Resonance assignments of an α-synuclein fibril prepared in Tris buffer at moderate ionic strength-Reference-Cited by-同舟云学术

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Resonance assignments of an α-synuclein fibril prepared in Tris buffer at moderate ionic strength

Published:2018-02-23 Issue:1 Volume:12 Page:195-199
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Barclay Alexander M.,Dhavale Dhruva D.,Courtney Joseph M.,Kotzbauer Paul T.,Rienstra Chad M.

Funder

National Institutes of Health

Michael J. Fox Foundation for Parkinson’s Research

National Science Foundation

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

http://link.springer.com/article/10.1007/s12104-018-9808-5/fulltext.html

Reference25 articles.

1. Bagchi DP, Yu L, Perlmutter JS et al (2013) Binding of the radioligand SIL23 to α-synuclein fibrils in Parkinson disease brain tissue establishes feasibility and screening approaches for developing a parkinson disease imaging agent. PLoS ONE 8:e55031

2. Bousset L, Pieri L, Ruiz-Arlandis G et al (2013) Structural and functional characterization of two alpha-synuclein strains. Nat Commun 4:2575

3. Chu W, Zhou D, Gaba V et al (2015) Design, synthesis, and characterization of 3-(benzylidene)indolin-2-one derivatives as ligands for α-synuclein fibrils. J Med Chem 58:6002–6017

4. Comellas G, Rienstra CM (2013) Protein structure determination by magic-angle spinning solid-state NMR, and insights into the formation, structure, and stability of amyloid fibrils. Annu Rev Biophys 42:515–536

5. Comellas G, Lemkau LR, Nieuwkoop AJ et al (2011a) Structured regions of α-synuclein fibrils include the early-onset Parkinson’s disease mutation sites. J Mol Biol 411:881–895

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