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ProteomicsChemoselective umpolung of thiols to episulfoniums for cysteine bioconjugation
Modification of native cysteine is an important tool in protein research and relies on fast and chemoselective reactions under bioambient conditions. Nucleophilic cysteine can be functionalized with electrophiles, such as maleimides, that carry specific chemical groups, depending on the desired appl...
ORGANISM(S): Escherichia Coli 
2023-12-20 | PXD038723 | JPOST Repository
ProteomicsQuantification of the percentage of oxidized cysteine thiols in GrxS12 under normal and H2O2 treatments.
To evaluate the percentage of oxidized cysteine thiols, the GrxS12 proteins underwent either with or without H2O2 treatment were alkylated by iodoacetamide (IAM), reduced with DTT, and subsequently the newly generated free Cys were alkylated with N-ethylmaleimide (NEM). The spectrometric analysis of...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD059065 | Pride
Grxs12 H2o2 Oxidized cysteine thiols Quantification 
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 
UnknownPrediction of reversibly oxidized protein cysteine thiols using protein structure properties.
Not available
S-EPMC2248312 | biostudies-literature
ProteomicsCysQuant: simultaneous quantification of cysteine oxidation and protein abundance using data dependent or independent acquisition mass spectrometry
Protein cysteinyl thiols are susceptible to reduction-oxidation reactions that can influence protein function, urging the need for accurate cysteine oxidation quantification to decode protein redox regulation. Here, we present a novel approach called CysQuant that enables simultaneous quantification...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-07-21 | PXD043895 | Pride
Cysteine oxidation Redox Data-independent acquisition Plexdia 
ProteomicsProteome-wide analysis of cysteine reactivity in Arabidopsis associated with biotic stress response
We used a method for the enrichment of proteins with oxidative post-translational modifications that enabled the comprehensive identification and label-free quantification of reversibly oxidized thiols across the plant proteome. The redoxomes were characterized in wild-type and the top1top2 null mut...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-03-19 | PXD010104 | Pride
Arabidopsis thaliana Pseudomonas syringae Thimet oligopeptidase Redox proteomics Biotic stress 
UnknownN-Acryloylindole-alkyne (NAIA) enables imaging and profiling new ligandable cysteines and oxidized thiols by chemoproteomics.
Not available
S-EPMC10272157 | biostudies-literature
ProteomicsQuantitative analysis of redox proteome reveals protein thiol switches regulating fundamental processes in developmental haematopoiesis
Foetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behaviour in normal and malignant haematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic appro...
ORGANISM(S): Mus musculus (Mouse) 
2022-06-09 | PXD030043 | Pride
Hematopoiesis Leukemia Oxidative modifications Redox proteomics 
ProteomicsNAIA for cysteine profiling in HepG2 cells, protein target identification of covalent ligand and studying cysteine oxidative modifications
New cysteine probes, N-acryloylindole-alkynes (NAIAs), have been developed. We have applied NAIA-5 for cysteine profiling in HepG2 cell lysates, and the results have been compared to the conventional cysteine probe iodoacetamide-alkyne (IAA). NAIA-5 allows identification of more ligandable Cys than ...
ORGANISM(S): Homo sapiens (Human) 
2023-06-14 | PXD041264 | Pride
Profiling ligandable cysteines and studying cysteine oxidative modifications in human liver cancer cells hepg2 by naia-5 using bruker timstof ms 
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
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