Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases - Wikidata - awgldk - TriplyDB

Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

http://www.wikidata.org/entity/Q27646887

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Prospective virtual screening with Ultrafast Shape Recognition: the identification of novel inhibitors of arylamine N-acetyltransferases Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery Polymorphisms in the human cytochrome P450 and arylamine N-acetyltransferase: susceptibility to head and neck cancers PharmGKB summary: very important pharmacogene information for N-acetyltransferase 2 Piperidinols That Show Anti-Tubercular Activity as Inhibitors of Arylamine N-Acetyltransferase: An Essential Enzyme for Mycobacterial Survival Inside Macrophages Structural and Biochemical Characterization of an Active Arylamine N-Acetyltransferase Possessing a Non-canonical Cys-His-Glu Catalytic Triad Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity Insight into cofactor recognition in arylamine N-acetyltransferase enzymes: structure of Mesorhizobium loti arylamine N-acetyltransferase in complex with coenzyme A Effects of single nucleotide polymorphisms on human N-acetyltransferase 2 structure and dynamics by molecular dynamics simulation A novel color change mechanism for breast cancer biomarker detection: naphthoquinones as specific ligands of human arylamine N-acetyltransferase 1 From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN)NAT1 and its homologue (MOUSE)NAT2 Rapid birth-and-death evolution of the xenobiotic metabolizing NAT gene family in vertebrates with evidence of adaptive selection Identification of cancer chemopreventive isothiocyanates as direct inhibitors of the arylamine N-acetyltransferase-dependent acetylation and bioactivation of aromatic amine carcinogens Polymorphisms in NAT2 (N-acetyltransferase 2) gene in patients with systemic lupus erythematosus.Probing the catalytic potential of the hamster arylamine N-acetyltransferase 2 catalytic triad by site-directed mutagenesis of the proximal conserved residue, Tyr190.Differences between murine arylamine N-acetyltransferase type 1 and human arylamine N-acetyltransferase type 2 defined by substrate specificity and inhibitor binding.Homologues of xenobiotic metabolizing N-acetyltransferases in plant-associated fungi: Novel functions for an old enzyme family.Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2 Treatment of Rats with Apocynin Has Considerable Inhibitory Effects on Arylamine N-Acetyltransferase Activity in the Liver.Arylamine N-acetyltransferases in mycobacteria.Update on the pharmacogenetics of NATs: structural considerations.Insights into how protein dynamics affects arylamine N-acetyltransferase catalysis.Crystal structure of arylamine N-acetyltransferases: insights into the mechanisms of action and substrate selectivity.Arylamine N-acetyltransferases: a structural perspective.Design strategy for photoinduced electron transfer-based small-molecule fluorescent probes of biomacromolecules.Molecular characterization of a novel N-acetyltransferase from Chryseobacterium sp.Evaluation of a New Molecular Entity as a Victim of Metabolic Drug-Drug Interactions-an Industry Perspective.Mechanisms and kinetics of human arylamine N-acetyltransferase 1 inhibition by disulfiram.The Role of N-Acetyl Transferases on Isoniazid Resistance from Mycobacterium tuberculosis and Human: An In Silico Approach.Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1.Xenobiotic-metabolizing enzymes in Bacillus anthracis: molecular and functional analysis of a truncated arylamine N-acetyltransferase isozyme.Current trends in N-acetyltransferase research arising from the 2007 International NAT Workshop.Comparative analysis of xenobiotic metabolising N-acetyltransferases from ten non-human primates as in vitro models of human homologues.

P2860

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P2860

Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

http://www.wikidata.org/entity/Q27646887

description

2007 nî lūn-bûn

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2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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name

Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Journal of Biological Chemistry

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Alexander N Plotnikov

http://www.w3.org/2001/XMLSchema#string

Denis M Grant

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Fernando Martin

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Geoffrey H Goodfellow

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Hong Wu

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Ludmila Dombrovsky

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P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases

Structure of arylamine N-acetyltransferase reveals a catalytic triad

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

Substructure solution with SHELXD

Likelihood-enhanced fast translation functions

The Amber biomolecular simulation programs

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10.1074/JBC.M704138200

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41

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282

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