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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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Auteurs principaux: Goloubinoff, Pierre, Mogk, Axel, Zvi, Anat Peres Ben, Tomoyasu, Toshifumi, Bukau, Bernd
Format: Artigo
Langue:Inglês
Publié: National Academy of Sciences 1999
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Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC24133/
https://ncbi.nlm.nih.gov/pubmed/10570141
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