Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

A major activity of molecular chaperones is to prevent aggregation and refold misfolded proteins. However, when allowed to form, protein aggregates are refolded poorly by most chaperones. We show here that the sequential action of two Escherichia coli chaperone systems, ClpB and DnaK-DnaJ-GrpE, can...

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Pubblicato in:	Proc Natl Acad Sci U S A
Autori principali:	Goloubinoff, Pierre, Mogk, Axel, Zvi, Anat Peres Ben, Tomoyasu, Toshifumi, Bukau, Bernd
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	National Academy of Sciences 1999
Soggetti:	Biological Sciences
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC24133/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10570141/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.24.13732
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