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ProteomicsProtein citrullination and homocitrullination profiling in mice using LC-MS/MS
Citrullination and homocitrullination are two post-translational modifications (PTMs) that may cause protein structural and functional changes. Although they have been linked to various biological processes and disease development, the understanding is still poor because of limitations to enrich, de...
ORGANISM(S): Mus musculus (Mouse) 
2022-12-05 | PXD023733 | Pride
Citrullination Mouse Biotin thiol tag Homocitrullination Lc-ms/ms 
UnknownEnabling Global Analysis of Protein Citrullination via Biotin Thiol Tag-Assisted Mass Spectrometry.
Not available
S-EPMC10276619 | biostudies-literature
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 
ProteomicsBenchmarking cleavable biotin tags for site-centric chemoproteomics
the performance of five common cleavable biotin linkers are assessed parallelly by using commercially available thiol-reactive probe IPM (2-iodo-N-(prop-2-yn-1-yl)acetamide) in profiling cysteinome
ORGANISM(S): Homo Sapiens 
2022-01-16 | PXD031019 |
UnknownMass Spectrometry-Based Precise Identification of Citrullinated Histones via Limited Digestion and Biotin Derivative Tag Enrichment.
Not available
S-EPMC11526168 | biostudies-literature
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 
ProteomicsThio-triazole-biotin-labeled peptides derived from iPA probes
iPAs are minimal-tag chemical probes - propargyl analogs of putrescine (PUT), spermidine (SPD), and spermine (SPM) - that preserve charge/spacing, retain transporter compatibility, and enable high-resolution intracellular imaging following paraformaldehyde (PFA)-based crosslinking and copper-catalyz...
ORGANISM(S): Homo sapiens (Human) 
2025-12-16 | PXD070115 | Pride
Artificialy modified peptides Propargyl tag Polyamines 
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 
UnknownThiol-disulphide independent in-cell trapping for the identification of peroxiredoxin 2 interactors.
Not available
S-EPMC8346688 | biostudies-literature
UnknownDual Labeling Biotin Switch Assay to Reduce Bias Derived From Different Cysteine Subpopulations: A Method to Maximize S-Nitrosylation Detection.
Not available
S-EPMC4979977 | biostudies-literature
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