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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Auteurs principaux: Rebecca San Gil, Tracey Berg, Heath Ecroyd
Format: article
Langue:EN
Publié: Nature Portfolio 2017
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Accès en ligne:https://doaj.org/article/c5b805513f5c4a0f924c87f420a182b2
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