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Structure based design of a Grp94-selective inhibitor: Exploiting a key residue in Grp94 to optimize paralog-selective binding
Grp94 and Hsp90, the ER and cytoplasmic hsp90 paralogs, share a conserved ATP-binding pocket that has been targeted for therapeutics. Paralog-selective inhibitors may lead to drugs with fewer side effects. Here, we analyzed 1 (BnIm), a benzyl imidazole resorcinylic inhibitor, for its mode of binding...
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| 出版年: | J Med Chem |
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| 主要な著者: | , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2018
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5897183/ https://ncbi.nlm.nih.gov/pubmed/29528635 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.jmedchem.7b01608 |
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