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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Publicado en:J Biol Chem
Autores principales: Li, Hongtao, Zhu, Huanyu, Sarbeng, Evans Boateng, Liu, Qingdai, Tian, Xueli, Yang, Ying, Lyons, Charles, Zhou, Lei, Liu, Qinglian
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Biochemistry and Molecular Biology 2020
Materias:
Enzymology
Acceso en línea: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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