Sort   by:  
 Page size 
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 
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
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
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 (Human) 
2016-01-12 | PXD001582 | Pride
Redox signalling Reactive oxygen species Photodynamic therapy Apoptosis Proteomic Reversible protein 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 
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
ProteomicsMonitoring of protein thiol-oxidation in S.aureus USA300 under hypochlorite stress using OxICAT approach.
During infections, S. aureus has to cope with the oxidative burst of activated macrophages and neutrophils, including reactive oxygen and nitrogen species (RNS, ROS) and the strong oxidant hypochloric acid. We aimed to understand the global thiol-redox state in the major pathogen S. aureus and disco...
ORGANISM(S): Staphylococcus aureus 
2016-12-22 | PXD004918 | Pride
Oxicat Naocl Gapdh H2o2 Oxidative stress Staphylococcus aureus 
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 
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 
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 
Sort   by:  
 Page size