Wolfgang Hoyer

Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Lothar Gremer, Daniel Schölzel, C. Schenk et al. · Science · 2017 · 1K citations · Full text

Fibril Structure, Neurodegenerative Diseases, Alzheimer's Disease +13

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Carlos W. Bertoncini, Young‐Sang Jung, Claudio O. Fernández et al. · Proceedings of the National Academy of Sciences · 2005 · 778 citations · Full text

Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR

Henrike Heise, Wolfgang Hoyer, Stefan Becker et al. · Proceedings of the National Academy of Sciences · 2005 · 632 citations · Full text

Dependence of α-Synuclein Aggregate Morphology on Solution Conditions

Wolfgang Hoyer, Thomas Antony, Dmitry Cherny et al. · Journal of Molecular Biology · 2002 · 568 citations · Full text

Neurodegenerative Diseases, α-Synuclein Aggregate Morphology, Protein Misfolding +3

Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation

Wolfgang Hoyer, Caroline Grönwall, Andreas Jonsson et al. · Proceedings of the National Academy of Sciences · 2008 · 414 citations · Full text

Protein Assembly, Molecular Biology, Alzheimer's Disease +17