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
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
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
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
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
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
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
