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The Hsp70 co-chaperone Ydj1/HDJ2 regulates ribonucleotide reductase activity

Hsp70 is a well-conserved molecular chaperone involved in the folding, stabilization, and eventual degradation of many “client” proteins. Hsp70 is regulated by a suite of co-chaperone molecules that assist in Hsp70-client interaction and stimulate the intrinsic ATPase activity of Hsp70. While previo...

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Detalles Bibliográficos
Autores principales: Sluder, Isaac T., Nitika, Knighton, Laura E., Truman, Andrew W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277125/
https://www.ncbi.nlm.nih.gov/pubmed/30452489
http://dx.doi.org/10.1371/journal.pgen.1007462