methods for the determination of protein-ligand interactions. 
    Protein-Ligand Interactions" (Editor: H. Gohlke) (series "Methods and Principles in Medicinal Chemistry"), Wiley-VCH; ISBN: 3-527-32966-8, (2012) 
  • Kroth H, Ansaloni A, Varisco Y, Jan A, Sreenivasachary N, Rezaei-Ghaleh N, Giriens V, Lohmann S, Pilar López-Deber M, Adolfsson O, Pihlgren M, Paganetti P, Froestl W, Nagel-Steger L, Willbold D, Schrader T, Zweckstetter M, Pfeifer A, Lashuel HA, Muhs A 
    Discovery and structure activity relationship of small molecule inhibitors of toxic β-amyloid-42 fibril formation. 
    J. Biol. Chem. 287, 34786-34800 (2012) 
  • Lecher J, Schwarz CKW, Stoldt M, Smits SHJ, Willbold D, Schmitt L 
    RTX toxin transporters tether its substrate prior to secretion via the unique function of its N- terminal domain. 
    Structure 20, 1778-1787 (2012) 
  • Luers L, Rysiewksi K, Dumpitak C, Birkmann E 
    Kinetics of AGE-formation on BSA with various reducing sugars and dicarbonyl compounds in equimolar ratios 
    Rejuvenation Res. 15(2), 201-5 (2012) 
  • Matousek J, Riesner D, Steger G 
    Viroids: the smallest known infectious agents cause accumulation of viroid-specific small RNAs 
    In "From Nucleic Acids Sequences to Molecular Medicine" (Erdmann VA, Barciszewski J) Springer-Verlag, Heidelberg IX, 629-644 (2012) 
    http://www.springer.com/biomed/molecular/book/978-3-642-27425-1  
  • Matousek J, Stehlík J, Procházková J, Orctová L, Wullenweber J, Füssy Z, Kovácik J, Duraisamy GS, Ziegler A, Schubert J, Steger G 
    Biological and molecular analysis of the pathogenic variant C3 of potato spindle tuber viroid (PSTVd) evolved during adaptation to chamomile (Matricaria chamomilla) 
    Biol Chem 393, 605-615 (2012) 
    http://dx.doi.org/10.1515/hsz-2011-0286  
  • Mazargui H, Lévêque C, Bartnik D, Fantini J, Gouget T, Melone MA, Funke SA, Willbold D, Perrone L 
    A synthetic amino acid substitution of Tyr10 in Aβ peptide sequence yields a dominant negative variant in amyloidogenesis. 
    Aging Cell 11, 530-541 (2012) 
  • Neudecker P, Robustelli P, Cavallli A, Walsh P, Lundstrom P, Zarrine-Afsar A, Sharpe S, Vendruscolo M, Kay LE 
    Structure of an intermediate state in protein folding and aggregation. 
    Science 336, 362-366 (2012) 
  • O'Donovan DJ, I Stokes-Rees, Y Nam, S Blacklow, GF Schröder, AT Brunger, Piotr Sliz 
    A grid-enabled web service for low-resolution crystal structure refinement. 
    Acta Cryst. D 68, 268 (2012) 
  • Rediger, A, Geißen, R, Steuten, B, Heilmann, B, Wagner, R and Axmann, I M 
    6S RNA – an old issue became blue-green. 
    Microbiology 158, 2480-2491 (2012) 
  • Singh S, Möckel L, Thiagarajan-Rosenkranz P, Wittlich M, Willbold D, Koenig B 
    Mapping the interaction between the cytoplasmic domains of HIV-1 VpU and human CD4 using NMR spectroscopy. 
    FEBS J. 279, 3705-3714 (2012) 
  • Steuten, B and Wagner, R 
    A conformational switch is responsible for the reversal of the 6S RNA-dependent RNA polymerase inhibition in Escherichia coli. 
    Biol. Chem. 393, 513–1522 (2012) 
  • Stratmann T, Pul U, Wurm R, Wagner R, Schnetz K 
    RcsB-BglJ activates the Escherichia coli leuO gene, encoding an H-NS antagonist and pleiotropic regulator of virulence determinants 
    Mol. Microbiol. 83, 1109-1123 (2012) 
  • Sun N, Funke SA, Willbold D 
    A survey of peptides with effective therapeutic potential in Alzheimer’s disease rodent models or in human clinical studies. 
    Mini. Rev. Med. Chem. 12, 388-398 (2012) 
    full text open access  
  • Sun N, Funke SA, Willbold D 
    Mirror image phage display - Generating stable therapeutically and diagnostically active peptides with biotechnological means. 
    J. Biotech. 161, 121-125 (2012) 
    http://dx.doi.org/10.1016/j.jbiotec.2012.05.019  
    full text  
  • Sun N, Hartmann R, Lecher J, Stoldt M, Funke SA, Gremer L, Ludwig H-H, Demuth H-U, Kleinschmidt M, Willbold D 
    Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy. 
    J. Pept. Science 18, 691-695 (2012) 
  • T Sabir, A Toulmin, L Ma, AC Jones, P McGlynn, GF Schröder, and SW Magennis 
    Branchpoint expansion in a fully-complementary three-way DNA junction. 
    J. Am. Chem. Soc. 134(14), 6280 (2012) 
  • van Groen T, Kadish I, Funke A, Bartnik D, Willbold D 
    Treatment with Aβ42 Binding d-Amino Acid Peptides Reduce Amyloid Deposition and Inflammation in APP/PS1 Double Transgenic Mice. 
    Adv. Protein. Chem. Struct. Biol. 88, 133-152 (2012) 
  • Wagner R, Pul U 
    CRISPR - a bacterial immunity system based on small RNAs 
    In: From Nucleic Acids Sequences to Molecular Medicine, Erdmann, Volker A.; Barciszewski, Jan (Eds.), Springer-Verlag IX, 121-143 (2012) 
    full text  
  • Wang W, Pacheco V, Krause H-J, Zhang Y, Dong H, Hartmann R, Willbold D, Offenhaeusser A, Gu Z 
    Size and compositional effects on contrast efficiency of functionalized superparamagnetic nanoparticles at ultralow and ultrahigh magnetic fields. 
    J. Phys. Chem. C 116, 17880-17884 (2012) 
    http://dx.doi.org/10.1021/jp302758h  
  • Wang Z, Schröder GF 
    Real-space Refinement with DireX: From Global Fitting to Side-chain Improvements. 
    Biopolymers 97(9), 687 (2012) 
  • X Yu, C Goforth, C Meyer, R Rachel, R Wirth, GF Schröder, and EH Egelman 
    Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices. 
    J. Mol. Biol. 422(2), 274 (2012) 
  • Ziegler A, Matousek J, Steger G, Schubert J 
    Complete sequence of a cryptic virus from hemp (Cannabis sativa) 
    Arch. Virol. 157, 383-385 (2012) 
    http://dx.doi.org/10.1007/s00705-011-1168-8  
  • Alexander K. Buell, Elin K. Esbjörner, Patrick J. Riss, Duncan A. White, Franklin I. Aigbirhio, Gergely Toth, Mark E. Welland, Christopher M. Dobson and Tuomas P.J. Knowles 
    Probing small molecule binding to amyloid fibrils 
    Phys Chem Chem Phys 13, 20044-20052 (2011) 
    https://www.ncbi.nlm.nih.gov/pubmed/22006124  
  • Bajaj P, Steger G, Hammann C 
    Sequence elements outside the catalytic core of natural hairpin ribozymes modulate the reactions differentially 
    Biol. Chem. 392, 593-600 (2011) 
    http://dx.doi.org/10.1515/BC.2011.071  
  • Cong Y, Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, and Chiu W 
    Symmetry-Free Cryo-EM Structures of the Chaperonin TRiC Along its ATPase-Driven Conformational Cycle. 
    EMBO J 31, 720 (2011) 
  • Feuerstein S, Solyom Z, Aladag A, Hoffmann S, Willbold D, Brutscher B 
    1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus nonstructural protein 5A 
    Biomol. NMR Assign. 53, 241-243 (2011) 
  • Funke SA 
    Detection of Soluble Amyloid-β Oligomers and Insoluble High-Molecular-Weight Particles in CSF: Development of Methods with Potential for Diagnosis and Therapy Monitoring of Alzheimer's Disease. 
    Int J Alzheimers Dis. 2011, 151645 (2011) 
  • Funke SA, Willbold D 
    Quantitation of Amyloid-β oligomers in human body fluids for Alzheimer’s disease early diagnosis or therapy monitoring. 
    Alzheimer's diagnosis. Charles E. Ronson (Ed.), Hauppage, NY, USA (2011) 
    Nova Science Publishers, ISBN 978-1-61209-846-3 
  • Gao S, von der Malsburg A, Dick A, Faelber K, Schröder GF, Haller O, Kochs G, Daumke O 
    Three domain architecture of dynamin-like MxA GTPase. 
    Immunity 35, 514 (2011) 
  • Glück JM 
    Ligand interaction analysis of membrane-anchored proteins. 
    Schriften des Forschungszentrums Jülich Reihe Gesundheit, Band 31, (2011) 
    http://wwwzb1.fz-juelich.de/contentenrichment/inhaltsverzeichnisse/2010/verlag/gesund31_i.pdf  
  • Glück JM, Koenig BW, Willbold D 
    Nanodiscs allow the use of integral membrane proteins as analytes in surface plasmon resonance studies. 
    Anal. Biochem. 408, 46-52 (2011) 
  • Hickman DT, López-Deber MP, Ndao DM, Silva AB, Nand D, Pihlgren M, Giriens V, Madani R, St-Pierre A, Karastan H, Nagel-Steger L, Willbold D, Riesner D, Nicolau C, Baldus M, Pfeifer A, Muhs A 
    Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases. 
    J. Biol.Chem. 286, 13966-13976 (2011) 
  • Hochdörffer K, März-Berberich J, Nagel-Steger L, Epple M, Meyer-Zaika W, Horn AH, Sticht H, Sinha S, Bitan G, Schrader T 
    Rational Design of β-Sheet Ligands Against Aβ(42)-Induced Toxicity. 
    J. Am. Chem. Soc. 133, 4348-4358 (2011) 
  • Hofmann H, Wurm R, Wagner, R 
    The E. coli Anti-Sigma Factor Rsd: Studies on the Specificity and Regulation of its Expression. 
    PLoS ONE 6, e19235 (2011) 
    http://dx.doi.org/10.1371/journal.pone.0019235  
    http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0019235  
  • Jaenicke E, Büchler K, Decker H, Markl J, Barends T, and Schröder GF 
    The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges. 
    IUBMB Life 63(3), 183 (2011) 
  • Janssen S, Schudoma C, Steger G, Giegerich R 
    Lost in folding space? Comparing four variants of the thermodynamic model for RNA secondary structure prediction. 
    BMC Bioinformatics 12, 429 (2011) 
    http://dx.doi.org/10.1186/1471-2105-12-429  
  • Jore MM, Lundgren M, van Duin E, Bultema JB, Westra ER, Waghmare SP, Wiedenheft B, Pul U, Wurm R, Wagner R, Beijer M, Barendregt RA, Zhou K, Snijders APL, Dickman MJ, Doudna JA, Boekema EJ, Heck AJR, van der Oost J and Brouns SJJ 
    Structural basis for CRISPR RNA-guided DNA recognition by Cascade. 
    Nat. Struct. Mol. Biol. 18, 529–536 (2011) 
    http://dx.doi.org/10.1038/nsmb.2019  
    http://www.nature.com/nsmb/journal/v18/n5/full/nsmb.2019.html  
  • Kirchberg K, Kim TY, Möller M, Skegro D, Dasara Raju G, Granzin J, Büldt G, Schlesinger R, Alexiev U 
    Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. 
    Proc Natl Acad Sci U S A 108(46), 18690-5 (2011) 
    http://dx.doi.org/10.1073/pnas.1015461108  
  • Kolmsee, T, Delic, D, Agyenim, T, Calles, C and Wagner, R 
    Differential stringent control of E. coli rRNA promoters: effects of ppGpp, DksA and the initiating nucleotides. 
    Microbiology 157, 2871-2879 (2011) 
  • Lecher J, Stoldt M, Schwarz CKW, Smits SHJ, Schmitt L, Willbold D 
    ¹H, ¹⁵N and ¹³C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB). 
    Biomol. NMR Assign. 53, 199-201 (2011) 
  • Pfannkuche A, Büther K, Karthe J, Poenisch M, Bartenschlager R, Trilling M, Hengel H, Willbold D, Häussinger D, Bode JG 
    c-Src is required for complex formation between the hepatitis C virus encoded proteins NS5A and NS5B – a prerequisite for replication. 
    Hepatology 53, 1127-1136 (2011) 
  • Sabir T, Schröder GF, Toulmin A, McGlynn P, and Magennis SW 
    Global Structure of Forked DNA in Solution Revealed by High-Resolution Single-Molecule Fluorescence Resonance Energy Transfer. 
    J. Am. Chem. Soc. 135(5), 1188 (2011) 
  • Schünke S 
    NMR solution structures of the MloK1 cyclic nucleotide-gated ion channel binding domain. 
