Hsp110 Is a Bona Fide Chaperone Using ATP to Unfold Stable Misfolded Polypeptides and Reciprocally Collaborate with Hsp70 to Solubilize Protein Aggregates

Structurally and sequence-wise, the Hsp110s belong to a subfamily of the Hsp70 chaperones. Like the classical Hsp70s, members of the Hsp110 subfamily can bind misfolding polypeptides and hydrolyze ATP. However, they apparently act as a mere subordinate nucleotide exchange factors, regulating the abi...

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Detaylı Bibliyografya
Asıl Yazarlar: Mattoo, Rayees U. H., Sharma, Sandeep K., Priya, Smriti, Finka, Andrija, Goloubinoff, Pierre
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: American Society for Biochemistry and Molecular Biology 2013
Konular:
Protein Structure and Folding
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC3774407/
https://ncbi.nlm.nih.gov/pubmed/23737532
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.479253
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