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L. Gardon, N. Becker, N. Rähse, C. Hölbling, A. Apostolidis, C. M. Schulz, K. Bochinsky, L. Gremer, H. Heise, N.-A. Lakomek, Amyloid fibril formation kinetics of low-pH denatured bovine PI3K-SH3 monitored by three different NMR techniques, Front. Mol. Biosci. 2023, 10.
N. Becker, B. Frieg, L. Gremer, T. Kupreichyk, L. Gardon, P. Freiburg, P. Neudecker, D. Willbold, H. Gohlke, H. Heise, Atomic Resolution Insights into pH Shift Induced Deprotonation Events in LS-Shaped Aβ(1–42) Amyloid Fibrils. J. Am. Chem. Soc. 2023, 145, 2161.
D. Willbold, B. Strodel, G. F. Schröder, W. Hoyer, H Heise, Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids, Chem. Rev. 2021, 121, 8285-8307.
A. König, N. Rösener, L. Gremer, M. Tusche, D. Flender, E. Reinartz, W. Hoyer, P. Neudecker, D. Willbold, H. Heise, Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy, J. Biol. Chem. 2021, 296, 100499.
H. Park, B. Uluca-Yazgi, S. Heumann, R. Schlögl, J. Granwehr, H. Heise, P. P. M. Schleker, Heteronuclear cross-relaxation effect modulated by the dynamics of N-functional groups in the solid state under 15N DP-MAS DNP, J. Magn. Reson. 2020, 312, 106688.
L. Siemons, B. Uluca-Yazgi, R. B. Pritchard, S. McCarthy, H. Heise, D. F. Hansen, Determining isoleucine side-chain rotamer-sampling in proteins from 13C chemical shift, Chem. Commun. 2019, 55, 14107-14110.
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N.S. Rösener, L. Gremer, E. Reinartz, A. König, O. Brener, H. Heise, W. Hoyer, P. Neudecker, D. Willbold, A D-enantiomeric peptide interferes with hetero-association of amyloid-β oligomers and prion protein, J. Biol. Chem. 2018, 293, 15748–15764.
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F. Weirich, L. Gremer, E.A: Mirecka, S. Schiefer, W. Hoyer, H. Heise. Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment is Part of the beta-sheet Core, PLoS ONE, 2016, 11, e0161243.
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