Title : Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.

Pub. Date : 2019 Feb 8

PMID : 30455352






1 Functional Relationships(s)
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1 Hsp70 chaperones are central hubs of the protein quality control network and collaborate with co-chaperones having a J-domain (an ~70-residue-long helical hairpin with a flexible loop and a conserved His-Pro-Asp motif required for ATP hydrolysis by Hsp70s) and also with nucleotide exchange factors to facilitate many protein-folding processes that (re)establish protein homeostasis. Aspartic Acid heat shock protein family A (Hsp70) member 4 Homo sapiens