An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity

Heat shock proteins of 70 kDa (Hsp70s) are ubiquitous and highly conserved molecular chaperones. They play multiple essential roles in assisting with protein folding and maintaining protein homeostasis. Their chaperone activity has been proposed to require several rounds of binding to and release of...

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Bibliografiske detaljer
Udgivet i:J Biol Chem
Main Authors: Li, Hongtao, Zhu, Huanyu, Sarbeng, Evans Boateng, Liu, Qingdai, Tian, Xueli, Yang, Ying, Lyons, Charles, Zhou, Lei, Liu, Qinglian
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2020
Fag:
Enzymology
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC6956537/
https://ncbi.nlm.nih.gov/pubmed/31806707
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.009686
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