The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.
Hsp90 is a dimeric ATPase responsible for the activation or maturation of a specific set of substrate proteins termed 'clients'. This molecular chaperone acts in the context of a structurally dynamic and highly regulated cycle involving ATP, co-chaperone proteins and clients. Co-chaperone proteins r...
محفوظ في:
| المؤلفون الرئيسيون: | , , , , |
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| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
Public Library of Science (PLoS)
2012-01-01
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| سلاسل: | PLoS ONE |
| الوصول للمادة أونلاين: | http://europepmc.org/articles/PMC3498168?pdf=render |
| الوسوم: |
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