    Schriften des Forschungszentrums Jülich, Reihe Schlüsseltechnologien, Band 26 , (2011) 
    http://wwwzb.zb.kfa-juelich.de/publikationen/schriftreihe.asp?Schriftreihe=65  
  • Schünke S, Stoldt M, Lecher J, Kaupp UB, Willbold D 
    Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. 
    Proc. Natl. Acad. Sci. USA 108, 6121-6126 (2011) 
  • Schwarz CKW, Tschapek B, Jumpertz T, Jenewein S, Lecher J, Willbold D, Panjikar S, Halland B, Smits SHJ, Schmitt L 
    Crystallisation and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter Haemolysin B 
    Acta Cryst. F67, 630-633 (2011) 
  • Seebahn A, Dinkel H, Mohrlüder J, Hartmann R, Vogel N, Becker CM, Sticht H, Enz R 
    Structural characterization of intracellular C-terminal domains of group III metabotropic glutamate receptors 
    FEBS Lett 585, 511-516 (2011) 
  • Seehafer C, Kalweit A, Steger G, Gräf S, Hammann C 
    From alpaca to zebrafish: hammerhead ribozymes wherever you look 
    RNA 17, 21-26 (2011) 
    http://dx.doi.org/10.1261/rna.2429911  
  • Stöhr J, Elfrink K, Weinmann N, Wille H, Willbold D, Birkmann E and Riesner D 
    In vitro conversion of the posttranslationally modified prion protein. 
    Biol. Chem. 392, 415-421 (2011) 
  • van Groen T, Kadish I, Funke A and Willbold D 
    Staining of Amyloid Beta (Abeta) Using (Immuno) Histochemical Techniques and Abeta42 Specific Peptides 
    In: Neuroimaging for Clinicians - Combining Research and Practice. In Tech. Editor: Julio F. P. Peres; ISBN 978-953-307-450-4, Chapter 4 (2011) 
    free download  
  • VE Galkin, A Orlova, D Kudryashov, A Solodukhin, E Reisler, GF Schröder, and EH Egelman 
    Remodeling of Actin Filaments by ADF/Cofilin Proteins. 
    PNAS 108(51), 20568 (2011) 
  • Wagner R, Pul U 
    Mikrobielles "Immunsystem": Abwehr gegen Fremd-DNA durch das bakterielle CRISPR/Cas-System. 
    BIOspektrum 4, 393-395 (2011) 
  • Wang W, Dong H, Pacheco V, Willbold D, Zhang Y, Offenhausser A, Hartmann R, Weirich T, Ma P, Krause H, Gu Z 
    Relaxation behavior study of ultra-small superparamagnetic iron oxide nanoparticles at ultra-low and ultra-high magnetic fields. 
    J. Phys. Chem.B 115, 14789-14793 (2011) 
  • Zerrad L, Merli A, Schröder GF, Varga A, Gráczer E, Pernot P, Round A, Vas M, and Bowler MW 
    A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase. 
    JBC 286, 14040 (2011) 
  • Bartnik D, Funke SA, Andrei-Selmer L-C, Bacher M, Dodel R, Willbold D 
    Differently selected D-enantiomeric peptides act on different Aß species. 
    Rejuvenation Res. 13, 202-205 (2010) 
  • Batra-Safferling R, Granzin J, Moedder S, Hoffmann S, Willbold D 
    Structural studies of PI3K SH3 domain in complex with a peptide ligand: Role of anchor residue in ligand binding. 
    Biol. Chem. 391, 33-42 (2010) 
  • Bauer MS, Strodel B, Fejer SN, Koslover EF, Wales DJ 
    Interpolation Schemes for Peptide Rearrangements. 
    J. Chem. Phys. 132, (2010) 
  • Diermann N, Matousek J, Junge M, Riesner D, Steger G 
    Characterization of plant miRNAs and small RNAs derived from potato spindle tuber viroid (PSTVd) in infected tomato  
    Biol Chem 391, 1379-1390 (2010) 
    http://dx.doi.org/10.1515/BC.2010.148  
  • Funke SA, van Groen T, Kadish I, Bartnik D, Nagel-Steger L, Brener O, Sehl T, Batra-Safferling R, Moriscot C, Schoehn G, Horn AHC, Müller-Schiffmann A, Korth C, Sticht H, Willbold D 
    Oral Treatment with the D-Enantiomeric Peptide D3 Improves Pathology and Behavior of Alzheimer’s disease Transgenic Mice 
    ACS Chem. Neurosci. 1, 639-648 (2010) 
    http://dx.doi.org/10.1021/cn100057j  
    Highlighted in: Chemical & Engineering News, 88(33), August 16, 2010 
  • Funke SA, Wang L, Birkmann E, Willbold D 
    Single particle detection system for Aß: Adaptation of surface-FIDA to laser scanning microscopy. 
    Rejuvenation Res. 13, 206-209 (2010) 
  • Galkin VE, Orlova A, Schröder GF, Egelman EH 
    Structural Polymorphism in F-actin 
    Nat. Struct. Mol. Biol. , (2010) 
    http://dx.doi.org/10.1038/nsmb.1930  
  • Geißen, R, Steuten, B, Polen, T and Wagner, R 
    E. coli 6S RNA - a universal transcriptional regulator within the centre of growth adaptation. 
    RNA Biol. 7, (2010) 
  • Giuliodori AM, Di Pietro F, Marzi S, Masquida B, Wagner R, Romby P, Gualerzi CO and Pon CL 
    The cspA mRNA is a thermosensor that modulates translation of the cold-shock protein CspA. 
    Mol. Cell 37, 21-33 (2010) 
  • Glück JM, Hoffmann S, Koenig BW, Willbold D 
    Single Vector System for Efficient N-myristoylation of Recombinant Proteins in E. coli 
    PLoS ONE 5, e10081 (2010) 
    full text open access  
    The plasmids in this publication can be received via https://www.addgene.org/Dieter_Willbold/ 
  • Hoffmann S, Funke SA, Wiesehan K, Moedder S, Glück JM, Feuerstein S, Gerdts M, Moetter J, Willbold D 
    Competitively selected protein ligands pay theirs increase in specificity by a decrease in affinity. 
    Mol. BioSyst 6, 116-123 (2010) 
  • Klenin K, Strodel B, Wales DJ, Wenzel W 
    Modelling Proteins: Conformational Sampling and Reconstruction of Folding Kinetics 
    BBA-Proteins and Proteomics, in press , (2010) 
  • Kumar A, Heise H, Blommers MJJ, Krastel P, Schmitt E, Petersen F, Mandelkow EM, Carlomagno T, Griesinger C, Baldus M 
    Interaction of Epothilone B (Patupilone) with Microtubules, as Detected by Solid-State NMR Spectroscopy 
    Angew. Chem. Int. Ed. Engl. 49, 7504-7507 (2010) 
  • Liu HM, Funke SA, Willbold D 
    Transport of Alzheimer's disease amyloid-ß peptide binding D-amino acid peptides across a blood-brain barrier in vitro model. 
    Rejuvenation Res. 13, 210-213 (2010) 
  • Luers L, Panza G, Henke F, Aygenim T, Weiß J, Willbold D, Birkmann E 
    Amyloid formation: Age-related mechanism in Creutzfeldt-Jakob disease? 
    Rejuvenation Res. 13, 214-216 (2010) 
  • Luheshi LM, Hoyer W, de Barros TP, van Dijk-Härd I, Brorsson AC, Macao B, Persson C, Crowther DC, Lomas DA, Ståhl S, Dobson CM, Härd T 
    Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo 
    PLoS Biol. 8, e1000334 (2010) 
  • Ma P, Mohrlüder J, Schwarten M, Stoldt M, Singh SK, Hartmann R, Pacheco V, Willbold D 
    Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy 
    Chembiochem 11, 1967-1970 (2010) 
  • Merdanovic M, Mamant N, Meltzer M, Poepsel S, Auckenthaler A, Melgaard R, Hauske P, Nagel-Steger L, Clarke AR, Kaiser M, Huber R, Ehrmann M 
    Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. 
    Nat. Struct. Mol. Biol. 17, 837-843 (2010) 
    http://dx.doi.org/10.1038/nsmb.1839  
    http://www.nature.com/nsmb/journal/v17/n7/full/nsmb.1839.html  
  • Mötter J 
    Identifizierung von Interaktionspartnern für HIV-1 Nef und ihre potentielle Relevanz bei der Entwicklung der HIV-assoziierten Demenz 
    Schriften des Forschungszentrums Jülich Reihe Gesundheit, Band 19, (2010) 
    http://dmssrv.zb.kfa-juelich.de/w2p2/tmp/65BABBA2-3F48-4BB4-8276-7624B2D91FB4/Gesundheit_19.pdf  
  • Müller-Schiffmann A, März-Berberich J, Andrjevna A, Rönicke R, Bartnik D, Brener O, Kutzsche J, Horn AHC, Hellmert M, Polkowska J, Gottmann K, Reymann K, Funke SA, Nagel-Steger L, Moriscot C, Schoehn G, Sticht H, Willbold D, Schrader T, Korth C 
    Combining independent drug classes into superior, synergistically acting hybrid molecules. 
    Angew. Chem. Int. Ed. Engl. 49, 8743-8746 (2010) 
    http://dx.doi.org/10.1002/anie.201004437  
  • Nagel-Steger L, Demeler B, Meyer-Zaika W, Hochdörffer K, Schrader T, Willbold D 
    Modulation of aggregate size- and shape-distributions of the amyloid-beta peptide by a designed ß-sheet breaker. 
    Eur. Biophys. J. 39, 415-422 (2010) 
    http://dx.doi.org/10.1007/s00249-009-041  
  • Neußer T, Polen T, Geißen R and Wagner R 
    Depletion of the non-coding regulatory 6S RNA in E. coli causes a surprising reduction in the expression of the translation machinery. 
    BMC Genomics 11, 165-179 (2010) 
  • Pacheco V, Ma P, Thielmann Y, Hartmann R, Weiergräber OH, Mohrlüder J, Willbold D 
    Assessment of GABARAP self-association by its diffusion properties 
    J Biomol NMR 48, 49-58 (2010) 
  • Panza G, Dumpitak C, Birkmann E 
    Amyloid formation: Influence of the Maillard Reaction to Prion Protein Aggregation. 
    Rejuvenation Res. 13, 220-223 (2010) 
  • Panza G, Luers L, Stöhr J, Nagel-Steger L, Weiβ J, Riesner D, Willbold D, Birkmann E 
    Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro. 
    PLoS ONE 5, e14283 (2010) 
    http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0014283  
  • Pul U, Wurm R, Arslan Z, Geißen R, Hofmann N and Wagner R 
    Identification and Characterization of E. coli CRISPR-cas Promoters and their Silencing by H-NS. 
    Mol. Microbiol 75, 1495-1512 (2010) 
    http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07073.x/abstract  
  • Schröder GF, Levitt M, Brunger AT 
    Super-resolution biomolecular crystallography with low-resolution data 
    Nature 464, 1218-1222 (2010) 
  • Schünke S, Lecher J, Stoldt M, Kaupp UB, Willbold D 
    Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain. 
    Biomol. NMR Assign. 4, 147-150 (2010) 
  • Schwarten M, Stoldt M, Mohrlüder J, Willbold D 
    Solution structure of Atg8 reveals conformational polymorphism of the N-terminal domain 
    Biochem Biophys Res Commun 395, 426-431 (2010) 
  • Smits SHJ, Meyer T, Mueller A, van Os N, Stoldt M, Willbold D, Schmitt L, Grieshaber MK 
    Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography 
    PLoS ONE 5, e12312 (2010) 
    http://dx.doi.org/10.1371/journal.pone.0012312  
    http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0012312  
  • Strodel B, Lee JWL, Whittleston CS, Wales DJ 
    Transmembrane structures for Alzheimer's Aβ1-42 oligomers. 
    J. Am. Chem. Soc. , (2010) 
  • Teune, J-H, Steger G 
    novoMIR: de novo prediction of microRNA-coding regions in a single plant genome. 
    J. Nucleic Acids 2010, (2010) 
    http://dx.doi.org/10.4061/2010/495904  
  • Westra E R, Pul U, Heidrich N, Jore M M, Lundgren M, Stratmann T, Wurm R, Raine A, Mescher M, van Heereveld L, Mastop M, Wagner E G H, Schnetz K, van der Oost J, Wagner R and Brouns S J J 
    H-NS mediated repression of CRISPR-based immunity in Escherichia coli K12 can be relieved by the transcription activator LeuO. 
    Mol. Microbiol. 77, 1380-1393 (2010) 
    http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2010.07315.x/abstract  
    Highlighted in: Mol Microbiol. 2010 Sep;77(6):1341-5 
  • Wittlich M, Thiagarajan P, Koenig BW, Hartmann R, Willbold D 
    NMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles. 
    Biochim Biophys Acta 1798, 122-127 (2010) 
  • Wurm R , Neußer T, Wagner R 
    6S RNA-dependent inhibition of RNA polymerase is released by RNA-dependent synthesis of small de novo products. 
    Biol. Chem. 39, 187-196 (2010) 
  • Zhang J, Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W 
    Mechanism of folding chamber closure in a group II chaperonin 
    Nature 463, 379-383 (2010) 
  • Brown JW, Birmingham A, Griffiths PE, Jossinet F, Kachouri-Lafond R, Knight R, Lang BF, Leontis N, Steger G, Stombaugh J, Westhof E 
    The RNA structure alignment ontology.  
