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Dirk Matthes
Dirk Matthes
Max Planck Institute for Multidisciplinary Sciences
Bestätigte E-Mail-Adresse bei gwdg.de - Startseite
Titel
Zitiert von
Zitiert von
Jahr
Secondary structure propensities in peptide folding simulations: a systematic comparison of molecular mechanics interaction schemes
D Matthes, BL De Groot
Biophysical journal 97 (2), 599-608, 2009
1452009
Driving forces and structural determinants of steric zipper peptide oligomer formation elucidated by atomistic simulations
D Matthes, V Gapsys, BL de Groot
Journal of molecular biology 421 (2-3), 390-416, 2012
762012
Mapping the conformational dynamics and pathways of spontaneous steric zipper peptide oligomerization
D Matthes, V Gapsys, V Daebel, BL de Groot
PloS one 6 (5), e19129, 2011
552011
Primary steps of pH‐dependent insulin aggregation kinetics are governed by conformational flexibility
J Haas, E Vöhringer‐Martinez, A Bögehold, D Matthes, U Hensen, ...
ChemBioChem 10 (11), 1816-1822, 2009
512009
The 3D structure of lipidic fibrils of α-synuclein
B Frieg, L Antonschmidt, C Dienemann, JA Geraets, EE Najbauer, ...
Nature communications 13 (1), 6810, 2022
352022
An atomistic view of amyloidogenic self-assembly: structure and dynamics of heterogeneous conformational states in the pre-nucleation phase
D Matthes, V Gapsys, JT Brennecke, BL de Groot
Scientific Reports 6 (1), 33156, 2016
302016
Resolving the atomistic modes of Anle138b inhibitory action on peptide oligomer formation
D Matthes, V Gapsys, C Griesinger, BL de Groot
ACS chemical neuroscience 8 (12), 2791-2808, 2017
272017
Spontaneous aggregation of the insulin-derived steric zipper peptide VEALYL results in different aggregation forms with common features
D Matthes, V Daebel, K Meyenberg, D Riedel, G Heim, U Diederichsen, ...
Journal of Molecular Biology 426 (2), 362-376, 2014
262014
The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils
L Antonschmidt, D Matthes, R Dervişoğlu, B Frieg, C Dienemann, ...
Nature Communications 13 (1), 5385, 2022
192022
Molecular dynamics simulations reveal the importance of amyloid-beta oligomer β-sheet edge conformations in membrane permeabilization
D Matthes, BL de Groot
Journal of Biological Chemistry 299 (4), 2023
72023
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