Cover Picture: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase (ChemBioChem 8/2014). Issue 8 (26th May 2014)

• Record Type: Journal Article
• Authors: Oh, Angela; Ho, Yen‐Ching; Zak, Mark; Liu, Yongbo; Chen, Xukun; Yuen, Po‐wai; Zheng, Xiaozhang; Liu, Yichin; Dragovich, Peter S.; Wang, Weiru
• Is Part Of: Chembiochem. Volume 15:Issue 8(2014)
• Page Start: 1053
• Page End: 1053
• Publication Date: 2014-05-26
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201490024
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> a crystal structure of nicotinamide phosphoribosyltransferase (NAMPT) in complex with an inhibitor adduct. Some NAMPT inhibitors undergo NAMPT‐dependent phosphoribosylation. On <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 1121 ff., </ext-link> W. Wang et al. explain how crystallography analysis and biochemical studies have revealed that the binding characteristics of the inhibitor adduct are a key determinant of the time‐dependent inhibitory potency, and contribute to sustained inhibition in cellular environments.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgh7g00hn3" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>