    RNA 15, 1623-1631 (2009) 
    http://dx.doi.org/10.1261/rna.1601409  
  • Demeler B, Brookes E, Nagel-Steger L  
    Analysis of heterogeneity in molecular weight and shape by analytical ultracentrifugation using parallel distributed computing. 
    Meth. Enzymol. 454, 87-113 (2009) 
    http://dx.doi.org/10.1016/S0076-6879(08)03804-4  
  • Feuerstein SE, Pulvermüller A, Hartmann R, Granzin J, Stoldt M, Henklein P, Ernst OP, Heck M, Willbold D, Koenig BW 
    Helix formation in Arrestin accompanies recognition of photoactivated Rhodopsin. 
    Biochemsitry 48, 10733-42 (2009) 
  • Fu Y, Bannach O, Chen H, Teune JH, Schmitz A, Steger G, Xiong L, Barbazuk WB 
    Alternative Splicing of Anciently Exonized 5S rRNA Regulates Plant Transcription Factor TFIIIA. 
    Genome Research 19, 913-21 (2009) 
    http://dx.doi.org/10.1101/gr.086876.108  
  • Funke SA, Birkmann E, Willbold D 
    Detection of Amyloid-β aggregates in body fluids: A suitable method for early diagnosis of Alzheimer's diesease? 
    Curr. Alzheimer Res. 6, 285-289 (2009) 
  • Funke SA, Willbold D 
    Mirror image phage display - a method to generate D-peptide ligands for use in diagnostic or therapeutical applications? 
    Mol. BioSyst. 5, 783-786 (2009) 
  • Glück JM, Wittlich M, Feuerstein S, Hoffmann S, Willbold D, Koenig BW 
    Integral membrane proteins in nanodiscs can be studied by solution NMR spectroscopy. 
    J. Am. Chem. Soc. 131, 12060-61 (2009) 
  • Görtz P, Opatz J, Siebler M, Funke SA, Willbold D, Lange-Asschenfeldt C 
    Transient reduction of spontaneous neuronal network activity by sublethal amyloid beta (1-42) peptide concentrations. 
    J. Neural Transmission 116, 351-355 (2009) 
  • Karpinar DP, Balija MBG, Kügler S, Opazo F, Rezaei-Ghaleh N, Bender N, Kim HY, Taschenberger G, Falkenburger BH, Heise H, Kumar A, Riedel D, Fichtner L, Voigt A, Braus GH, Giller K, Becker S, Herzig A, Baldus M, Jäckle H, Eimer S, Schulz JB, Griesinger C, Zweckstetter M 
    Pre-fibrillar a-Synuclein Variants with Impaired beta-Structure Increase Neurotoxicity in Parkinson`s Disease Models 
    EMBO J. 28, 3256-3268 (2009) 
  • Leliveld SR, Hendriks P, Michel M, Sajnani G, Bader V, Trossbach S, Prikulis I, Hartmann R, Jonas E, Willbold D, Requena JR, Korth C 
    Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C. 
    Biochemistry 48, 7746-7755 (2009) 
  • Mangels C, Frank AO, Ziegler J, Klingenstein R, Schweimer K, Willbold D, Korth C, Rösch P, Schwarzinger S 
    Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules. 
    J. Biomol. Struct. Dyn. 27, 163-170 (2009) 
  • Mohrlüder J, Schwarten M, Willbold D 
    Structure and potential function of gamma-aminobutyrate type A receptor-associated protein 
    FEBS J 276, 4989-5005 (2009) 
  • Müller-Schiffman A, Petsch B, Leliveld SR, Muyrers J,Salwierz A, Mangels C, Schwarzinger S, Riesner D, Stitz L, Korth C 
    Complementarity determining regions of an anti-prion protein scFv fragment orchestrate conformation specificity and antiprion activity 
    Molecular Immunology 46 4, 532 - 540 (2009) 
  • Schlenzig D, Manhart S, Cinar Y, Willbold D, Funke SA, Kleinschmidt M, Hause G, Schilling S, Demuth H-U 
    Pyroglutamate formation influences solubility and amyloidenicity of amyloid peptides. A driving force in different neurodegenerative disorders? 
    Biochemistry 48, 7072-7078 (2009) 
  • Schünke S, Stoldt M, Novak K, Kaupp UB, Willbold D 
    Solution structure of the M.loti K1 channel cyclic nucleotide binding domain in complex with cAMP. 
    EMBO Rep. 10, 729-735 (2009) 
  • Schwarten M, Mohrlüder J, Ma P, Stoldt M, Thielmann Y, Stangler T, Hersch N, Hoffmann B, Merkel R, Willbold D 
    Nix directly binds to GABARAP: a possible crosstalk between apoptosis and autophagy 
    Autophagy 5, 690-698 (2009) 
  • Schwarten M, Stoldt M, Mohrlüder J, Willbold D 
    Sequence-specific 1H, 13C, and 15N resonance assignment of the autophagy-related protein Atg8 
    Biomol NMR Assign 3, 137-139 (2009) 
  • Thielmann Y, Weiergräber OH, Ma P, Schwarten M, Mohrlüder J, Willbold D 
    Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE-16 
    Proteins 77, 637-646 (2009) 
  • Thielmann Y, Weiergräber OH, Mohrlüder J, Willbold D 
    Structural characterization of GABARAP-ligand interactions 
    Mol Biosyst 5, 575-579 (2009) 
  • Thielmann Y, Weiergräber OH, Mohrlüder J, Willbold D 
    Structural framework of the GABARAP-calreticulin interface - implications for substrate binding to endoplasmic reticulum chaperones 
    FEBS J 276, 1140-1152 (2009) 
  • van Groen T, Kadish I, Wiesehan K, Funke, SA, Willbold D 
    In vitro and in vivo staining characteristics of small, fluorescent, Aß42 binding D-enantiomeric peptides in transgenic AD mouse models. 
    ChemMedChem 4, 276-282 (2009) 
  • Wagner R 
    Translational Components in Prokaryotes: Genetics and Regulation of Ribosomes. 
    In: ENCYCLOPEDIA OF LIFE SCIENCES. John Wiley & Sons, Ltd: Chichester , (2009) 
    http://www.els.net/  
    [DOI: 10.1002/9780470015902.a0000538.pub2] 
  • Wagner R 
    ppGpp Signaling. 
    in Bacterial Signaling, Kraemer, R. and Jung, K. (Eds.) , (2009) 
    Wiley-VCH, Weinheim, ISBN: 978-3-527-32365. 
  • Wagner R, Pul U 
    Nucleoid-associated proteins – structural properties. 
    In Bacterial Chromatin, Dame, R. T. and Dorman, C. J. (Eds.), 2009, Springer , (2009) 
    http://dx.doi.org/10.1007/978-90-481-3473-1_8  
  • Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D 
    NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. 
    FEBS J. 276, 6560-75 (2009) 
  • Bailly A, Sovero V, Vincenzetti V, Santelia D, Bartnik D, Koenig BW, Mancuso S, Martinoia E, Geisler M  
    Modulation of P-glycoproteins by auxin transport inhibitors is mediated by interaction with immunophilins.  
    J. Biol. Chem. 283, 21817-26 (2008) 
  • Birkmann E & Riesner D 
    Prion infection – seeded fibrillization or more? 
    Prion 2, 67-72 (2008) 
  • Birkmann E, Funke SA, Riesner D, Willbold D 
    Single particle Detection - a diagnostic tool for particle associated diseases like Alzheimer’s disease and Creutzfeldt-Jakob disease, 
    INSTICC, Proceedings of Biosignals 2, 431-436 (2008) 
  • Birkmann E, Henke F, Funke SA, Bannach O, Riesner D, Willbold D 
    A highly sensitive diagnsotic assay for aggregate-related diseases e.g. prion disease and Alzheimer's disease. 
    Rejuvenation Res. 11, 359-363 (2008) 
  • Cisneros D, Oberbarnscheidt L, Pannier A, Klare J, Helenius J, Engelhard M, Oesterhelt F, Müller D J 
    Transducer binding establishes localized interactions that tune sensory rhodopsin II 
    Structure 16, 1206-13 (2008) 
  • Elfrink K, Ollesch J, Stoehr J, Willbold D, Riesner D, Gerwert K 
    Structural changes of PrPc upon membrane anchoring. 
    Proc. Natl. Acad. Sci. 105, 10815-10819 (2008) 
  • Funke SA, Birkmann E, Henke F, Görtz P, Lange-Asschenfeldt C, Riesner D, Willbold D 
    An ultra sensitive assay for early diagnosis of Alzheimer's disease. 
    Rejuvenation Res. 11, 315-318 (2008) 
  • Gardiennet C, Loquet A, Etzkorn M, Heise H, Baldus M, Böckmann A 
    Structural constraints for the Crh protein from solid-state NMR experiments. 
    J. Biomol. NMR 40, 239-250. (2008) 
  • Hartmann R, Koenig BW, Stangler T, Willbold D 
    Structural Proteomics: Exploring Protein-Ligand Interactions by Solution NMR. 
    in 'Proteomics Sample Preparation', J. v. Hagen, Wiley-VCH , 273-281 (2008) 
  • Heise H 
    Solid-State NMR Spectroscopy of Amyloid Proteins. 
    ChemBioChem 9, 179-189 (2008) 
  • Heise H, Celej MS, Becker S, Riedel D, Pelah A, Kumar A, Jovin TM, Baldus M 
    Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein 
    J. Mol. Biol. 380, 444-450 (2008) 
  • Kaimann T, Metzger S, Kuhlmann K, Brandt B, Birkmann E, Höltje HD, Riesner D 
    Molecular model of an alpha-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. 
    J.Mol.Biol. 376, 582-596 (2008) 
  • Matoušsek J, Orctová L, ŠSkopek J, Pesšina K, Steger G 
    Elimination of hop latent viroid upon developmental activation of pollen nucleases. 
    Biol. Chem. 389, 905-918 (2008) 
    http://dx.doi.org/10.1515/BC.2008.096  
  • Mueller CB, Loman A, Pacheco V, Koberling F, Willbold D, Richtering W, Enderlein J 
    Precise measurement of diffusion by multi-color dual-focus fluorescence correlation spectroscopy. 
    Europhys. Lett. 83, 46001 (2008) 
  • Müller H, Stitz L, Riesner D  
    Prion decontamination during the oleochemical process of fat hydrogenation. 
    Eur J Lipid Sci Technol 110, 392-399 (2008) 
    http://dx.doi.org/10.1002/ejlt.200700171  
  • Nagel-Steger L, Demeler B, Hochdörfer K, Schrader T, Willbold D 
    Modulation of aggregate size and shape distributions of amyloid-ß peptide solutions by a designed ß-sheet breaker. 
    NIC Workshop 2008 (From Computational Biophysics to Systems Biology; CBSB08) Vol. 40, (2008) 
    http://www.fz-juelich.de/nic-series/volume40/nagel_steger.pdf  
  • Neußer T , Gildehaus N, Wurm R and Wagner R 
    Studies on the expression of 6S RNA from E. coli: involvement of regulators important for stress and growth adaptation. 
    Biol. Chem. 389, 285-297 (2008) 
  • Panza G, Stöhr J, Birkmann E, Riesner D, Willbold D, Baba O, Terashima T, Dumpitak C 
    Aggregation and amyloid fibril formation of the prion protein is accelerated in presence of glycogen. 
    Rejuvenation Res. 11, 365-369 (2008) 
  • Panza G, Stöhr J, Dumpitak C, Papathanassiou D, Weinmann N, Weiß J, Riesner D, Willbold D, Birkmann E 
    Spontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine Prion Protein. 
    Biochem. Biophys. Research Comm. 373, 493.497 (2008) 
  • Pul U, Lux B, Wurm R, Wagner R 
    Effect of upstream curvature and transcription factors H-NS and LRP on the efficiency of E. coli rRNA promoters P1 and P2 - A phasing analysis. 
    Microbiology 154, 2533-2545 (2008) 
    Highlighted in: Microbiology Today, Hot of the Press Nov 2008 
  • Stöhr J, Weinmann N, Wille H, Kaimann T, Nagel-Steger L, Birkmann E, Panza G, Prusiner SB, Eigen M, Riesner D 
    Mechanisms of prion protein assembly into amyloid. 
    Proc. Natl. Acad. Sci. U S A 105, 2409-2414 (2008) 
    http://dx.doi.org/10.1073/pnas.0712036105  
  • Thielmann Y, Mohrlüder J, Koenig BW, Stangler T, Hartmann R, Becker K, Höltje HD, Willbold D 
    An indole binding site is a major determinant of the ligand specificity of the GABA type A receptor-associated protein GABARAP 
    Chembiochem 9, 1767-1775 (2008) 
  • Tiffert Y, Supra P, Wurm R, Wohlleben W, Wagner R and Reuther J 
    The Streptomyces coelicolor GlnR regulon: identification of new GlnR targets and evidence for a central role of GlnR in nitrogen metabolism in actinomycetes. 
