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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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: Li, Hongtao, Zhu, Huanyu, Sarbeng, Evans Boateng, Liu, Qingdai, Tian, Xueli, Yang, Ying, Lyons, Charles, Zhou, Lei, Liu, Qinglian
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2020
Assuntos:
Enzymology
Acesso em linha: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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