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Crystallographic and SAR Analyses Reveal High Requirement to Selectively and Potently Inhibit SIRT2 Deacetylase and Decanoylase

Abstract

A high-quality X-ray crystal structure reveals the mechanism of compound 1a inhibiting SIRT2 deacetylase and decanoylase. Structure-activity relationship (SAR) analysis of the synthesized derivatives of 1a reveals the high requirement for selective inhibitors to accommodate with the induced hydrophobic pocket and potently inhibit sirtuin 2 deacylase.

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Publication details

The article was received on 13 Sep 2018, accepted on 06 Dec 2018 and first published on 07 Dec 2018


Article type: Research Article
DOI: 10.1039/C8MD00462E
Citation: Med. Chem. Commun., 2018, Accepted Manuscript
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    Crystallographic and SAR Analyses Reveal High Requirement to Selectively and Potently Inhibit SIRT2 Deacetylase and Decanoylase

    L. Yang, W. Xu, J. Yan, H. Su, Y. Chen, C. Li, X. Zhang, Z. Yu, Y. Yan, Y. Yu, Q. Chen, Z. Wang, L. Li, S. Qian and G. Li, Med. Chem. Commun., 2018, Accepted Manuscript , DOI: 10.1039/C8MD00462E

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