    Mol. Microbiol. 67, 861-880 (2008) 
  • van Groen T, Wiesehan K, Funke SA, Kadish I, Nagel-Steger L, Willbold D 
    Reduction of Alzheimer's disease amyloid plaque load in transgenic mice by D3, a D-enantiomeric peptide identified by mirror image phage display. 
    ChemMedChem 3, 1848-1852 (2008) 
    http://dx.doi.org/10.1002/cmdc.200800273  
    [This article was evaluated by the faculty of 1000 Biology as a "must read"]  
  • Weiergräber OH, Stangler T, Thielmann Y, Mohrlüder J, Wiesehan K, Willbold D 
    Ligand binding mode of GABAA receptor-associated protein 
    J Mol Biol 381, 1320-1331 (2008) 
  • Wiesehan K, Stöhr J, Nagel-Steger K, van Groen T, Riesner D and Willbold D 
    Inhibition of cytotoxicity and fibril formation by a D-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide 
    Prot. Eng. Des. Sel. 21, 241-246 (2008) 
    http://dx.doi.org/10.1093/protein/gzm054  
  • Wilm A, Linnenbrink K, Steger G 
    ConStruct: improved construction of RNA consensus structures 
    BMC Bioinformatics 9, 219 (2008) 
    http://dx.doi.org/10.1186/1471-2105-9-219  
  • Wittlich M, Koenig BW, Willbold D 
    Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV-1 VpU. 
    J. Pept. Sci. 14, 804-10 (2008) 
  • Birkmann E, Henke F, Weinmann N, Dumpitak C, Groshup M, Funke SA, Willbold D, Riesner D, 
    Counting of single prion particles bound to a capture-antibody surface (surface-FIDA), 
    Vet. Microbiol. 123, 294-304 (2007) 
  • Censarek P, Steger G, Paolini C, Hohlfeld T, Grosser T, Zimmermann N, Fleckenstein D, Schrör K, Weber A-A 
    Alternative splicing of platelet cyclooxygenase-2 mRNA in patients after coronary artery bypass grafting 
    Thrombosis and Haemostasis 98, 1309-1315 (2007) 
    http://dx.doi.org/10.1160/TH07-05-0346  
  • Elfrink K, Nagel-Steger L, Riesner D 
    Interaction of the cellular prion protein with raft-like lipid membranes. 
    Biol. Chem. 388, 79-90 (2007) 
    http://dx.doi.org/10.1515/BC.2007.010, 01/01/2007  
  • Funke SA, Birkmann E, Henke F, Görtz P, Lange-Asschenfeldt C, Riesner D, Willbold D, 
    Single particle detection of amyloid-ß aggregates associated with Alzheimer's disease. 
    Biochem. Biophys. Res. Comm. 364, 902-907 (2007) 
  • Gildehaus N, Neußer T, Wurm R and Wagner R 
    Studies on the function of the riboregulator 6S RNA from E. coli: RNA polymerase binding, inhibition of in vitro transcription and synthesis of RNA-directed de novo transcripts 
    Nucleic Acids Research 35, 1885–1896 (2007) 
    [This article was evaluated by the faculty of 1000 Biology] 
  • Hänel K, Willbold D 
    SARS-CoV accessory protein 7a directly interacts with human LFA-1. 
    Biol. Chem. 388, 1325-1332 (2007) 
  • Hoffmann S, Jonas E, Konig S, Preusser-Kunze A, Willbold D 
    Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus. 
    Biol. Chem. 366, 181-183 (2007) 
  • Koenig BW 
    Residual dipolar couplings report on the active conformation of rhodopsin-bound protein fragments. 
    In: 'Topics in Current Chemistry', vol. 272, Bioactive Conformation I. T. Peters, editor. Springer-Verlag Berlin Heidelberg , 187-215 (2007) 
  • Matoušek J, Kozlová P, Orctová L, Schmitz A, Pesina K, Bannach O, Diermann N, Steger G, Riesner D 
    Accumulation of viroid-specific small RNAs and increase in nucleolytic activities linked to viroid-caused pathogenesis. 
    Biol. Chem. 388, 1-13 (2007) 
    http://dx.doi.org/10.1515/BC.2007.0  
  • Matoušek J, Orctová L, Ptácek J, Patzak J, Dedic P, Steger G, Riesner D 
    Experimental transmission of Pospiviroid populations to weed species characteristic for potato and hop fields. 
    J. Virol. 81, 11891-11899 (2007) 
    http://dx.doi.org/10.1128/JVI.01165-07  
  • Mittelbach M, Pokits B, Müller H, Müller M & Riesner D 
    Risk Assessment for prion protein reduction under the conditions of the biodiesel production process. 
    Eur J Lipid Sci Technol. 109, 79-90 (2007) 
  • Mohrlüder J, Hoffmann Y, Stangler T, Hänel K, Willbold D 
    Identification of clathrin heavy chain as a direct interaction partner for the gamma-aminobutyric acid type A receptor associated protein 
    Biochemistry 46, 14537-14543 (2007) 
  • Mohrlüder J, Stangler T, Wiesehan K, Hoffmann Y, Mataruga A, Willbold D 
    Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library 
    FEBS J 274, 5543-5555 (2007) 
  • Muhs A, Hickmann DT, Pihlgren M, Chuard N, Giriens V, Meerschman C, van der Auwera I, van Leuven F, Sugawara M, Weingertner MC, Bechinger B, Greferath R, Kolonko N, Nagel-Steger L, Riesner D, Brady RO, Pfeifer A, Nicolau C 
    Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice 
    Proc. Natl. Acad. Sci. 104, 9810-9815 (2007) 
    http://dx.doi.org/10.1073/pnas.0703137104  
  • Müller H, Stitz L, Wille H, Prusiner SB, Riesner D 
    Influence of water, fat, and glycerol on the mechanism of thermal prion inactivation. 
    J Biol Chem 282, 35855-35867 (2007) 
    http://dx.doi.org/10.1074/jbc.M706883200  
  • Nagel-Steger L, Demeler B, Willbold D 
    Aggregate size and shape distributions in amyloid-ß peptide solutions. Aggregate Size and Shape Distributions in Amyloid-beta Peptide Solutions. 
    NIC Workshop (From Computational Biophysics to Systems Biology; CBSB07) Vol. 36, (2007) 
    http://www.fz-juelich.de/nic-series/volume36/nagel-steger.pdf  
  • Pul U, and Wagner R 
    Nukleoid-assoziierte Proteine bei Mikroorganismen. 
    Biospektrum 5, 495-497 (2007) 
  • Pul U, Wurm R and Wagner R 
    The Role of LRP and H-NS in Transcription Regulation: Involvement of Synergism, Allostery and Macromolecular Crowding 
    J. Mol. Biol. 366, 900–915 (2007) 
  • Scheidt HA, Vogel A, Eckhoff A, Koenig BW, Huster D 
    Solid state NMR characterization of the putative membrane anchor of TWD1 from Arabidopsis thaliana. 
    Eur. Biophys. J. 36, 393-404 (2007) 
  • Schmidt H, Hoffmann S, Tran T, Stoldt M, Stangler T, Wiesehan K, Willbold D 
    Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes. 
    J. Mol. Biol. 365, 1517-1532 (2007) 
  • Schmitz M, Steger G 
    Potato spindle tuber viroid (PSTVd). 
    Plant viruses. 1, 106-115 (2007) 
  • Schünke S, Novak K, Stoldt M, Kaupp UB, Willbold D 
    Resonance assignment of the cyclic nucleotide binding domain from a cyclic nucleotide-gated K+ channel in complex with cAMP. 
    Biomol. NMR Assign. 1, 179-181 (2007) 
  • Skegro D, Pulvermüller A, Krafft B, Granzin J, Hofmann KP, Büldt G, Schlesinger R 
    N-terminal and C-terminal domains of arrestin both contribute in binding to rhodopsin. 
    Photochem Photobiol. 83(2), 385-92 (2007) 
  • Spiess HW, Jeschke G, Koenig BW, Willbold D 
    Magnetische Resonanzspektroskopie. 
    Nachr. Chemie 55, 288-293 (2007) 
  • Stangler T, Hartmann R, Willbold D, Koenig BW 
    Modern high resolution NMR for the study of structure, dynamics and interactions of biological macromolecules. 
    In: 'Progress in Physical Chemistry', Vol. 1 / Different Aspects of Intermolecular Interaction, Oldenbourg, München , 111-157 (2007) 
  • Stangler T, Tran T, Hoffmann S, Schmidt H, Jonas E, Willbold D 
    Competitive displacement of full-length HIV-1 Nef from Hck SH3 domain by a high affinity artificial peptide. 
    Biol. Chem. 388, 611-615 (2007) 
  • Stellbrink J, Niu AZ, Allgaier J, Richter D, Koenig BW, Hartmann R, Coates GW, Fetters LJ 
    Analysis of polymeric methylaluminoxane (MAO) via small angle neutron scattering. 
    Macromolecules 40, 4972-81 (2007) 
  • Wiesehan K, Funke SA, Fries M, Willbold D 
    Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide. 
    J. Chrom. B 856, 229-233 (2007) 
  • Wittlich M, Koenig BW, Hoffmann S, Willbold D 
    Structural characterisation of the transmembrane and cytoplasmic domains of human CD4. 
    Biochim Biophys Acta 1768, 2949-60 (2007) 
  • Wittlich M, Wiesehan K, Koenig BW, Willbold D 
    Expression, purification, and membrane reconstitution of a CD4 fragment comprising the transmembrane and cytoplasmic domains of the receptor. 
    Protein Expr. Purif. 55, 198-207 (2007) 
  • Batra-Safferling R, Abaraca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB 
    Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. 
    J Biol Chem 281, 1449-1460 (2006) 
  • Birkmann E, Schafer O, Weinmann N, Dumpitak C, Beekes M, Jackman R, Thorne L, Riesner D 
    Detection of prion particles in samples of BSE and scrapie by fluorescence correlation spectroscopy without proteinase K digestion. 
    Biol Chem. 387, 95-102 (2006) 
  • Dalli D, Wilm A, Mainz I, Steger, G 
    STRAL: Progressive alignment of non-coding RNA using base pairing probability vectors in quadratic time. 
    Bioinformatics 22, 1593-1599 (2006) 
    https://doi.org/10.1093/bioinformatics/btl142  
  • Gräf S, Teune J-H, Strothmann D, Kurtz S, Steger, G 
    A computational approach to search for non-coding RNAs in large genomic data. 
    In Nellen, W. & Hammann, C. (Hrsg.), Small RNAs: Analysis and Regulatory functions., Nucleic Acids and Molecular Biology Series, Band 17. Springer Verlag , 74-75 (2006) 
  • Hänel K, Stangler T, Stoldt M, Willbold D 
    Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains. 
    J. Biomed. Sci. 13, 281-293 (2006) 
  • Hörnlimann B, Schulz-Schaeffer W, Oberthür R, Müller H & Riesner D 
    Chemicaldisinfection and inactivation of prions. 
    In: Prions and prion diseases. Edited by Hörnlimann B, Riesner D & Kretzschmar H. Berlin New York: Walter de Gruyter. , 505-515 (2006) 
  • Kolonko N, Bannach O, Aschermann K, Hu KH, Moors M, Schmitz M, Steger G, Riesner, D 
    Transcription of potato spindle tuber viroid by RNA polymerase II starts in the left terminal loop. 
    Virology 347, 392-404 (2006) 
    http://dx.doi.org/10.1016/j.virol.2005.11.039  
  • Lemaitre V, Wray V, Willbold D, Watts A, Fischer WB 
    Full length Vpu from HIV-1: Combining molecular dynamics simulations with NMR spectroscopy. 
    J. Biomol. Struct. Dyn. 23, 485-496 (2006) 
  • Marszalkowski M, Teune J-H, Steger G, Hartmann RK, Willkomm, DK 
    Thermostable RNase P RNAs lacking P18 identified in the Aquificales. 
    RNA 12, 1915-1921 (2006) 
    http://dx.doi.org/10.1261/rna.242806  
  • Müller H, Stitz L & Riesner D: 
    Risk assessment for fat derivatives in case of contamination with BSE. 
    Eur J Lipid Sci Technol. 108, 812-826 (2006) 
  • Oberthür R, Müller H & Riesner D 
    Thermal inactivation of prions. 
    In: Prions and prion diseases. Edited by Hörnlimann B, Riesner D & Kretzschmar H. Berlin New York: Walter deGruyter. , 516-526 (2006) 
  • Psurek A, Feuerstein S, Willbold D, Scriba GKE 
    Effects of the secondary structure of amphiphilic a-helical peptides on separation selectivity in nonaqueous compared to aqueous capillary electrophoresis. 
    Electrophoresis 27, 1868-1775 (2006) 
  • Riesner, D, Birkmann E, Dumpitak C, Elfrink K, Kellings K, Leffers K-W, Nagel-Steger L, Stöhr J 
    PrP-Fibrillen und Infektiosität 
    Nova Acta Leopoldina 347, 61-77 (2006) 
  • Schmitz A, Riesner D 
    Purification of nucleic acids by selective precipitation with polyethylene glycol 6000. 
