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ProteomicsIntegrated Dissection of Cysteine Oxidative Modification Proteome During Cardiac Hypertrophy
Cysteine oxidative modification of cellular proteins is crucial for many aspects of cardiac hypertrophy development. However, integrated dissection of multiple types of cysteine oxidation proteome in cardiac hypertrophy is currently missing. Here we developed a novel discovery platform encompassing ...
ORGANISM(S): Mus musculus (Mouse) 
2018-08-29 | PXD010336 | Pride
Mouse Cardiac hypertrophy Heart Biotin switch Dimethyl labeling Cysteine oxidation Reversible cysteine oxidation Cysteine sulfinylation Cysteine sulfonylation Quantitative proteomics 
ProteomicsPersulfidation and direct detection of sulfonylation in aging Brain of WT, CSE-/- and MPST-/- mice
Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-re...
ORGANISM(S): Mus musculus (Mouse) 
2026-05-23 | PXD045806 | Pride
ProteomicsNAGK sulfonylation data associated with "A lysis-derived PMSF and orthovanadate oxidant defines a distinct cysteine-engagement profile"
The N-acetylglucosamine kinase, NAGK, was found to undergo a mobility shift on SDS-PAGE that was reliant on the presence of PMSF and orthovanadate in the lysis buffer. The mobility shift was prevented by the addition of reducing agent to the lysis buffer, so in the assay described and deposited here...
ORGANISM(S): Homo sapiens (Human) 
2026-08-08 | PXD081578 | Pride
Nagk Pmsf Sulfonylation Orthovanadate 
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 
UnknownIntegrated Dissection of Cysteine Oxidative Post-translational Modification Proteome During Cardiac Hypertrophy.
Not available
S-EPMC6650147 | biostudies-literature
UnknownCysteine hyperoxidation rewires communication pathways in the nucleosome and destabilizes the dyad.
Not available
S-EPMC11001638 | biostudies-literature
ProteomicsMass spectrometry-based direct detection of multiple types of protein thiol modifications in pancreatic beta cells under endoplasmic reticulum stress
A 2D-LC-MS/MS strategy coupled with TMT-10 labeling was applied to mouse pancreatic beta cells (hetaTC-6) induced with ER stress by Thapsigargin to study the global proteome and protein cysteine PTM changes under ER stress. Samples were digested with trypsin, labeled with 10-plex TMT, then analyzed ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2021-05-29 | MSV000087543 | MassIVE
ProteomicsThermal proteome profilling in WT and CSE-/- MEF cells upon H2O2 treatment
Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-re...
ORGANISM(S): Mus musculus (Mouse) 
2026-05-23 | PXD045820 | Pride
ProteomicsSulfenylation and total proteome changes analysis aging Brain of WT, CSE-/- and MPST-/- mice
Cellular homeostasis relies on precise regulation through chemical processes, such as protein posttranslational modifications and physical processes, such as biomolecular condensation. Aging disrupts this balance, increasing susceptibility to diseases and death. However, the mechanisms behind age-re...
ORGANISM(S): Mus musculus (Mouse) 
2026-05-23 | PXD045785 | Pride
UnknownOxidative posttranslational modifications mediate decreased SERCA activity and myocyte dysfunction in Galphaq-overexpressing mice.
Not available
S-EPMC2909347 | biostudies-literature
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