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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...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2011
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| Aiheet: | |
| Linkit: | 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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