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Small Heat-shock Proteins Prevent -Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation

Cox, Dezerae; Selig, Emily; Griffin, Michael D.W.; Carver, John; Ecroyd, Heath

Description

The aggregation of α-synuclein (α-syn) into amyloid fibrils is associated with neurodegenerative diseases, collectively referred to as the α-synucleinopathies. In vivo, molecular chaperones, such as the small heat-shock proteins (sHsps), normally act to prevent protein aggregation; however, it remains to be determined how aggregation-prone α-syn evades sHsp chaperone action leading to its disease-associated deposition. This work examines the molecular mechanism by which two canonical sHsps,...[Show more]

CollectionsANU Research Publications
Date published: 2016
Type: Journal article
URI: http://hdl.handle.net/1885/152872
Source: Journal of Biological Chemistry
DOI: 10.1074/jbc.M116.739250
Access Rights: Open Access

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