Structure-function roles of four cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT) by site-directed mutagenesis.
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Candidate single nucleotide polymorphism markers for arsenic responsiveness of protein targetsArsenic binding to proteinsIdentification of the third binding site of arsenic in human arsenic (III) methyltransferaseEvolution- and structure-based computational strategy reveals the impact of deleterious missense mutations on MODY 2 (maturity-onset diabetes of the young, type 2)CoagVDb: a comprehensive database for coagulation factors and their associated SAPsIn silico profiling of deleterious amino acid substitutions of potential pathological importance in haemophlia A and haemophlia B.Interspecies differences in metabolism of arsenic by cultured primary hepatocytesPathway of human AS3MT arsenic methylation.Residues in human arsenic (+3 oxidation state) methyltransferase forming potential hydrogen bond network around S-adenosylmethionine.Synthesis, biocompatible, and self-assembly properties of poly (ethylene glycol)/lactobionic acid-grafted chitosan.The functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferaseMethylation of arsenic by recombinant human wild-type arsenic (+3 oxidation state) methyltransferase and its methionine 287 threonine (M287T) polymorph: Role of glutathione.Rapid equilibrium kinetic analysis of arsenite methylation catalyzed by recombinant human arsenic (+3 oxidation state) methyltransferase (hAS3MT).Comparative oxidation state specific analysis of arsenic species by high-performance liquid chromatography-inductively coupled plasma-mass spectrometry and hydride generation-cryotrapping-atomic absorption spectrometryIdentification and catalytic residues of the arsenite methyltransferase from a sulfate-reducing bacterium, Clostridium sp. BXM.Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S-adenosylmethionine.
P2860
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P2860
Structure-function roles of four cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT) by site-directed mutagenesis.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Structure-function roles of fo ...... by site-directed mutagenesis.
@en
Structure-function roles of four cysteine residues in the human arsenic
@nl
type
label
Structure-function roles of fo ...... by site-directed mutagenesis.
@en
Structure-function roles of four cysteine residues in the human arsenic
@nl
prefLabel
Structure-function roles of fo ...... by site-directed mutagenesis.
@en
Structure-function roles of four cysteine residues in the human arsenic
@nl
P2093
P1476
Structure-function roles of fo ...... ) by site-directed mutagenesis
@en
P2093
Chengying Li
Jingshu Zhu
Ningsheng Bian
Xiaoli Song
Xinrong Zhang
Zhilin Wang
Zhirong Geng
P304
P356
10.1016/J.CBI.2008.12.018
P50
P577
2009-01-10T00:00:00Z