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The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins

Date

Authors

Rekas, Agata

Ahn, Keun Jae

Kim, Jongsun

Carver, John

Publisher

John Wiley & Sons Inc

Abstract

α-Synuclein is the principal component of the Lewy body deposits that are characteristic of Parkinson's disease. In vivo, and under physiological conditions in vitro, α-synuclein aggregates to form amyloid fibrils, a process that is likely to be associa

Keywords

Keywords: alpha synuclein; amyloid; chaperone; thioflavine; amino terminal sequence; article; beta sheet; binding site; carboxy terminal sequence; circular dichroism; correlation analysis; light scattering; mutational analysis; priority journal; protein aggregation Aggregation; Amyloid fibril; Binding site; Circular dichroism; Dynamic light scattering; Parkinson's disease; Thioflavin T

URI

http://hdl.handle.net/1885/63371

Collections

ANU Research Publications

Source

Proteins

Type

Journal article

DOI

10.1002/prot.24028

Restricted until

2037-12-31

Downloads

File

Description

01_Rekas_The_chaperone_activity_of_2012.pdf (1.22 MB)

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