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Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins

Heat shock protein 90 (Hsp90) accounts for 1–2% of the total proteins in normal cells and functions as a molecular chaperone that folds, assembles, and stabilizes client proteins. Hsp90 is over-expressed (3–6-fold increase) in stressed cells, including cancer cells, and regulates over 200 client and...

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Detalles Bibliográficos
Main Authors: Ardi, Veronica C., Alexander, Leslie D., Johnson, Victoria, McAlpine, Shelli R.
Formato: Artigo
Idioma:Inglês
Publicado: 2011
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3241894/
https://ncbi.nlm.nih.gov/pubmed/21950602
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/cb200203m
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