Heat shock protein 47 (HSP47) is a molecular chaperone which assists procollagen triple helix assembly and secretion. As a molecular chaperone it is unique in that it binds specifically to a very narrow range of protein "substrates" (i.e., procollagen and collagen only), and it is also a member of t
Structure and function of the molecular chaperone Hsp104 from yeast
β Scribed by Valerie Grimminger-Marquardt; Hilal A. Lashuel
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2010
- Tongue
- English
- Weight
- 982 KB
- Volume
- 93
- Category
- Article
- ISSN
- 0006-3525
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## Abstract For Abstract see ChemInform Abstract in Full Text.
The heat shock proteins (HSP) gp96 and hsp70 have been shown to have a critical role in eliciting adaptive immune responses to cancers and viruses. This role derives from (i) their ability to chaperone antigenic peptides generated in the cells from which the HSP are isolated, and (ii) their capacity
Expression of the Saccharomyces cerevisiae Hsp82 chaperone in a pep4-3and hsc82-deficient strain of S. cerevisiae yielded over 25% of the total cell protein as intact Hsp82. Similarly, the amino-terminal domain (residues 1-220) of Hsp82 was expressed to 18% of the total cell protein. Crystals of the