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The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

The heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential in numerous cellular processes. Its three domains (N, M, and C) are connected via linkers that allow the rearrangement of domains during Hsp90’s chaperone cycle. A unique linker, called charged linker (CL), connects the N-...

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Podrobná bibliografie
Vydáno v:Proc Natl Acad Sci U S A
Hlavní autoři: Jahn, Markus, Rehn, Alexandra, Pelz, Benjamin, Hellenkamp, Björn, Richter, Klaus, Rief, Matthias, Buchner, Johannes, Hugel, Thorsten
Médium: Artigo
Jazyk:Inglês
Vydáno: National Academy of Sciences 2014
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC4273377/
https://ncbi.nlm.nih.gov/pubmed/25468961
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1414073111
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