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Publikationen

  • 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  
  • Bovdilova A, Alexandre BM, Höppner A, Luís IM, Alvarez CE, Bickel D, Gohlke H, Decker C, Nagel-Steger L, Alseekh S, Fernie AR, Drincovich MF, Abreu IA, Maurino VG. 
    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  
    http://www.plantcell.org/content/31/10/2525.long  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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) 
  • 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) 
  • 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, 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  
  • 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  
  • 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  
  • 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) 
  • 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) 
  • 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 
  • 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  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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"]  
  • 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  
  • 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  
  • 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  
  • 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  
  • 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) 
  • 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  
  • 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  
  • 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  
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