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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...
Autores principales: | Sluder, Isaac T., Nitika, Knighton, Laura E., Truman, Andrew W. |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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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 |
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