Phosphorylation Dependence of Hsp27 Multimeric Size and Molecular Chaperone Function

The molecular chaperone Hsp27 exists as a distribution of large oligomers that are disassembled by phosphorylation at Ser-15, -78, and -82. It is controversial whether the unphosphorylated Hsp27 or the widely used triple Ser-to-Asp phospho-mimic mutant is the more active molecular chaperone in vitro...

Full description

Saved in:
Bibliographic Details
Main Authors: Hayes, David, Napoli, Vanessa, Mazurkie, Andrew, Stafford, Walter F., Graceffa, Philip
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2009
Subjects:
Protein Structure and Folding
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2707219/
https://ncbi.nlm.nih.gov/pubmed/19411251
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.011353
Tags: Add Tag
No Tags, Be the first to tag this record!

Similar Items