Insights into the molecular mechanism of amyloid filament formation: Segmental folding of α-synuclein on lipid membranes

Author:

Antonschmidt Leif1ORCID,Dervişoğlu Rıza1ORCID,Sant Vrinda12,Tekwani Movellan Kumar1ORCID,Mey Ingo3ORCID,Riedel Dietmar4ORCID,Steinem Claudia356ORCID,Becker Stefan1ORCID,Andreas Loren B.1ORCID,Griesinger Christian16ORCID

Affiliation:

1. Department of NMR-Based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.

2. Department of Mechanical and Aerospace Engineering, University of California San Diego, San Diego, CA, USA.

3. Institute of Organic and Biomolecular Chemistry, Georg-August-Universität Göttingen, Göttingen, Germany.

4. Laboratory of Electron Microscopy, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.

5. Biomolecular Chemistry Group, Max-Planck Institute for Dynamics and Self-Organization, Am Fassberg 17, 37077 Göttingen, Germany.

6. Cluster of Excellence “Multiscale Bioimaging: From Molecular Machines to Networks of Excitable Cells” (MBExC), University of Göttingen, Göttingen, Germany.

Abstract

Aggregation intermediates of Parkinson’s disease–related α-synuclein on liposomes are structurally characterized by NMR.

Funder

ASCRS Research Foundation

Deutsche Forschungsgemeinschaft

Max-Planck-Gesellschaft

Alzheimer Nadační Fond

FUNDING

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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