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Heat-inactivated proteins are rescued by the DnaK⋅J-GrpE set and ClpB chaperones

Functional chaperone cooperation between Hsp70 (DnaK) and Hsp104 (ClpB) was demonstrated in vitro. In a eubacterium Thermus thermophilus, DnaK and DnaJ exist as a stable trigonal ring complex (TDnaK⋅J complex) and the dnaK gene cluster contains a clpB gene. When substrate proteins were heated at hig...

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Pubblicato in:Proc Natl Acad Sci U S A
Autori principali: Motohashi, Ken, Watanabe, Yohei, Yohda, Masafumi, Yoshida, Masasuke
Natura: Artigo
Lingua:Inglês
Pubblicazione: National Academy of Sciences 1999
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Accesso online:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC22047/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10377389/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.13.7184
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