Isotopically Labeled Clickable Glutathione to Quantify Protein S‐Glutathionylation
Sign Up to like & getrecommendations! Published in 2019 at "ChemBioChem"
DOI: 10.1002/cbic.201900528
Abstract: Protein S‐glutathionylation is one of the important cysteine oxidation events that regulate various redox‐mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S‐glutathionylation.… read more here.
Keywords: glutathionylation; labeled clickable; protein glutathionylation; isotopically labeled ... See more keywords
Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation.
Sign Up to like & getrecommendations! Published in 2017 at "Biophysical journal"
DOI: 10.1016/j.bpj.2017.08.059
Abstract: Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence… read more here.
Keywords: protein; glutathionylation; kinase; receptor ... See more keywords
Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.
Sign Up to like & getrecommendations! Published in 2019 at "Chemico-biological interactions"
DOI: 10.1016/j.cbi.2018.12.003
Abstract: Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated… read more here.
Keywords: buffering capacity; redox buffering; protein glutathionylation; glutathionylation ... See more keywords
Contribution of glutaredoxin-1 to Fas s-glutathionylation and inflammation in ethanol-induced liver injury.
Sign Up to like & getrecommendations! Published in 2020 at "Life sciences"
DOI: 10.1016/j.lfs.2020.118678
Abstract: AIMS The reversible protein S-glutathionylation (PSSG) modification of Fas augments apoptosis, which can be reversed by the cytosolic deglutathionylation enzyme glutaredoxin-1 (Grx1), but its roles in alcoholic liver injury remain unknown. Therefore, the objective of… read more here.
Keywords: fas; glutathionylation; grx1; ethanol induced ... See more keywords
High glutathionylation of placental endothelial nitric oxide synthase in preeclampsia
Sign Up to like & getrecommendations! Published in 2019 at "Redox Biology"
DOI: 10.1016/j.redox.2019.101126
Abstract: Decreased nitric oxide (NO) bioavailability plays a critical role in the pathophysiology of preeclampsia (PE). Recent evidence indicates that S-glutathionylation may occur on the endothelial nitric oxide synthase (eNOS), leading to eNOS uncoupling, characterized by… read more here.
Keywords: endothelial nitric; po2; glutathionylation; enos glutathionylation ... See more keywords
S-glutathionylation, friend or foe in cardiovascular health and disease
Sign Up to like & getrecommendations! Published in 2020 at "Redox Biology"
DOI: 10.1016/j.redox.2020.101693
Abstract: Glutathione is a low molecular weight thiol that is present at high levels in the cell. The high levels of glutathione in the cell make it one of the most abundant antioxidants contributing to cellular… read more here.
Keywords: glutathionylation; foe cardiovascular; disease; cardiovascular health ... See more keywords
Glutathionylation Inhibits the Catalytic Activity of Arabidopsis β-Amylase3 but Not That of Paralog β-Amylase1.
Sign Up to like & getrecommendations! Published in 2018 at "Biochemistry"
DOI: 10.1021/acs.biochem.7b01274
Abstract: β-Amylase3 (BAM3) is an enzyme that is essential for starch degradation in plant leaves and is also transcriptionally induced under cold stress. However, we recently reported that BAM3's enzymatic activity decreased in cold-stressed Arabidopsis leaves,… read more here.
Keywords: glutathionylation; bam3; amylase3; activity ... See more keywords
Profiling Glutathionylome in CD38-Mediated Epithelial-Mesenchymal Transition.
Sign Up to like & getrecommendations! Published in 2022 at "Journal of proteome research"
DOI: 10.1021/acs.jproteome.1c00893
Abstract: Protein S-glutathionylation is an important posttranslational modification that regulates various cellular processes. However, changes in glutathionylome in epithelial-mesenchymal transition (EMT), a crucial cellular process for embryonic development, wound healing, and carcinoma progression and metastasis, have… read more here.
Keywords: glutathionylation; epithelial mesenchymal; glutathionylome cd38; cd38 ... See more keywords
Glutathionylation of Yersinia pestis LcrV and Its Effects on Plague Pathogenesis
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DOI: 10.1128/mbio.00646-17
Abstract: ABSTRACT Glutathionylation, the formation of reversible mixed disulfides between glutathione and protein cysteine residues, is a posttranslational modification previously observed for intracellular proteins of bacteria. Here we show that Yersinia pestis LcrV, a secreted protein… read more here.
Keywords: glutathionylation; pestis; virulence; plague pathogenesis ... See more keywords
A Phase 1 dose-escalation study of disulfiram and copper gluconate in patients with advanced solid tumors involving the liver using S-glutathionylation as a biomarker
Sign Up to like & getrecommendations! Published in 2021 at "BMC Cancer"
DOI: 10.1186/s12885-021-08242-4
Abstract: Background Disulfiram and metals inactivate key oncoproteins resulting in anti-neoplastic activity. The goal of this study was to determine the maximum tolerated dose of copper when administered with disulfiram in patients with advanced solid tumors… read more here.
Keywords: copper gluconate; solid tumors; glutathionylation; copper ... See more keywords
Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues
Sign Up to like & getrecommendations! Published in 2017 at "Journal of Cell Science"
DOI: 10.1242/jcs.202853
Abstract: ABSTRACT Cch1p, the yeast homolog of the pore-forming subunit α1 of the mammalian voltage-gated Ca2+ channel (VGCC), is located on the plasma membrane and mediates the redox-dependent influx of Ca2+. Cch1p is known to undergo… read more here.
Keywords: glutathionylation; cch1p; yeast; activation ... See more keywords