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ProteomicsQuantification of sulfenic acid modification in an atherosclerosis
Physiological stimuli such as thrombin, or pathological stimuli such as lysophosphatidic acid (LPA), activate platelets. The activated platelets bind to monocytes through P-selectin-PSGL-1 interactions, but also release the contents of their granules, commonly called “platelet releasate”. It is know...
ORGANISM(S): Homo sapiens (Human) 
2016-10-10 | PXD004862 | Pride
Sulfenic acid Biotin switch assay Thp-1 cell Nox 
ProteomicsQuantification of sulfenic acid modifications in an atherosclerotic model
Physiological stimuli such as thrombin or pathological stimuli such as lysophosphatidic acid (LPA) activate platelets. The activated platelets bind to monocyte through P-selectin-PSGL-1 interactions, but also release the contents of their granules, which were defined as platelet releasate. It is kno...
ORGANISM(S): Homo sapiens (Human) 
2016-10-10 | PXD003365 | Pride
Sulfenic acid Biotin switch assay Atherosclerosis 
ProteomicsQuantification of sulfenic acid modifications in an atherosclerotic model-2
Physiological stimuli such as thrombin or pathological stimuli such as lysophosphatidic acid (LPA) activate platelets. The activated platelets bind to monocyte through P-selectin-PSGL-1 interactions, but also release the contents of their granules, which were defined as platelet releasate. It is kno...
ORGANISM(S): Homo sapiens (Human) 
2016-10-10 | PXD003363 | Pride
Sulfenic acid Biotin switch assay Atherosclerosis 
ProteomicsQuantification of sulfenic acid modifications on an atherosclerotic model-1
Redox imbalance in cells, due to the accumulation of reactive oxygen species (ROS), has been implicated in the pathogenesis of several diseases, including atherosclerosis. However, the molecular details of redox regulation in atherosclerosis remain to be established.1 During the progression of ather...
ORGANISM(S): Homo sapiens (Human) 
2016-10-10 | PXD003354 | Pride
Atheroscelrosis Sulfenic acid Biotin switch assay 
ProteomicsProtein S-glutathionylation in HeLa cells identified by nanoLC-LTQ-Orbitrap XL MS/MS
Cysteine modifications have been widely detected among different protein in different species. Here, we examined protein glutathionylation in HeLa cells under both untreated and diamide-treated conditions. A strategy using resin-assisted enrichment of glutathionylated proteins or peptides after biot...
ORGANISM(S): Homo sapiens (Human) 
2020-04-29 | PXD017717 | Pride
Nanolc-ltq-orbitrap xl ms/ms Biotin switch S-glutathionylation 
ProteomicsS-nitrosylation of p53 in A375 cells
Nitric oxide (NO) is a pleiotropic signaling molecule that affects numerous biological functions. One unique posttranslational modification of proteins by NO is termed S-nitrosylation (SNO), but the role in modulating key proteins’ function in melanoma has not been fully characterized. In the presen...
ORGANISM(S): Homo sapiens (Human) 
2025-07-21 | PXD031807 | Pride
A375 Mass spectrometry S-nitrosylation P53 Melanoma cells 
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
ProteomicsTMT-switch assay for the detection of SNO
To maximize SNO-proteome coverage and ensure capture of all modified sites, different experimental configurations using both iodo- and cysTMT were evaluated.
ORGANISM(S): Homo sapiens (Human) 
2016-12-23 | PXD000741 | Pride
S-nitrosylation S-nitrosation Tandem mass tag 
TranscriptomicsPhenobarbital mediates an epigenetic switch at the constitutive androstane receptor (CAR) target gene Cyp2b10 in the liver of B6C3F1 mice.
This SuperSeries is composed of the following subset Series: GSE34423: Phenobarbital mediates an epigenetic switch at the constitutive androstane receptor (CAR) target gene Cyp2b10 in the liver of B6C3F1 mice [Expression array]. GSE34462: Phenobarbital mediates an epigenetic switch at the constituti...
ORGANISM(S): Mus musculus 
2011-12-16 | E-GEOD-34463 | biostudies-arrayexpress
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 
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