    Anal Biochem. 354, 311-313 (2006) 
  • Schwarzinger S, Willbold D, Ziegler J 
    Structural Studies of Prion Proteins. 
    in 'Prions and prion diseases', B. Hörnlimann, D. Riesner, H. Kretzschmer,eds. de Gruyter, Berlin , (2006) 
  • Stangler T, Hartmann R, Willbold D, Koenig BW 
    Modern high resolution NMR for the study of structure, dynamics and interactions of biological macromolecules. 
    Z. Phys. Chem. 220, 567-613 (2006) 
  • Wagner R 
    Protein-Nucleinsäure Wechselwirkungen. 
    in Bioanalytik, Lottspeich, F. and Engels, J. W., Spektrum-Akademischer Verlag , (2006) 
  • Wilm A, Mainz I, Steger G 
    An enhanced RNA alignment benchmark for sequence alignment programs. 
    Algorithms Mol Biol 1, 19 (2006) 
    http://dx.doi.org/10.1186/1748-7188-1-19  
  • Briese L, Preusser A, Willbold D 
    Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy. 
    J. Biomed. Sci. 12, 451-456 (2005) 
  • Dumpitak C, Beekes M, Weinmann N, Metzger S, Winklhofer KF, Tatzelt J, Riesner D 
    The polysaccharide scaffold of PrP 27-30 is a common compound of natural prions and consists of alpha-linked polyglucose. 
    Biol Chem. 386, 1149-1155 (2005) 
  • Gardner PP, Wilm A, Washietl, S 
    A benchmark of multiple sequence alignment programs upon structural RNAs. 
    Nucleic Acids Res. 33, 2433-2439 (2005) 
    http://dx.doi.org/10.1093/nar/gki541  
  • Gräf S, Przybilski R, Steger G, Hammann C 
    A database search for hammerhead ribozyme motifs. 
    Biochem. Soc. Trans. 33, 477-478 (2005) 
    Publisher  
  • Harrer E, Bäuerle M, Ferstl B, Chaplin P, Petzold B, Mateo L, Handley A, Tzatzaris M, Vollmar J, Bergmann S, Rittmaier M, Eismann K, Müller S, Kalden JR, Spriewald B, Willbold D, Harrer T 
    Therapeutic vaccination of HIV-1-infected patients on HAART with a recombinant HIV-1 nef-expressing MVA: safety, immunogenicity and influence on viral load during treatment interruption. 
    Antiviral Therapy 10, 285-300 (2005) 
  • Hillebrand A, Wurm R, Menzel A, Wagner R 
    The seven E. coli ribosomal RNA operon upstream regulatory regions differ in structure and transcription factor binding efficiencies. 
    Biol Chem. 386, 523-534 (2005) 
  • Koenig BW, Gawrisch K 
    Lipid ethanol interaction studied by NMR on bicelles. 
    J. Phys. Chem. B. 109, 7540-47 (2005) 
  • Koenig BW, Gawrisch K 
    Specific volumes of unsaturated phosphatidylcholines in the liquid crystalline lamellar phase. 
    Biochim Biophys Acta. 1715, 65-70 (2005) 
  • Leffers KW, Wille H, Stohr J, Junger E, Prusiner SB, Riesner D 
    Assembly of natural and recombinant prion protein into fibrils. 
    Biol Chem. 386, 569-580 (2005) 
  • Müller H, Riesner D: 
    Thermal degradation of prions in presence of fats: implication for oleochemical processess. 
    Eur J Lipid Sci Technol. 107, 833-839 (2005) 
  • Müller H, Strom A, Hunsmann G, Stuke AW 
    Separation of native prion protein (PrP)glycoforms by copper-binding using immobilized metal affinity chromatography (IMAC). 
    Biochem J. 388, 371-378 (2005) 
  • Niu AZ, Stellbrink J, Allgaier J, Willner L, Radulescu A, Richter D, Koenig BW, May RP, Fetters LJ 
    An in situ study of the t-butyllithium initiated polymerization of butadiene in d-heptane via small angle neutron scattering and H-NMR. 
    J. Chem. Phys. 122, 134906 (2005) 
  • Przybilski R, Gräf S, Lescoute A, Nellen W, Westhof E, Steger G, Hammann, C 
    Functional hammerhead ribozymes naturally encoded in the genome of Arabidopsis thaliana. 
    Plant Cell 17, 1877-1885 (2005) 
    http://dx.doi.org/10.1105/tpc.105.032730  
  • Pul U, Wurm R, Lux B, Meltzer M, Menzel A, Wagner R 
    LRP and H-NS--cooperative partners for transcription regulation at Escherichia coli rRNA promoters. 
    Mol Microbiol. 58, 864-876 (2005) 
  • Tran T, Hoffmann S, Wiesehan K, Jonas E, Luge C, Aladag A, Willbold D 
    Insights into human Lck SH3 domain binding specificity: different binding modes of artificial and native ligands. 
    Biochemistry 44, 15042-15052 (2005) 
  • Willbold D 
    Interaction of HIV-1 Nef with human CD4 and Lck. 
    in 'Viral membrane proteins: structure, function and drug design', W. Fischer, ed. Kluwer Academic Publishers, New York , (2005) 
  • Elfrink, K and Riesner, D 
    Purification of PrPC. In: Techniques in Prion Research, 
    S. Lehmann and J. Grassi eds. (Basel, Switzerland: Birkhaeuser Verlag) , 4–15 (2004) 
  • Gräf S, Borisova BE, Nellen W, Steger G, Hammann, C 
    A database search for double-strand containing RNAs in Dictyostelium discoideum. 
    Biol. Chem. 385, 961-965 (2004) 
    http://dx.doi.org/10.1515/BC.2004.125  
  • Khayat R, Batra R, Bebernitz GA, Olson MW, Tong L 
    Characterization of the monomer-dimer equilibrium of human cytomegalovirus protease by kinetic methods. 
    Biochemistry 43(2), 316-22 (2004) 
  • Leffers KW, Schell J, Jansen K, Lucassen R, Kaimann T, Nagel-Steger L, Tatzelt J, Riesner D 
    The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. 
    J Mol Biol 344, 839-853 (2004) 
    http://dx.doi.org/10.1016/j.jmb.2004.09.071  
  • Matoušek J, Orctová L, Steger G, Riesner D 
    Biolistic inoculation of plants with viroid nucleic acids. 
    J. Virol. Methods 122, 153-164 (2004) 
    http://dx.doi.org/j.jviromet.2004.08.011  
  • Matoušek J, Orctová L, Steger G, Škopek J, Moors M, Dědič P, Riesner D 
    Analysis of thermal stress-mediated PSTVd variation and biolistic inoculation of progeny of viroid "thermomutants" to tomato and Brassica species. 
    Virology 323, 9-23 (2004) 
    http://dx.doi.org/10.1016/j.virol.2004.02.010  
  • Riesner D 
    No Transmissible spongiform encephalopathies: the prion theory--background and basic information. 
    Contrib Microbiol. 11, 1-13 (2004) 
  • Riesner D, Steger G 
    Viroids and viroid-like agents. 
    Polish J. Pathology 4, 67-78 (2004) 
    http://www.poljpathol.cm-uj.krakow.pl/suplement/04_4_s.pdf  
  • Riesner D, Steger G 
    Temperature-gradient gel-electrophoresis. 
    In Bindereif, A., Hartmann, R., Schön, A. & Westhof, E. (Hrsg.), Handbook of RNA Biochemistry, Wiley-VCH , 398-414 (2004) 
  • Rzepecki P, Nagel-Steger L, Feuerstein S, Linne U, Molt O, Zadmard R, Aschermann K, Wehner M, Schrader T, Riesner D 
    Prevention of Alzheimer's disease-associated Aß aggregation by rationally designed nonpeptidic ß-sheet ligands. 
    J Biol Chem 279, 47497-47505 (2004) 
    http://dx.doi.org/10.1074/jbc.M405914200  
  • Schmitz, M 
    Change of RNase P function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy. 
    Nucl. Acids Res. 32, 6358-6366 (2004) 
  • Steger, G 
    Secondary Structure Prediction. 
    In Bindereif, A., Hartmann, R., Schön, A. & Westhof, E. (Hrsg.), Handbook of RNA Biochemistry, Wiley-VCH , 513-535 (2004) 
  • Steger, G & Riesner, D 
    Properties of Viroids: Molecular characteristics. 
    In Hadidi, A., Flores, R., Randles, J.W. & Semancik, J.S. (Hrsg.), Viroids, CSIRO Publishing, Australia , 15-29 (2004) 
  • Stoldt M, Kupce E, Rehm BHA, Görlach M 
    Backbone resonance assignemnt of an aminogycoside-3'-phosphotransferase type IIa. 
    J. Biomol. NMR 28, 93-94 (2004) 
  • Willbold D, Koenig BW 
    NMR Analysis of Biopolymer Structure. 
    In 'Physics meets Biology: From Soft Matter to Cell Biology', G. Gompper, UB. Kaupp, JKG Dhont, D Richter, RG Winkler,eds. , B3.1-B3.14 (2004) 
  • Briese L and Willbold D 
    Structure determination of human Lck unique and SH3 domains by nuclear magentic resonance spectroscopy. 
    BMC Struct. Biol. 3, 3 (2003) 
  • Choe HW, Park KS, Labahn J, Granzin J, Kim CJ, Büldt G 
    Crystallization and preliminary X-ray diffraction studies of alpha-cyclodextrin glucanotransferase isolated from Bacillus macerans. 
    Acta Crystallogr D Biol Crystallogr. 59(Pt 2), 348-9 (2003) 
  • Dingley AJ, Steger G, Esters B, Riesner D, Grzesiek S 
    Structural characterization of the 69 nucleotide potato spindle tuber viroid left-terminal domain by NMR and thermodynamic analysis. 
    J. Mol. Biol. 334, 751-767 (2003) 
    http://dx.doi.org/10.1016/j.jmb.2003.10.015  
  • Joeres L, Wagner R 
    Essential steps in the ppGpp-dependent regulation of bacterial ribosomal RNA promoters can be explained by substrate competition. 
    J Biol Chem. 278, 16834-16843 (2003) 
  • Khayat R, Batra R, Qian C, Halmos T, Bailey M, Tong L 
    Structural and biochemical studies of inhibitor binding to human cytomegalovirus protease. 
    Biochemistry 42(4), 885-91 (2003) 
  • Koenig BW, Rogowski M, Louis JM 
    A rapid method to attain isotope labeled small soluble peptides for NMR studies. 
    J. Biomol. NMR 26, 193-202 (2003) 
  • Owens RA, Sano T, Feldstein PA, Hu Y, Steger G 
    Identification of a novel structural interaction in Columnea latent viroid. 
    Virology 313, 604-614 (2003) 
    http://dx.doi.org/10.1016/S0042-6822(03)00352-0  
  • Preusser A, Jonas G and Willbold D 
    Purification of recombinantly expressed human cluster determinant 4 cytoplasmatic domain. 
    J. Chromatogr. B 786, 39-44 (2003) 
  • Riesner D 
    Biochemistry and structure of PrP(C) and PrP(Sc). 
    British Medical Bulletin 66, 21-33 (2003) 
  • Schrader O, Baumstark T, Riesner D 
    A mini-RNA containing the tetraloop, wobble-pair and loop E motifs of the central conserved region of potato spindle tuber viroid is processed into a minicircle. 
    Nucleic Acids Res. 31, 988-998 (2003) 
  • Steger G 
    Bioinformatik: Methoden zur Vorhersage von RNA- und Proteinstruktur. 
    Birkhäuser Verlag Basel , (2003) 
  • Steger G, Riesner D 
    Properties of Viroids: Molecular characteristics. 
    In "Viroids" (Hadidi A, Flores R, Randles JW, Semancik JS, eds.) CSIRO Publishing , 15-29 (2003) 
  • Wiesehan K, Buder K, Linke RP, Patt S, Stoldt M, Unger E, Schmitt B, Bucci E and Willbold D 
    Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide Abeta(1-42) by mirror image phage display. 
    ChemBioChem 4, 748-753 (2003) 
  • Wiesehan K, Willbold D 
    Mirror image phage display: Aiming at the mirror. 
    ChemBioChem 4, 811-815 (2003) 
  • Batra R, Christendat D, Edwards A, Arrowsmith C, Tong L 
    Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase. 
    Proteins 49(2), 285-8 (2002) 
  • Böttcher B, Scheide D, Hesterberg M, Nagel-Steger L, Friedrich T 
    A novel, enzymatically active conformation of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). 
    J Biol Chem 277, 17970-17977 (2002) 
    http://dx.doi.org/10.1074/jbc.M112357200  
  • Engler A, Stangler T, Willbold D 
    Structure of human immunodeficiency virus type 1 Vpr (34-51) peptide in micelle containing aqueous solution. 
    Eur. J. Biochem. 269, 3264-3269 (2002) 
  • Gawrisch K, Koenig BW 
    Lipid-peptide interactions investiagted by NMR. 
    In: 'Current Topics in Membranes. Vol. 52: Peptide-lipid interactions' S.A. Simon and T. J. McIntosh, Eds., Academic Press, San Diego , 163-190 (2002) 
  • Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, Büldt G, Savopol T, Scheidig AJ, Klare JP, Engelhard M 
    Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex. 
    Nature 419(6906), 484-7 (2002) 
  • Koenig BW 
    Structure and orientation of ligands bound to membrane proteins are reflected by residual dipolar couplings in solution NMR experiments. 
