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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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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2014
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| 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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