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Issue 1, 2019
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Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

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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 requirements needed for selective inhibitors to bind with the induced hydrophobic pocket and potently inhibit sirtuin 2 deacetylase.

Graphical abstract: Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

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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., 2019,10, 164-168

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    Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

    L. Yang, W. Xu, J. Yan, H. Su, C. Yuan, C. Li, X. Zhang, Z. Yu, Y. Yan, Y. Yu, Q. Chen, Z. Wang, L. Li, S. Qian and G. Li, Med. Chem. Commun., 2019, 10, 164
    DOI: 10.1039/C8MD00462E

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