Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
about
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes.Systematic and quantitative assessment of hydrogen peroxide reactivity with cysteines across human proteomes.Specificity of reversible ADP-ribosylation and regulation of cellular processes.Mass-Tag Labeling Using Acyl-PEG Exchange for the Determination of Endogenous Protein S-Fatty Acylation.
P2860
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
description
2017 nî lūn-bûn
@nan
2017年の論文
@ja
2017年学术文章
@wuu
2017年学术文章
@zh
2017年学术文章
@zh-cn
2017年学术文章
@zh-hans
2017年学术文章
@zh-my
2017年学术文章
@zh-sg
2017年學術文章
@yue
2017年學術文章
@zh-hant
name
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@en
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@nl
type
label
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@en
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@nl
prefLabel
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@en
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@nl
P2093
P2860
P356
P1476
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress.
@en
P2093
Henrik Molina
Howard C Hang
Joseph P Fernandez
Nathan P Westcott
P2860
P2888
P304
P356
10.1038/NCHEMBIO.2280
P577
2017-01-16T00:00:00Z