Abstract
Heat shock proteins protect cells from various conditions of stress. Hsp70, the most ubiquitous and highly conserved Hsp, helps proteins adopt native conformation or regain function after misfolding. Various co-chaperones specify Hsp70 function and broaden its substrate range. We discuss Hsp70 structure and function, regulation by co-factors and influence on propagation of yeast prions.
Keywords: Hsp70, chaperone, co-chaperone, prion
Protein & Peptide Letters
Title: Hsp70 Structure, Function, Regulation and Influence on Yeast Prions
Volume: 16 Issue: 6
Author(s): Deepak Sharma and Daniel C. Masison
Affiliation:
Keywords: Hsp70, chaperone, co-chaperone, prion
Abstract: Heat shock proteins protect cells from various conditions of stress. Hsp70, the most ubiquitous and highly conserved Hsp, helps proteins adopt native conformation or regain function after misfolding. Various co-chaperones specify Hsp70 function and broaden its substrate range. We discuss Hsp70 structure and function, regulation by co-factors and influence on propagation of yeast prions.
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Cite this article as:
Sharma Deepak and Masison C. Daniel, Hsp70 Structure, Function, Regulation and Influence on Yeast Prions, Protein & Peptide Letters 2009; 16 (6) . https://dx.doi.org/10.2174/092986609788490230
DOI https://dx.doi.org/10.2174/092986609788490230 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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