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
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
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
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
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
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)
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)
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)
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
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)
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
Holze R, Jacob T, Schünke S, Neudecker P, Willbold D Physical Chemistry 2011 Nachr. Chemie 60, 313-322 (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)
Lehmann K, Hoffmann S, Neudecker P, Suhr M, Becker WM, Rösch P High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2 Protein Expr. Purif. 31, 250-9 (2003)
Neudecker P, Lehmann K, Nerkamp J, Haase T, Wangorsch A, Fotisch K, Hoffmann S, Rösch P, Vieths S, Scheurer S Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure Biochem J. 15, 97-107 (2003)
