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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.
Hsp90 is an abundant molecular chaperone essential to the establishment of many cellular regulation and signal transduction systems, but remains one of the least well described chaperones. The biochemical mechanism of protein folding by Hsp90 is poorly understood, and the direct involvement of ATP h...
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| Auteurs principaux: | , , , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
1998
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1170812/ https://ncbi.nlm.nih.gov/pubmed/9707442 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/17.16.4829 |
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