Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue.
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The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancerThioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae.Inhibition of caspase-3 activity and activation by protein glutathionylation.Evaluation of a dithiocarbamate derivative as a model of thiol oxidative stress in H9c2 rat cardiomyocytes.Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines.Regulation of mitochondrial processes by protein S-nitrosylation.Glutathione disulfide induces neural cell death via a 12-lipoxygenase pathway.Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegansRedox proteomics: identification and functional role of glutathionylated proteins.In vivo tagging and characterization of S-glutathionylated proteins by a chemoenzymatic method.Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damageDehydroalanine analog of glutathione: an electrophilic busulfan metabolite that binds to human glutathione S-transferase A1-1.Elucidation of thioredoxin target protein networks in mouse.Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.Redox modulation of endothelial nitric oxide synthase by glutaredoxin-1 through reversible oxidative post-translational modification.Thiol-based redox switches in eukaryotic proteins.S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensingThe glutathione system: a new drug target in neuroimmune disorders.Glutathionylspermidine in the modification of protein SH groups: the enzymology and its application to study protein glutathionylation.The minor structural difference between the antioxidants quercetin and 4'O-methylquercetin has a major impact on their selective thiol toxicity.Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells.Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster.S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signalingContributions to catalysis and potential interactions of the three catalytic domains in a contiguous trimeric creatine kinase.Top-down characterization of endogenous protein complexes with native proteomics.Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle.
P2860
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P2860
Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue.
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Inactivation of creatine kinas ...... active-site cysteine residue.
@ast
Inactivation of creatine kinas ...... active-site cysteine residue.
@en
type
label
Inactivation of creatine kinas ...... active-site cysteine residue.
@ast
Inactivation of creatine kinas ...... active-site cysteine residue.
@en
prefLabel
Inactivation of creatine kinas ...... active-site cysteine residue.
@ast
Inactivation of creatine kinas ...... active-site cysteine residue.
@en
P2093
P2860
P1433
P1476
Inactivation of creatine kinas ...... active-site cysteine residue.
@en
P2093
P2860
P304
P356
10.1042/0264-6021:3470821
P407
P478
P577
2000-05-01T00:00:00Z