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Thermodynamics of Binding of Structurally Similar Ligands to Histone Deacetylase 8 Sheds Light on Challenges in the Rational Design of Potent and Isozyme-Selective Inhibitors of the Enzyme
[Image: see text] Among the different histone deacetylase (HDAC) isozymes, HDAC8 is the most highly malleable enzyme, and it exhibits the potential to accommodate structurally diverse ligands (albeit with moderate binding affinities) in its active site pocket. To probe the molecular basis of this fe...
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| 出版年: | Biochemistry |
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| 主要な著者: | , , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American
Chemical Society
2014
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| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4263425/ https://ncbi.nlm.nih.gov/pubmed/25407689 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi500711x |
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