Using bicistronic constructs to evaluate the chaperone activities of heat shock proteins in cells

Abstract Heat shock proteins (Hsps) are molecular chaperones that prevent the aggregation of client proteins by facilitating their refolding, or trafficking them for degradation. The chaperone activities of Hsps are dependent on dynamic protein-protein interactions, including their oligomerisation i...

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Bibliographic Details
Main Authors: Rebecca San Gil, Tracey Berg, Heath Ecroyd
Format: article
Language:EN
Published: Nature Portfolio 2017
Subjects:
R
Q
Online Access:https://doaj.org/article/c5b805513f5c4a0f924c87f420a182b2
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