    ChemBioChem 3, 975-980 (2002) 
  • Koenig BW, Kontaxis G, Mitchell DC, Louis JM, Litman BJ, Bax A 
    Structure and orientation of a G protein fragment in the receptor bound state from residual couplings. 
    J. Mol. Biol. 322, 441-461 (2002) 
  • Labahn J, Neumann S, Büldt G, Kula MR, Granzin J 
    An alternative mechanism for amidase signature enzymes. 
    J Mol Biol. 322(5), 1053-64 (2002) 
  • Neumann S, Granzin J, Kula MR, Labahn J 
    Crystallization and preliminary X-ray data of the recombinant peptide amidase from Stenotrophomonas maltophilia. 
    Acta Crystallogr D Biol Crystallogr. 58(Pt 2), 333-5 (2002) 
  • Preusser A, Briese L, Willbold D 
    Presence of a helix in human CD4 cytoplasmic domain promotes binding to HIV-1 Nef protein. Biochem. 
    Biochem. Biophys. Res. Comm. 292, 734-740 (2002) 
  • Riesner D 
    No molecular basis of prion diseases. 
    J Neurovirol. 8, Suppl. 2: 8-20 (2002) 
  • Schroder AR, Riesner D 
    Detection and analysis of hairpin II, an essential metastable structural element in viroid replication intermediates. 
    Nucleic Acids Res. 30, 3349-3359 (2002) 
  • Stangler T, Mayr LM, Willbold D 
    Solution structure of the GABAA receptor associated protein GABARAP: Implications for biological function and its regulation. 
    J. Biol. Chem. 277, 13363-13366 (2002) 
  • Tsiavaliaris G, Fujita-Becker S, Batra R, Levitsky DI, Kull FJ, Geeves MA, Manstein DJ 
    Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium. 
    EMBO Rep. 3(11), 1099-105 (2002) 
  • Wagner R 
    Regulation of ribosomal RNA synthesis in E. coli: effects of the global regulator guanosine tetraphosphate (ppGpp). 
    J Mol Microbiol Biotechnol. 4, 331-340 (2002) 
  • Yukawa Y, Matousek J, Grimm M, Vrba L, Steger G, Sugiura M, Beier H 
    Plant 7SL RNA and tRNA(Tyr) genes with inserted antisense sequences are efficiently expressed in an in vitro system from Nicotiana tabacum cells. 
    Plant Mol. Biol. 50, 713-723 (2002) 
    http://dx.doi.org/10.1023/A:1019905730397  
  • Appel T, Wolff M, von Rheinbaben F, Heinzel M, Riesner D  
    Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures  
    J Gen Virol 82(Pt 2), 465-73 (2001) 
  • Appel T, Wolff M, von Rheinbaben F, Heinzel M, Riesner D 
    Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures. 
    J Gen Virol. 82, 465-473 (2001) 
  • Batra R, Khayat R, Tong L 
    Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease. 
    Nature Struct Biol. 8(9), 810-7 (2001) 
  • Batra R, Khayat R, Tong L 
    Structural studies of herpesvirus proteases 
    Protein and Peptide Letters 8(5), 333-342 (2001) 
    http://dx.doi.org/10.2174/0929866013409229  
  • Briese L, Hoffmann S, Friedrich U, Biesinger B, Willbold D 
    Sequence-specific 1H, 13C and 15N resonance assignments of lymphocyte specific kinase unique and SH3 domains. 
    J. Biomol. NMR 19, 193-194 (2001) 
  • Engler A, Stangler T, Willbold D 
    Solution structure of human immunodeficiency virus type 1 Vpr (13-33) peptide in micelles. 
    Eur. J. Biochem. 268, 389-395 (2001) 
  • Fels A, Hu K, Riesner D 
    Transcription of potato spindle tuber viroid by RNA polymerase II starts predominantly at two specific sites. 
    Nucleic Acids Res. 29, 4589-4597 (2001) 
  • Gräf S, Strothmann D, Kurtz S, Steger, G 
    HyPaLib: a database of RNAs and RNA structural elements defined by hybrid patterns. 
    Nucleic Acids Res. 29, 196-198 (2001) 
    http://dx.doi.org/10.1093/nar/29.1.196  
  • Jansen K, Schafer O, Birkmann E, Post K, Serban H, Prusiner SB, Riesner D 
    Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form. 
    Biol Chem. 382, 683-691 (2001) 
  • Jonas G, Hoffmann S, Willbold D 
    Binding of phage displayed HIV-1 Tat to TAR RNA in the presence of Cyclin T1. 
    J. Biomed. Sci. 8, 340-346 (2001) 
  • Jonas-Straube E, Schünemann D 
    Functional Analysis of the Protein-interacting Domains of Chloroplast SRP43- 
    J Biol Chem 276, 24654-24660 (2001) 
  • Khayat R, Batra R, Massariol MJ, Lagacé L, Tong L 
    Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease. 
    Biochemistry 40(21), 6344-51 (2001) 
  • Matoušek J, Patzak J, Orctová L, Schubert J, Vrba L, Steger G, Riesner D 
    The variability of hop latent viroid as induced upon heat treatment. 
    Virology 287, 349-358 (2001) 
    http://dx.doi.org/10.1006/viro.2001.1044  
  • Preusser A, Briese L, Baur AS, Willbold D 
    Direct in vitro binding of full-length HIV-1 Nef protein to CD4 cytoplasmic domain. 
    J. Virol. 75, 3960-3964 (2001) 
  • Riesner D 
    No The prion theory: background and basic information. 
    Contrib Microbiol. 7, 7-20 (2001) 
  • Schaferkordt J, Wagner R 
    Effects of base change mutations within an Escherichia coli ribosomal RNA leader region on rRNA maturation and ribosome formation. 
    Nucleic Acids Res. 29, 3394-3403 (2001) 
  • Schroder O, Tippner D, Wagner R 
    Toward the three-dimensional structure of the Escherichia coli DNA-binding protein H-NS: A CD and fluorescence study. 
    Biochem Biophys Res Commun. 282, 219-227 (2001) 
  • Willbold D & Wiesehan K 
    Peptid zur Diagnose und Therapie der Alzheimer-Demenz National: DE 10117281A1, international: PCT/EP02/03862 
    , (2001) 
  • Antal M, Mougin A, Kis M, Boros E, Steger G, Jakab G, Solymosy F, Branlant C  
    Molecular characterization at the RNA and gene levels of U3 snoRNA from a unicellular green alga, Chlamydomonas reinhardtii 
    Nucleic Acids Res 28, 2959-2968 (2000) 
    http://dx.doi.org/10.1093/nar/28.15.2959  
  • Post K, Brown DR, Groschup M, Kretzschmar HA, Riesner D  
    Neurotoxicity but not infectivity of prion proteins can be induced reversibly in vitro  
    Arch Virol Suppl (16), 265-73 (2000) 
  • Schroder O, Wagner R  
    The bacterial DNA-binding protein H-NS represses ribosomal RNA transcription by trapping RNA polymerase in the initiation complex  
    J Mol Biol 298(5), 737-48 (2000) 
  • Wagner R  
    Transcription Regulation in Prokaryotes 
    Oxford University Press , (2000) 
  • Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L 
    Potent and competitive inhibition of malic enzymes by lanthanide ions. 
    Biochem Biophys Res Commun 2;274(2), 440-4 (2000) 
  • Afflerbach H, Schroder O, Wagner R  
    Conformational changes of the upstream DNA mediated by H-NS and FIS regulate E. coli RrnB P1 promoter activity  
    J Mol Biol. 286(2), 339-53 (1999) 
  • Afflerbach H, Schroder O, Wagner R 
    Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo. 
    Mol Microbiol. 28(3), 641-53 (1999) 
  • Appel TR, Dumpitak C, Matthiesen U, Riesner D 
    Prion rods contain an inert polysaccharide scaffold 
    Biol Chem 380(11), 1295-306 (1999) 
  • Batra R, Geeves MA, Manstein DJ 
    Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region. 
    Biochemistry 38(19), 6126-34 (1999) 
  • Batra R, Manstein DJ 
    Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine 
    Biol Chem. 380(7-8), 1017-23 (1999) 
  • Besancon W, Wagner R  
    Characterization of transient RNA-RNA interactions important for the facilitated structure formation of bacterial ribosomal 16S RNA 
    Nucleic Acids Res 27(22), 4353-62 (1999) 
  • Lück R, Gräf S, Steger G 
    ConStruct: a tool for thermodynamic controlled prediction of conserved secondary structure  
    Nucleic Acids Res 27, 4208-4217 (1999) 
    PubMed  
  • Matoušek J, Junker V, Vrba L, Schubert J, Patza, J, Steger G  
    Molecular characterization and genome organization of 7SL RNA genes from hop (Humulus lupulus L)  
    Gene 239, 173-183 (1999) 
    http://dx.doi.org/10.1016/S0378-1119(99)00352-2  
  • Repsilber D, Wiese U, Rachen M, Schröder AR, Riesner D, Steger G 
    Formation of metastable RNA structures by sequential folding during transcription: Time-resolved structural analysis of potato spindle tuber viroid (-)-stranded RNA by temperature-gradient gel electrophoresis. 
    RNA 5, 574-584 (1999) 
    Publisher  
  • Schell J, Wulfert M, Riesner D 
    Detection of point mutations by capillary electrophoresis with temporal temperature gradients  
    Electrophoresis 20(14), 2864-9 (1999) 
  • Tyagi R, Batra R, Gupta MN 
    Amorphous enzyme aggregates: Stability toward heat and aqueous-organic cosolvent mixtures 
    Enzyme and Microbial Technology 24(5-6), 348-354 (1999) 
  • Van Dijk J, Furch M, Derancourt J, Batra R, Knetsch ML, Manstein DJ, Chaussepied P 
    Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II. 
    Eur J Biochem 260(3), 672-83 (1999) 
  • Afflerbach H, Schroder O, Wagner R  
    Effects of the Escherichia coli DNA-binding protein H-NS on rRNA synthesis in vivo  
    Mol Microbiol 28(3), 641-53 (1998) 
  • Balzer M, Wagner R  
    A chemical modification method for the structural analysis of RNA and RNA-protein complexes within living cells  
    Anal Biochem 380(11), 1295-306 (1998) 
  • Balzer M, Wagner R  
    Mutations in the leader region of ribosomal RNA operons cause structurally defective 30 S ribosomes as revealed by in vivo structural probing  
    J Mol Biol 276(3), 547-57 (1998) 
  • Balzer M, Wagner R 
    A chemical modification method for the structural analysis of RNA and RNA-protein complexes within living cells. 
    Anal Biochem. 256(2), 240-2 (1998) 
  • Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Büldt G 
    X-ray crystal structure of arrestin from bovine rod outer segments. 
    Nature 391(6670), 918-21 (1998) 
  • Hemmings-Mieszczak M, Steger G, Hohn T 
    Regulation of CaMV 35S RNA translation is mediated by a stable hairpin in the leader. 
    RNA 4, 101-111 (1998) 
  • Klein TR, Kirsch D, Kaufmann R, Riesner D  
    Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry  
    Biol Chem 379(6), 655-66 (1998) 
  • Mathur J, Koncz-Kalman Z 
    Gene identification with sequenced T-DNA tags generated by tranformation of Arabidopsis cell suspension 
    The Plant Journal 13(5), 707-716 (1998) 
  • Pitschke M, Prior R, Haupt M, Riesner D  
    Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy  
    Nat Med 4(7), 832-4 (1998) 
  • Post K, Pitschke M, Schafer O, Wille H, Appel TR, Kirsch D, Mehlhorn I, Serban H, Prusiner SB, Riesner D  
    Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation  
    Biol Chem 379(11), 1307-17 (1998) 
  • Schluckebier G, Labahn J, Granzin J, Saenger W 
    M.TaqI: possible catalysis via cation-pi interactions in N-specific DNA methyltransferases. 
    Biol Chem. 379(4-5), 389-400 (1998) 
  • Schmitz A, Riesner D 
    Correlation between bending of the VM region and pathogenicity of different Potato Spindle Tuber Viroid strains  
    RNA 4(10), 1295-303 (1998) 
  • Schroder AR, Baumstark T, Riesner D  
    Chemical mapping of co-existing RNA structures  
    Nucleic Acids Res 26(14), 3449-50 (1998) 
  • Smith III GJ, Donello JE, Lück R, Steger G, Hope TJ 
    The hepatitis B virus post-transcriptional regulatory element contains two conserved RNA stem-loops which are required for function. 
    Nucleic Acids Res 26, 4818-4827 (1998) 
  • Batra R, Tyagi R, Gupta MN 
    Influence of immobilization on enzyme activity in aqueous-organic cosolvent mixtures 
    Biocatalysis and Biotransformation 15(2), 101-119 (1997) 
  • Baumstark T, Schroder AR, Riesner D  
    Viroid processing: switch from cleavage to ligation is driven by a change from a tetraloop to a loop E conformation  
    EMBO J 16(3), 599-610 (1997) 
  • Gupta MN, Batra R, Tyagi R, Sharma, A 
    Polarity index: The guiding solvent parameter for enzyme stability in aqueous-organic cosolvent mixtures 
    Biotechnology Progress 13(3), 284-288 (1997) 
  • Heinemann M, Wagner R  
    Guanosine 3',5'-bis(diphosphate) (ppGpp)-dependent inhibition of transcription from stringently controlled Escherichia coli promoters can be explained by an altered initiation pathway that traps RNA polymerase  
    Eur J Biochem 247(3), 990-9 (1997) 
  • Hemmings-Mieszczak M, Steger G, Hohn T 
    Alternative structures of the cauliflower mosaic virus 35S RNA leader. 
