Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90

The molecular chaperone heat shock protein 90 (Hsp90) and the co-chaperone/ubiquitin ligase carboxyl terminus of Hsc70-interacting protein (CHIP) control the turnover of client proteins. How this system decides to stabilize or degrade the client proteins under particular physiological or pathologica...

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Detalles Bibliográficos
Autores principales: Yan, Shan, Sun, Xuxu, Xiang, Binggang, Cang, Hui, Kang, Xunlei, Chen, Yuying, Li, Hui, Shi, Guiying, Yeh, Edward T H, Wang, Beilei, Wang, Xiangrui, Yi, Jing
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2989103/
https://www.ncbi.nlm.nih.gov/pubmed/20924358
http://dx.doi.org/10.1038/emboj.2010.245

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2989103/
https://www.ncbi.nlm.nih.gov/pubmed/20924358
http://dx.doi.org/10.1038/emboj.2010.245

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