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MetabolomicsRedox proteomics reveal a role for peroxiredoxinylation in stress protection.

The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional...

2025-07-17 | MTBLS11979 | MetaboLights
ProteomicsQuantitative thiol reactivity profiling
Cysteine is unique among all protein-coding amino acids owing to its intrinsically high nucleophilicity. The cysteinyl thiol group can be covalently modified by both a broad range of redox mechanisms and various electrophiles derived from exogenous or endogenous sources. Measuring proteomic cysteine...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2020-07-24 | PXD016048 | Pride
Thiol Redox Chemical proteomics Electrophile 
ProteomicsComprehensive redox profiling of the thiol proteome of Clostridium difficile
The strictly anaerobic bacterium C. difficile has become one of the most problematic hospital acquired pathogens and a major burden for health care systems. Although antibiotics work effectively in most C. difficile infections (CDIs), their detrimental effect on the intestinal microbiome paves the w...
ORGANISM(S): Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2018-03-05 | PXD007278 | Pride
Thiol redox proteomics Clostridium difficile 
ProteomicsSpecificity and dynamics of H2O2 detoxification by the cytosolic redox regulatory network as revealed by in vitro reconstitution
The thiol redox state is a decisive functional characteristic of proteins in cell biology. Plasmatic cell compartments maintain a thiol-based redox regulatory network linked to the glutathione/glutathione disulfide couple (GSH/GSSG) and the NAD(P)H system. The basic network constituents are known an...
ORGANISM(S): Escherichia Coli 
2025-01-21 | PXD048374 | JPOST Repository
ProteomicsClick Chemistry-based Thiol Redox Proteomics Reveals Significant Cysteine Reduction Induced by Chronic Ethanol Consumption
In the U.S., alcohol-associated liver disease (ALD) impacts millions of people and is a major healthcare burden. While the pathology of ALD is unmistakable, the molecular mechanisms underlying ethanol hepatotoxicity are not fully understood. Hepatic ethanol metabolism is intimately linked with alte...
ORGANISM(S): Mus musculus (Mouse) 
2024-09-19 | PXD042070 | Pride
Redox proteomics Proteomics Glutathione Mus musculus Agilent 6550 q-tof Redox Cysteine Thiol Click chemistry Alcohol-associated liver disease 
UnknownThiol redox proteomics: Characterization of thiol-based post-translational modifications.
Not available
S-EPMC10764013 | biostudies-literature
ProteomicsStochiometric Quantification of the Thiol Redox Proteome Reveals Subcellular Compartmentalization and Susceptibility to Oxidative Perturbations
Posttranslational modifications of protein cysteine thiols play a significant role in redox regulation and the pathogenesis of human diseases. However, the cellular redox landscape in terms of quantitative, site-specific occupancies of thiol modifications at the proteome level, especially under phys...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-13 | PXD019913 | Pride
Site-occupancy Macrophage Resin-assisted enrichment Redox proteomics S-glutathionylation Stoichiometry Redox modification Protein thiols 
ProteomicsQuantifying changes in the bacterial thiol redox proteome during host-pathogen interaction
In this study, we used a quantitative redox proteomic method (OxICAT) to assess the in vivo thiol oxidation status of phagocytized E. coli. The majority (65.5%) of identified proteins harbored thiols that were significantly oxidized (>30%) upon phagocytosis. A substantial number of these proteins ar...
ORGANISM(S): Escherichia coli 
2019-01-07 | PXD011386 | Pride
Plb-985 Neutrophils Escherichia coli Redox proteomics 
UnknownStoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.
Not available
S-EPMC8004825 | biostudies-literature
Proteomicscys TMTRAQ_an integrative method for unbiased thiol-based redox proteomics
quantification of protein redox regulation. we combine cysteine reaction tandem mass tag(cysTMT) and isobaric tag for relative abd absolute quantification( ITRAQ) in one one experiment. we developed a double labeling strategy using iTRAQ and cysTMT in one experiment for simultaneous determination of...
ORGANISM(S): Homo sapiens (Human) 
2017-02-02 | PXD001319 | Pride
Itraq Cys tmtraq Cystmt 
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