Cover Picture: Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase (ChemBioChem 8/2014) | Zendy

Oh Angela | Zendy; Ho YenChing | Zendy; Zak Mark | Zendy; Liu Yongbo | Zendy; Chen Xukun | Zendy; Yuen Powai | Zendy; Zheng Xiaozhang | Zendy; Liu Yichin | Zendy; Dragovich Peter S. | Zendy; Wang Weiru | Zendy

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

Author(s) -

Oh Angela,

Ho YenChing,

Zak Mark,

Liu Yongbo,

Chen Xukun,

Yuen Powai,

Zheng Xiaozhang,

Liu Yichin,

Dragovich Peter S.,

Wang Weiru

Publication year - 2014

Publication title -

chembiochem

Language(s) - English

Resource type - Reports

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.201490024

Subject(s) - nicotinamide phosphoribosyltransferase , chemistry , potency , adduct , nicotinamide , stereochemistry , biochemistry , nad+ kinase , enzyme , in vitro , organic chemistry

The cover picture shows a crystal structure of nicotinamide phosphoribosyltransferase (NAMPT) in complex with an inhibitor adduct. Some NAMPT inhibitors undergo NAMPT‐dependent phosphoribosylation. On p. 1121 ff., 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.

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