{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wei B"],"funding":["Chinese Government Scholarship","Fonds Wetenschappelijk Onderzoek","Universiteit Gent"],"pagination":["777"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7343964"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["In proteins, hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as <i>S</i>-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking, conformation, and function. Previously, we had identified <i>S</i>-sulfenylated proteins by using a tagged proteinaceous probe based on the yeast AP-1-like (Yap1) transcription factor that specifically reacts with sulfenic acids and traps them through a mixed disulfide bond. However, the identity of the <i>S</i>-sulfenylated amino acid residues within a protein remained enigmatic. By using the same transgenic YAP1C probe, we present here a technological advancement to identify <i>in situ</i> sulfenylated cystei"],"journal":["Frontiers in plant science"],"pubmed_title":["Identification of Sulfenylated Cysteines in <i>Arabidopsis thaliana</i> Proteins Using a Disulfide-Linked Peptide Reporter."],"pmcid":["PMC7343964"],"funding_grant_id":["01J11311","201606690036","1227020N","G003809N","G06916N","G055416N"],"pubmed_authors":["Yang J","Van Breusegem F","Wei B","Messens J","Willems P","Huang J","Tian C"],"additional_accession":[]},"is_claimable":false,"name":"Identification of Sulfenylated Cysteines in <i>Arabidopsis thaliana</i> Proteins Using a Disulfide-Linked Peptide Reporter.","description":"In proteins, hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as <i>S</i>-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking, conformation, and function. Previously, we had identified <i>S</i>-sulfenylated proteins by using a tagged proteinaceous probe based on the yeast AP-1-like (Yap1) transcription factor that specifically reacts with sulfenic acids and traps them through a mixed disulfide bond. However, the identity of the <i>S</i>-sulfenylated amino acid residues within a protein remained enigmatic. By using the same transgenic YAP1C probe, we present here a technological advancement to identify <i>in situ</i> sulfenylated cystei","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2026-04-08T00:32:37.117Z","creation":"2020-10-01T07:05:33Z"},"accession":"S-EPMC7343964","cross_references":{"pubmed":["32714340"],"doi":["10.3389/fpls.2020.00777"]}}