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MetabolomicsGeneration and characterization of thiol-deficient Mycobacterium tuberculosis mutants
Mycothiol (MSH) and ergothioneine (ERG) are thiols able to compensate for each other to protect mycobacteria such as Mycobacterium smegmatis against oxidative stress. Gamma-glutamylcysteine (GGC), another thiol and an intermediate in ERG biosynthesis has detoxification abilities. Five enzymes are in...
2018-07-05 | MTBLS661 | MetaboLights
MetabolomicsSingle-cell thiol profiling enabled by live-cell labeling reveals metabolic heterogeneity in ferroptosis

Raw data of both bulk and single-cell metabolomics. It includes all MS, LC-MS and LC-MS/MS raw data associated with the article 'Single-cell thiol profiling enabled by live-cell labeling reveals metabolic heterogeneity in ferroptosis'.

2026-02-14 | MTBLS13900 | MetaboLights
ProteomicsThiol-cleavable Biotin for Chemical and Enzymatic Biotinylation and its Application to Mitochondrial TurboID Proteomics
Protein biotinylation via chemical or enzymatic reactions is often coupled with streptavidin-based enrichment and on-beads digestion in numerous biological applications. However, the popular on-beads digestion method faces major challenges of streptavidin contamination, the lost information of bioti...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-21 | MSV000087256 | MassIVE
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 
ProteomicsAnalysis of ageing-dependent thiol oxidation reveals early oxidation of proteins involved in core proteostasis functions
Oxidants have a profound impact on biological systems in physiology and under pathological conditions. Oxidative post-translational modifications of protein thiols are well-recognized as a readily occurring alteration of proteins. Changes in protein thiol redox state can modify the function of prote...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-02-07 | PXD042047 | Pride
Yeast Oxicat Proteostasis Thiol oxidation 
ProteomicsMonitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress
Mycothiol (AcCys-GlcN-Ins, MSH) is the major thiol-redox buffer in Actinomycetes, including Mycobacterium and Corynebacterium species. ). Protein S-mycothiolation controls the activities of several redox enzymes that function in detoxification of ROS and methionine sulfoxides, including the thiol pe...
ORGANISM(S): Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) 
2017-06-30 | PXD003303 | Pride
Oxicat S-mycothiolation Bacteria Oxidative stress Mycobacterium smegmatis Mycothiol 
ProteomicsStudy of reversible oxidation of thiol proteins after hexyl aminolevulinate mediated photodynamic therapy
This proteomic study This proteomic study focuses on the role of reversible thiol oxidation after hexyl aminolevulinate mediated PDT (HAL-PDT). The human epidermoid carcinoma cell line A431 was used as model system and red light as light source, a clinical relevant in vitro model. The light dose dep...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-01 | MSV000080866 | MassIVE
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 
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 
ProteomicsCysteine thiol trioxidation induce aging
LC-MS/MS proteomic method is used to coduct skin and lungs proteomics profiling. Many protein with cysteine thiol trioxidation were identified in tissues of old mice. the modified proteins are predicted to induce celllular aging.
ORGANISM(S): Mus musculus (Mouse) 
2024-05-22 | PXD037908 | Pride
Lc-ms/ms Lungs Skin 
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