    J Mol Biol 267, 1057-1088 (1997) 
  • Hoffmann S, Willbold D 
    A selection system to study protein-RNA interactions: Functional display of HIV-1 Tat protein on filamentous bacteriophage M13 
    Biochem. Biophys. Res. Comm. 235, 806-811 (1997) 
  • Klaff P, Mundt S, Steger G 
    Complex formation of the spinach chloroplast psbA mRNA 5' untranslated region with proteins is dependent on the RNA structure. 
    RNA 3, 1480-1485 (1997) 
  • Metzger AU, Bayer B, Willbold D, Hoffmann S, Frank RW, Goody RS, Rösch P 
    The interaction of HIV-1 Tat (32-72) with its target RNA: A Fluorescence and Nuclear Magnetic Resonance Study 
    Biochem. Biophys. Res. Comm. 241, 31-36 (1997) 
  • Riesner D 
    Prions and their biophysical background  
    Biophys Chem 66, 259-268 (1997) 
  • Wilden U, Choe HW, Krafft B, Granzin J 
    Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment. 
    FEBS Lett. 415(3), 268-70 (1997) 
  • Willbold D, Hoffmann S, Rösch P 
    Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution 
    Eur. J. Biochem. 245, 581-588 (1997) 
  • Klaff P, Riesner D, Steger G  
    RNA structure and the regulation of gene expression  
    Plant Mol Biol 32, 89-106 (1996) 
  • Krohn M, Wagner R  
    Transcriptional pausing of RNA polymerase in the presence of guanosine tetraphosphate depends on the promoter and gene sequence 
    J Biol Chem 271(39), 23884-94 (1996) 
  • Lück R, Steger G, Riesner D 
    Thermodynamic prediction of conserved secondary structure: Application to RRE-element of HIV, tRNA-like element of CMV, and mRNA of prion protein. 
    J Mol Biol 258, 813-826 (1996) 
  • Owens RA, Steger G, Hu Y, Fels A, Hammond RW, Riesner D 
    RNA structural features responsible for potato spindle tuber viroid pathogenicity. 
    Virology 222, 144-158 (1996) 
    http://dx.doi.org/10.1006/viro.1996.0405  
  • Riesner D, Kellings K, Post K, Wille H, Serban H, Groth D, Baldwin MA, Prusiner SB 
    Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity  
    J Virol 70(3), 1714-22 (1996) 
  • Sattler A, Kanka S, Maurer KH, Riesner D 
    Thermostable variants of subtilisin selected by temperature-gradient gel electrophoresis  
    Electrophoresis 17(4), 784-92 (1996) 
  • Sattler A, Kanka S, Schrors W, Riesner D  
    Random mutagenesis of the weak calcium binding site in subtilisin Carlsberg and screening for thermostability by temperature-gradient gel electrophoresis 
    Adv Exp Med Biol 379, 171-82 (1996) 
  • Schmitz M, Steger G 
    Description of RNA folding by ``simulated annealing''. 
    J Mol Biol 255, 254-266 (1996) 
  • Baumstark T, Riesner D 
    Only one of four possible secondary structures of the central conserved region of potato spindle tuber viroid is a substrate for processing in a potato nuclear extract 
    Nucleic Acids Res 23(21), 4246-54 (1995) 
  • Chen X, Baumstark T, Steger G, Riesner D  
    High resolution SSCP by optimization of the temperature by transverse TGGE 
    Nucleic Acids Res 23(21), 4524-5 (1995) 
  • Dong GQ, Batra R, Kaul R, Gupta MN, Mattiasson B 
    Alternative modes of precipitation of Eudragit S100: A potential ligand carrier for affinity precipitation of protein 
    Bioseparation 5(6), 339-350 (1995) 
  • Grant M, Dangl J 
    Structure of the Arabidopsis RPM1 Gene enabling dual specifity disease resistance 
    Science 269, 843-846 (1995) 
  • Gruner R, Fels A, Qu F, Zimmat R, Steger G, Riesner D  
    Interdependence of pathogenicity and replicability with potato spindle tuber viroid 
    Virology 209(1), 60-9 (1995) 
  • Krohn M, Wagner R  
    A procedure for the rapid preparation of guanosine tetraphosphate (ppGpp) from Escherichia coli ribosomes  
    Anal Biochem 225(1), 188-90 (1995) 
  • Liebig B, Wagner R 
    Effects of different growth conditions on the in vivo activity of the tandem Escherichia coli ribosomal RNA promoters P1 and P2  
    Mol Gen Genet 249(3), 328-35 (1995) 
  • Martin S, Kardorf J, Schulte B, Lampeter EF, Gries FA, Melchers I, Wagner R, Bertrams J, Roep BO, Pfutzner A  
    Autoantibodies to the islet antigen ICA69 occur in IDDM and in rheumatoid arthritis 
    Diabetologia 38(3), 351-5 (1995) 
  • Martin S, Rieckmann P, Melchers I, Wagner R, Bertrams J, Voskuyl AE, Roep BO, Zielasek J, Heidenthal E, Weichselbraun I, et al  
    Circulating forms of ICAM-3 (cICAM-3). Elevated levels in autoimmune diseases and lack of association with cICAM-1  
    J Immunol 154(4), 1951-5 (1995) 
  • Pardon B, Wagner R 
    The Escherichia coli ribosomal RNA leader nut region interacts specifically with mature 16S RNA  
    Nucleic Acids Res 23(6), 932-41 (1995) 
  • Schluckebier G, Labahn J, Granzin J, Schildkraut I, Saenger W 
    A model for DNA binding and enzyme action derived from crystallographic studies of the TaqI N6-adenine-methyltransferase. 
    Gene 157(1-2), 131-4 (1995) 
  • Tippner D, Wagner R 
    Fluorescence analysis of the Escherichia coli transcription regulator H-NS reveals two distinguishable complexes dependent on binding to specific or nonspecific DNA sites  
    J Biol Chem 270(38), 22243-7 (1995) 
  • Wiese U, Wulfert M, Prusiner SB, Riesner D  
    Scanning for mutations in the human prion protein open reading frame by temporal temperature gradient gel electrophoresis  
    Electrophoresis 16(10), 1851-60 (1995) 
  • Batra R, Gupta MN 
    Enhancement of Enzyme-Activity in Aqueous-Organic Solvent Mixtures 
    Biotechnology Letters 16(10), 1059-1064 (1994) 
  • Batra R, Gupta MN 
    Noncovalent Immobilization of Potato (Solanum-Tuberosum) Polyphenol Oxidase on Chitin 
    Biotechnology and Applied Biochemistry 19, 209-215 (1994) 
  • Cvak L, Jegorov A, Sedmera P, Havlicek V, Ondracek J, Husak M, Pakhomova S, Kratochvil B, Granzin J 
    Ergogaline, a New Ergot Alkaloid, Produced by Claviceps purpurea: Isolation, Identification, Crystal Structure and Molecular conformation. 
    J. Chem. Soc. PERKIN TRANS. 2, 1861-1865 (1994) 
  • Kellings K, Prusiner SB, Riesner D  
    Nucleic acids in prion preparations: unspecific background or essential component  
    Philos Trans R Soc Lond B Biol Sci 343(1306), 425-30 (1994) 
  • Kumar A, Agarwal R, Batra R, Gupta MN 
    Effect of Polymer Concentration on Recovery of the Target Proteins in Precipitation Methods 
    Biotechnology Techniques 8(9), 651-654 (1994) 
  • Labahn J, Granzin J, Schluckebier G, Robinson DP, Jack WE, Schildkraut I, Saenger W 
    Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. 
    Proc Natl Acad Sci U S A. 91(23), 10957-61 (1994) 
  • Matousek J, Trena L, Dedic P, Rakousky S, Steger G, Riesner D 
    Inhibition of viroid infection by antisense RNA expression in transgenic plants. 
    Biol Chem Hoppe-Seyler 375, 765-777 (1994) 
  • Pardon B, Thelen L, Wagner R 
    The Escherichia coli ribosomal RNA leader: a structural and functional investigation 
    Biol Chem Hoppe Seyler 375(1), 11-20 (1994) 
  • Riesner D, Steger G, Wiese U, Wulfert M, Heibey M, Henco K 
    Temperature-gradient gel electrophoresis (TGGE) for the detection of polymorphic DNA and RNA. 
    Methods Mol Biol 31, 211-228 (1994) 
  • Schubert WD, Schluckebier G, Backmann J, Granzin J, Kisker C, Choe HW, Hahn U, Pfeil W, Saenger W 
    X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. 
    Eur J Biochem. 220(2), 527-34 (1994) 
  • Steger G 
    Thermal denaturation of double-stranded nucleic acids: Prediction of temperatures critical for gradient gel electrophoresis and polymerase chain reaction. 
    Nucleic Acids Res 22, 2760-2768 (1994) 
  • Steinecke P, Steger G, Schreier PH 
    A stable hammerhead structure is not required for endonucleolytic activity of a ribozyme in vivo. 
    Gene 149, 47-54 (1994) 
  • Tippner D, Afflerbach H, Bradaczek C, Wagner R 
    Evidence for a regulatory function of the histone-like Escherichia coli protein H-NS in ribosomal RNA synthesis  
    Mol Microbiol 11(3), 589-604 (1994) 
  • Wagner R  
    The regulation of ribosomal RNA synthesis and bacterial cell growth 
    Arch Microbiol 161, 100-109 (1994) 
  • Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D  
    Analysis of nucleic acids in purified scrapie prion preparations 
    Arch Virol Suppl 7, 215-25 (1993) 
  • Lenz A, Choe HW, Granzin J, Heinemann U, Saenger W 
    Three-dimensional structure of the ternary complex between ribonuclease T1, guanosine 3',5'-bisphosphate and inorganic phosphate at 0.19 nm resolution. 
    Eur J Biochem. 211(1-2), 311-6 (1993) 
  • Qu F, Heinrich C, Loss P, Steger G, Tien P, Riesner D  
    Multiple pathways of reversion in viroids for conservation of structural elements 
    EMBO J. 12(5), 2129-39 (1993) 
  • Riesner D, Kellings K, Wiese U, Wulfert M, Mirenda C, Prusiner SB  
    Prions and nucleic acids: search for "residual" nucleic acids and screening for mutations in the PrP-gene  
    Dev Biol Stand 80, 173-81 (1993) 
  • Rosenbaum V, Klahn T, Lundberg U, Holmgren E, von Gabain A, Riesner D  
    Co-existing structures of an mRNA stability determinant. The 5' region of the Escherichia coli and Serratia marcescens ompA mRNA  
    J Mol Biol 229(3), 656-70 (1993) 
  • Saenger W, Sandmann C, Theis K, Starikov EB, Kostrewa D, Labahn J, Granzin J 
    Structural and Functions Aspects of the DNA Binding Protein FIS; for Nucleic Acids and Molecular Biology. Edited by Fritz Eckstein and David M.J. Lilley. 
    Nucleic Acids and Molecular Biology Vol 7, Springer-Verlag. , (1993) 
  • Sattler A, Riesner D  
    Temperature-gradient gel electrophoresis for analysis and screening of thermostable proteases 
    Electrophoresis 14(8), 782-8 (1993) 
  • Theissen G, Schonborn J, Wagner R  
    Temperature-gradient gel electrophoresis for the detection and characterization of curved DNA-fragments  
    Nucleic Acids Res 21(19), 4643-4 (1993) 
  • Theissen G, Thelen L, Wagner R  
    Some base substitutions in the leader of an Escherichia coli ribosomal RNA operon affect the structure and function of ribosomes. Evidence for a transient scaffold function of the rRNA leader  
    J Mol Biol 233(2), 203-18 (1993) 
  • Ding J, Choe HW, Granzin J, Saenger W 
    Structure of ribonuclease T1 complexed with zinc(II) at 1.8 A resolution: a Zn2+.6H2O.carboxylate clathrate. 
    Acta Crystallogr B. 48 ( Pt 2), 185-91 (1992) 
  • Granzin J, Puras-Lutzke R, Landt O, Grunert HP, Heinemann U, Saenger W, Hahn U 
    RNase T1 mutant Glu46Gln binds the inhibitors 2'GMP and 2'AMP at the 3' subsite. 
    J Mol Biol. 225(2), 533-42. (1992) 
  • Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D  
    Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis  
    J Gen Virol 73 ( Pt 4), 1025-9 (1992) 
  • Kostrewa D, Granzin J, Koch C, Choe HW, Raghunathan S, Wolf W, Labahn J, Kahmann R, Saenger W 
    Three-Dimensional Structure of The DNA Binding Protein FIS. 
    Structure & Function Vol. 2: Proteins. Eds. R.H. Sarma & M.H. Sarma, Adenine Press. , (1992) 
  • Kostrewa D, Granzin J, Stock D, Choe HW, Labahn J, Saenger W 
    Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. 
