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ProteomicsIn situ identification of S-sulfenylation sites in Arabidopsis thaliana using the genetic YAP1 probe
Hydrogen peroxide (H2O2) reacts, directly or indirectly, with cysteines to form cysteine sulfenic acid, also known as S-sulfenylation. This cysteine oxidation steers diverse cellular processes by altering protein interactions, trafficking, conformation, and function. We present a method to identify ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-12-15 | PXD016723 | Pride
S-sulfenylation Arabidopsis thaliana Post-translational modification Disulfide Cross-link Redox Cysteine oxidation Yap1c 
UnknownIdentification of Sulfenylated Cysteines in Arabidopsis thaliana Proteins Using a Disulfide-Linked Peptide Reporter.
Not available
S-EPMC7343964 | biostudies-literature
ProteomicsPeroxisome-derived hydrogen peroxide can modulate the sulfenylation profiles of key redox signaling proteins in Flp-In T-REx 293 cells
Ever since the first characterization of peroxisomes, a central theme has been their involvement in cellular hydrogen peroxide (H2O2) metabolism. While the reputation of H2O2 drastically changed from an exclusively toxic molecule to a signaling messenger, the regulatory role of peroxisomes in these ...
ORGANISM(S): Homo sapiens (Human) 
2022-05-10 | PXD030782 | Pride
Peroxisome  hydrogen peroxide  cysteine thiol group  yap1c-based sulfenome mining  peroxiredoxin  mitochondrion 
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