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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
ProteomicsReversible oxidative signaling in Chlamydomonas following nitrogen deprivation
As global temperatures climb to historic highs, the far-reaching effects of climate change have impacted agricultural nutrient availability. This has extended to low latitude oceans, where a deficit in both nitrogen and phosphorus stores has led to dramatic decreases in carbon sequestration in ocean...
ORGANISM(S): Chlamydomonas reinhardtii 
2020-06-28 | PXD019491 | Pride
Oxidation Ptm Lcms Signaling Chlamydomonas 
ProteomicsOverexpression of catalase delays age-related cardiac disease by preventing oxidative cysteine modifications
Reactive protein cysteine thiolates are instrumental in redox regulation. Aging associated to oxidative stress, can impair redox signaling by damaging essential cysteine thiolates. Our initial study found that cardiac-specific overexpression of catalase, can protect from oxidative stress and delay c...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-24 | PXD002479 | Pride
Metabolism Proteomics Reversible cysteine thiol oxidation Tmt Post-translational protein modifications Mass spectrometry Cardiac aging and disease 
ProteomicsCysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A
p16INK4A inhibits the CDK4/6 kinases and is therefore an important cell cycle regulator. Accumulation of p16INK4A in response to oncogenic transformation leads to cellular senescence and it is therefore frequently lost in cancer. p16INK4A is also known to accumulate under conditions of cellular oxid...
ORGANISM(S): Homo sapiens (Human) 
2019-09-04 | PXD012353 | Pride
Cysteine oxidation amyloid fibril p16ink4a 
ProteomicsDevelopment of a maleimide-based chemical proteomic method for quantitative analysis of cysteine reactivity
Cysteine is the most intrinsically nucleophilic residue in proteins and serves as a sentinel against increasing reactive oxygen species (ROS) via reversible thiol oxidation. Despite the importance of Cys oxidation in understanding biological stress response, it remains largely unknown and a major an...
ORGANISM(S): Chlamydomonas reinhardtii 
2020-10-20 | PXD015409 | Pride
Thiol-reactivity profiling Chlamydomonas reinhardtii Chemical proteomics Cysteine oxidation 
UnknownPhotosynthetic Metabolism and Nitrogen Reshuffling Are Regulated by Reversible Cysteine Thiol Oxidation Following Nitrogen Deprivation in Chlamydomonas.
Not available
S-EPMC7355495 | biostudies-literature
ProteomicsChemical inhibition of the target of rapamycin kinase in Chlamydomonas reinhardtii leads to rapid cysteine oxidation and sustained physiological changes.
The target of rapamycin (TOR) kinase is a key metabolic regulator with a role in diverse processes, including nutritional sensing, protein translation, and autophagy. In the green alga Chlamydomonas reinhardtii, TOR maintains these responsibilities and is additionally linked to the regulation of inc...
ORGANISM(S): Chlamydomonas reinhardtii 
2019-10-04 | PXD014819 | Pride
Azd8055 Global proteomics Chlamydomonas reinhardtii Target of rapamycin Reversible cysteine oxidation 
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 
UnknownReversible Thiol Oxidation Inhibits the Mitochondrial ATP Synthase in Xenopus Laevis Oocytes.
Not available
S-EPMC7139892 | biostudies-literature
ProteomicsRegulation of hyperoxia-induced neonatal lung injury via posttranslational cysteine redox modifications
Lung tissue from normoxia- or hyperoxia-treated control or SCNN1B overexpression mice were processed with a redox proteomics workflow and analyzed by LC-MS/MS with TMT based quantification. Data was searched with MS-GF+ using PNNL's DMS Processing pipeline.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2022-08-18 | MSV000090157 | MassIVE
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