Asymmetric Hsp90 N-domain SUMOylation recruits Aha1 and ATP-competitive inhibitors

The stability and activity of numerous signaling proteins in both normal and cancer cells depends on the dimeric molecular chaperone Heat Shock Protein 90 (Hsp90). Hsp90 function is coupled to ATP binding and hydrolysis, and requires a series of conformational changes that are regulated by co-chaper...

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Main Authors: Mollapour, Mehdi, Bourboulia, Dimitra, Beebe, Kristin, Woodford, Mark R., Polier, Sigrun, Hoang, Anthony, Chelluri, Raju, Li, Yu, Guo, Ailan, Lee, Min-Jung, Fotooh-Abadi, Elham, Khan, Sahar, Prince, Thomas, Miyajima, Naoto, Yoshida, Soichiro, Tsutsumi, Shinji, Xu, Wanping, Panaretou, Barry, Stetler-Stevenson, William G., Bratslavsky, Gennady, Trepel, Jane B., Prodromou, Chrisostomos, Neckers, Len
格式: Artigo
語言:Inglês
出版: 2014
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC3964875/
https://ncbi.nlm.nih.gov/pubmed/24462205
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2013.12.007
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