    J Mol Biol. 226(1), 209-26 (1992) 
  • Krohn M, Pardon B, Wagner R  
    Effects of template topology on RNA polymerase pausing during in vitro transcription of the Escherichia coli rrnB leader region  
    Mol Microbiol 6(5), 581-9 (1992) 
  • Riesner D, Baumstark T, Qu F, Klahn T, Loss P, Rosenbaum V, Schmitz M, Steger G 
    Physical basis and biological examples of metastable RNA structures. 
    In "Structural tools for the analysis of protein-nucleic acids complexes. Advances in Life Sciences" (Lilley D, Heumann H, Suck D, eds.) Birkhäuser , 401-435 (1992) 
  • Riesner D, Steger G, Wiese U, Wulfert M, Heibey M, Henco K 
    Temperature-gradient gel electrophoresis for the detection of polymorphic DNA and for quantitative polymerase chain reaction  
    Electrophoresis 13(9-10), 632-6 (1992) 
  • Schmidt B, Riesner D, Lawen A, Kleinkauf H 
    Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases  
    FEBS Lett 307(3), 355-60 (1992) 
  • Schmitz M, Steger G 
    Base-pair probability profiles of RNA secondary structures. 
    CABIOS 8, 389-399 (1992) 
  • Steger G, Baumstark T, Mörchen M, Tabler M, Tsagris M, Sänger HL, Riesner D 
    Structural requirements for viroid processing by RNase T1. 
    J Mol Biol 227, 719-737 (1992) 
  • Keitel T, Granzin J, Simon O, Borriss R, Thomsen KK, Wessner H, Höhne W, Heinemann U 
    Crystallization of the hybrid Bacillus (1-3,1-4)-beta-glucanase H(A16-M). 
    J Mol Biol. 218(4), 703-4 (1991) 
  • Kostrewa D, Granzin J, Koch C, Choe HW, Raghunathan S, Wolf W, Labahn J, Kahmann R, Saenger W 
    Three-dimensional structure of the E. coli DNA-binding protein FIS. 
    Nature 349(6305), 178-80 (1991) 
  • Loss P, Schmitz M, Steger G, Riesner D  
    Formation of a thermodynamically metastable structure containing hairpin II is critical for infectivity of potato spindle tuber viroid RNA  
    EMBO J 10(3), 719-27 (1991) 
  • Meyer N, Rosenbaum V, Schmidt B, Gilles K, Mirenda C, Groth D, Prusiner SB, Riesner D  
    Search for a putative scrapie genome in purified prion fractions reveals a paucity of nucleic acids  
    J Gen Virol 72 ( Pt 1), 37-49 (1991) 
  • Owens RA, Thompson SM, Steger G 
    Effects of random mutagenesis upon potato spindle tuber viroid replication and symptom expression. 
    Virology 185, 18-31 (1991) 
  • Riesner D  
    Viroids: from thermodynamics to cellular structure and function 
    Mol Plant Microbe Interact 4, 122-131 (1991) 
  • Riesner D, Harders J, Hecker R, Klaff P, Lukacs N, Steger G  
    Viroid structures involved in protein binding and replication. 
    In "Plant Molecular Biology 2" (Herrmann RG, Larkins BA, eds.) NATOA ASI Series A, Life Sciences, Plenum Press 212, 75-90 (1991) 
  • Riesner D, Henco K, Steger G 
    Temperature-gradient gel electrophoresis: A method for the analysis of conformational transitions and mutations in nucleic acids and proteins. 
    In "Advances in electrophoresis" (Chrambach A, Dunn MJ, Radola BJ, eds.) VCH Weinheim Vol. 4, 169-250 (1991) 
  • Birmes A, Sattler A, Maurer KH, Riesner D  
    Analysis of the conformational transitions of proteins by temperature-gradient gel electrophoresis  
    Electrophoresis 11(10), 795-801 (1990) 
  • Granzin J, Saenger W, Stolarski R, Shugar D 
    Solid State and Solution Structures of an Adenine Analogue of the Antiviral Acyclonucleoside 9- (1,3-Dihydroxy-2-propoxymethyl) guanine. 
    Z. Naturforsch 45c, 915-921 (1990) 
  • Riesner D, Steger G 
    Viroids and viroid-like RNA. 
    In "Nucleic Acids, Subvol. d, Physical Data II, Theoretical Investigations, Landolt-Börnstein. Group VII Biophysics, 1, 194-243 (1990) 
  • Rubino L, Tousignant ME, Steger G, Kaper JM 
    Nucleotide sequence and structural analysis of two satellite RNAs associated with chicory yellow mottle virus (CYMV). 
    J Gen Virol 71, 1897-1904 (1990) 
  • Theissen G, Behrens SE, Wagner R  
    Functional importance of the Escherichia coli ribosomal RNA leader box A sequence for post-transcriptional events  
    Mol Microbiol 4(10), 1667-78 (1990) 
  • Theissen G, Eberle J, Zacharias M, Tobias L, Wagner R  
    The tL structure within the leader region of Escherichia coli ribosomal RNA operons has post-transcriptional functions  
    Nucleic Acids Res 18(13), 3893-901 (1990) 
  • Theissen G, Pardon B, Wagner R 
    A quantitative assessment for transcriptional pausing of DNA-dependent RNA polymerases in vitro  
    Anal Biochem 189(2), 254-61 (1990) 
  • Zacharias M, Wagner R, Goringer HU  
    Polyacrylamide gradient gel electrophoresis for the detection of bended DNA fragments  
    Nucleic Acids Res 18(9), 2827 (1990) 
  • Harders J, Lukacs N, Robert-Nicoud M, Jovin TM, Riesner D  
    Imaging of viroids in nuclei from tomato leaf tissue by in situ hybridization and confocal laser scanning microscopy  
    EMBO J 8(13), 3941-9 (1989) 
  • Riesner D, Steger G, Zimmat R, Owens RA, Wagenhofer M, Hillen W, Vollbach S, Henco K  
    Temperature-gradient gel electrophoresis of nucleic acids: analysis of conformational transitions, sequence variations, and protein-nucleic acid interactions  
    Electrophoresis 10(5-6), 377-89 (1989) 
  • Riesner D, Steger G, Zimmat R, Owens RA, Wagenhöfer M, Hillen W, Vollbach S, Henco K  
    Temperature-gradient gel electrophoresis: Analysis of conformational transitions, sequence variations, and protein-nucleic acid interactions. 
    Electrophoresis 10, 377-389 (1989) 
  • Weber H-J, Schulz M, Schmitz S, Granzin J, Siegert H 
    Determination and structural application of anisotropic bond polarisabilities in complex crystals. 
    J. Phys.: Condens. Matter 1, 8543-8557 (1989) 
  • Zimmat R, Gruner R, Hecker R, Steger G, Riesner D 
    Analysis of mutations in viroid RNA by non-denaturing and temperature-gradient gel electrophoresis. 
    In "Proceedings of the Sixth Conversation in Biomolecular Stereodynamics" (Sarma RH, Sarma MH, eds.) AdeninePress, Schenectady, New York , 339-357 (1989) 
  • Hecker R, Wang ZM, Steger G, Riesner D  
    Analysis of RNA structures by temperature-gradient gel electrophoresis: viroid replication and processing  
    Gene 72(1-2), 59-74 (1988) 
  • Kaper JM, Tousignant ME, Steger G 
    Nucleotide sequence predicts circularity and self-cleavage of 300-ribonucleotide satellite of arabis mosaic virus. 
    Biochem Biophys Res Commun 154, 318-325 (1988) 
  • Riesner D, Hecker R, Steger G 
    Structure of viroid replication intermediates as studied by thermodynamics and temperature-gradient gel electrophoresis. 
    In "Structure and expression. From Proteins to ribosomes" (Sarma RH, Sarma MH, eds.) Adenine Press 1, 261-285 (1988) 
  • Steger G 
    Structural properties of viroid replicative intermediates and of satellite RNAs of CMV. 
    In "Plant Molecular Biology" (van Wettstein D, Chua NH, eds.) NATOA ASI Series A, Life Sciences, Plenum Press 140, 469-481 (1988) 
  • Witt I, Witt HT, Di Fiore D, Röger M, Hinrichs W, Saenger W, Granzin J, Betzel C, Dauter Z 
    X-ray characterization of Single Crystals of the Reaction Center I of Water Splitting Photosysnthesis. 
    Ber. Bunsenges. Phys. Chem. 92, 1503-1506 (1988) 
  • Riesner D, Klaff P, Steger G, Hecker R 
    Viroids: Subcellular location and structure of replicative intermediates. 
    In "Endocytobiology III" (Lee JJ, Fredrick JF, eds.) The New York Academy of Sciences, New York , 212-237 (1987) 
  • Steger G, Tien P, Kaper J, Riesner D 
    Double-stranded cucumovirus associated RNA 5: Which sequence variations may be detected by optical melting and temperature-gradient gel electrophoresis? 
    Nucleic Acids Res 15, 5085-5103 (1987) 
  • Tien P, Steger G, Rosenbaum V, Kaper J, Riesner D 
    Double-stranded cucumovirus associated RNA 5: Experimental analysis of necrogenic and non-necrogenic variants by temperature-gradient gel electrophoresis. 
    Nucleic Acids Res 15, 5069-5083 (1987) 
  • Brosius B, Riesner D  
    Influence of lipid membranes on the conformational transitions of nucleic acids  
    J Biomol Struct Dyn 4(2), 271-90 (1986) 
  • Steger G, Rosenbaum V, Riesner D 
    Viroids: Structure formation and function. 
    In "Structure and dynamics of RNA" NATO ASI Series A, Life Sciences, Plenum Press 110, 315-329 (1986) 
  • Steger G, Tabler M, Brüggemann W, Colpan M, Klotz G, Sänger HL, Riesner D 
    Structure of viroid replicative intermediates: Physico-chemical studies on SP6 transcripts of cloned oligomeric potato spindle tuber viroid. 
    Nucleic Acids Res 14, 9613-9630 (1986) 
  • Werntges H, Steger G, Riesner D, Fritz HJ 
    Mismatches in DNA double strands: Thermodynamic parameters and their correlation to repair efficiencies. 
    Nucleic Acids Res 14, 3773-3790 (1986) 
  • Loss P, Steger G, Riesner D 
    Klonierung und Hybridisierung vonkrankheitsassoziierten Nukleinsäuren zur diagnostischen Erfassung von Waldschäden.  
    VDIn Berichte 560, 71-80 (1985) 
  • Steger G, Loss P, Schumacher J, Riesner D 
    Korrelation des Auftretens kleiner RNAs mit Waldschäden.  
    VDI Berichte 560, 61-70 (1985) 
  • Brosius B, Riesner D, Hillen W  
    Interaction of nucleic acids with lipid membranes 
    J Biomol Struct Dyn 1(6), 1535-41 (1984) 
  • Steger G, Hofmann H, Förtsch J, Gross HJ, Randles JW, Sänger HL, Riesner D 
    Conformational transitions in viroids and virusoids: Comparison of results from energy minimization algorithm and from experimental data. 
    J Biomol Struct Dyn 2, 543-571 (1984) 
  • Brosius B, Steger G, Hillen W, Riesner D 
    Thermodynamics of nucleic acids enclosed in reverse phase vesicles. 
    In "Reverse micelles: Biological and technological relevance, Proceedings of the IV. ESF Workshop on Polymer Science, Rigi-Kaltbad, Switzerland" Plenum Press , 279-­286 (1983) 
  • Gross HJ, Sänger HL, Schumacher J, Steger G, Riesner D  
    Viroids: their structure and possible origin. 
    In "Endocytobiology III" (Lee JJ, Fredrick JF, eds.) The New York Academy of Sciences, New York , 48-55 (1983) 
  • Riesner D, Colpan M, Goodman TC, Nagel L, Schumacher J, Steger G, Hofmann H 
    Dynamics and interactions of viroids. 
    J Biomol Struct Dyn 1, 669-688 (1983) 
  • Riesner D, Steger G, Schumacher J, Gross HJ, Randles JW, Sänger HL 
    Structure and function of viroids. 
    Biophys Struct Mech 9, 145­-170 (1983) 
  • Schumacher J, Sanger HL, Riesner D  
    Subcellular localization of viroids in highly purified nuclei from tomato leaf tissue 
    EMBO J 2(9), 1549-55 (1983) 
  • Randles JW, Steger G, Riesner D 
    Structural transitions in viroid-like RNAs associated with cadang-cadang disease, velvet tobacco mottle virus, and Solanum nodiflorum mottle virus. 
    Nucleic Acids Res 10, 5569-5586 (1982) 
  • Gross HJ, Krupp G, Domdey H and, Steger G, Riesner D, Sänger HL 
    The structure of the plant viroids. 
    Nucleic Acids Res Symp Ser 10, 91-98 (1981) 
  • Henco K, Steger G, Riesner D 
    Melting curves on less than 1 ug of nucleic acid. 
    Analyt Biochem 101, 225-229 (1980) 
  • Steger G, Müller H, Riesner D 
    Helix-coil transitions in double-stranded viral RNA: Fine resolution melting and ionic strength dependence. 
    Biochim Biophys Acta 606, 274-284 (1980) 
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