Residues in human arsenic (+3 oxidation state) methyltransferase forming potential hydrogen bond network around S-adenosylmethionine.
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Identification of the third binding site of arsenic in human arsenic (III) methyltransferaseThe functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferaseStructural Analysis of Glycine Sarcosine N-methyltransferase from Methanohalophilus portucalensis Reveals Mechanistic Insights into the Regulation of Methyltransferase Activity.
P2860
Residues in human arsenic (+3 oxidation state) methyltransferase forming potential hydrogen bond network around S-adenosylmethionine.
description
2013 nî lūn-bûn
@nan
2013 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@ast
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@en
type
label
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@ast
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@en
prefLabel
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@ast
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@en
P2093
P2860
P1433
P1476
Residues in human arsenic (+3 ...... k around S-adenosylmethionine.
@en
P2093
Shuping Wang
Xiangli Li
Xiaoli Song
Zhilin Wang
Zhirong Geng
P2860
P304
P356
10.1371/JOURNAL.PONE.0076709
P407
P50
P577
2013-10-04T00:00:00Z