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ProteomicsReactive Metabolite-induced Protein Glutathionylation Mechanistically Accounts for Acetaminophen Hepatotoxicity
Although covalent protein binding is established as the pivotal event underpinning acetaminophen (APAP) toxicity, its mechanistic details remain unclear. In this study, we demonstrated that APAP induces widespread protein glutathionylation in a time-, dose- and bioactivation-dependent manner in Hepa...
ORGANISM(S): Homo Sapiens (human) 
2018-09-20 | PXD009986 | JPOST Repository
ProteomicsSite-specific Identification of Glutathionylation
Cardiomyocytes proteins were investigated for their glutathionylation in response to hydrogen peroxide generated from glucose oxidase and using a clickable glutathione derivative. After exposure, or not, to hydrogen peroxide the glutathionylated proteins were enriched and LC-MS/MS analyses was perfo...
ORGANISM(S): Mus musculus (Mouse) 
2019-03-06 | PXD012171 | Pride
Ptm Glutathionylation Affinity purification 
ProteomicsThe adaptive metabolic response involves specific protein glutathionylation during the filamentation process in the pathogen Candida albicans
Candida albicans is an opportunist pathogen responsible for a large spectrum of infections, from superficial mycosis to the systemic disease candidiasis. Its ability to adopt various morphological forms, such as unicellular yeasts, filamentous pseudohyphae and hyphae, contributes to its ability to s...
ORGANISM(S): Candida albicans (Yeast) 
2016-04-21 | PXD003685 | Pride
Candida albicans / filamentation/ glutathionylation/ isocitrate lyase / mitochondria 
ProteomicsIsotopic-labelled Clickable Glutathione to Quantify Protein S-Glutathionylation
Investigated protein glutathionylation in HL-1 cardiomyocyte cells in response to hydrogen peroxide using a clickable glutathione approach. After exposure, or not, to hydrogen peroxide the glutathionylated proteins with heavy or light azido glutathione were enriched and subjected to LC-MS/MS analysi...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-08 | PXD014937 | Pride
Clickable glutathione Glutathionylation Cardiomyocyte 
ProteomicsS-glutathionylation proteome profiling of Streptococcus mutans
S-glutathionylation is an important post-translational modification (PTM) process that targets the protein cysteine thiol by the addition of glutathione (GSH). This modification can prevent proteolysis from over-oxidation of protein cysteine residue during the condition of oxidative or nitrosative s...
ORGANISM(S): Streptococcus mutans UA159 
2020-07-14 | PXD019564 | Pride
S-glutathionylation  streptococcus mutans  post-translational modification 
ProteomicsClickable glutathione-based Isotope Coded Affinity Label to quantify glutathionylation
Identification of cysteines with high oxidation susceptibility is important for understanding redox-mediated biological processes associated with health and disease. We developed a chemical proteomic strategy that helps find cysteines with high susceptibility to S-glutathionylation. Our strategy is ...
ORGANISM(S): Mus musculus (Mouse) 
2024-03-07 | PXD034976 | Pride
Lc-ms/ms for glutathionylation in mouse c2c12 
ProteomicsMass-spectroscopic quantification of CHAC1-regulated protein cysteine S-glutathionylation
S-glutathionylation is an important post-translational modification of a cysteine residue of target protein. We applied a quantitative redox proteomics approach to identify the specific cysteine residues as targets of S-glutathionylation. Using this approach, we profiled CHAC1-associated changes in ...
ORGANISM(S): Mus Musculus 
2024-03-12 | PXD050569 |
ProteomicsClickable Glutathione Approach for Identification of Protein Glutathionylation in Response to Glucose Metabolism
Glucose metabolism and mitochondrial function are closely interconnected with cellular redox-homeostasis. Although glucose starvation, which often occurs in ischemic heart or insufficient vascularization of tumor cells, is known to induce redox-disturbance, global and individual protein glutathionyl...
ORGANISM(S): Homo sapiens (Human) 
2018-10-26 | PXD004026 | Pride
Glutathionylation 
ProteomicsProtein S-glutathionylation in HeLa cells identified by nanoLC-LTQ-Orbitrap XL MS/MS
Cysteine modifications have been widely detected among different protein in different species. Here, we examined protein glutathionylation in HeLa cells under both untreated and diamide-treated conditions. A strategy using resin-assisted enrichment of glutathionylated proteins or peptides after biot...
ORGANISM(S): Homo sapiens (Human) 
2020-04-29 | PXD017717 | Pride
Nanolc-ltq-orbitrap xl ms/ms Biotin switch S-glutathionylation 
ProteomicsAlterations of protein S-glutathionylation modification in macrophages under oxidative conditions
S-glutathionylation is an important regulatory posttranslational modification of protein cysteine (Cys) thiols, yet the role of specific cysteine residues as targets of modification is poorly understood. To identify the specific molecular targets and pathways of Grx1 that are susceptible to redox-de...
ORGANISM(S): Mus musculus (Mouse) 
2021-11-01 | PXD027965 | Pride
Bmdm S-glutathionylation Lc–ms/ms 
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