Different Conformational Subensembles of the Intrinsically Disordered Protein α-Synuclein in Cells
Author:
Affiliation:
1. Nanobiophysics Group, Faculty of Science and Technology, University of Twente, Enschede, The Netherlands
Publisher
American Chemical Society (ACS)
Subject
General Materials Science,Physical and Theoretical Chemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.8b00092
Reference31 articles.
1. Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations
2. A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders
3. Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement
4. α-Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics
5. α-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton
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