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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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Detalhes bibliográficos
Main Authors: Goloubinoff, Pierre, Mogk, Axel, Zvi, Anat Peres Ben, Tomoyasu, Toshifumi, Bukau, Bernd
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 1999
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC24133/
https://ncbi.nlm.nih.gov/pubmed/10570141
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