<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wei B</submitter><funding>Chinese Government Scholarship</funding><funding>Fonds Wetenschappelijk Onderzoek</funding><funding>Universiteit Gent</funding><pagination>777</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7343964</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11</volume><pubmed_abstract>In proteins, hydrogen peroxide (H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as &lt;i>S&lt;/i>-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking, conformation, and function. Previously, we had identified &lt;i>S&lt;/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 &lt;i>S&lt;/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 &lt;i>in situ&lt;/i> sulfenylated cystei</pubmed_abstract><journal>Frontiers in plant science</journal><pubmed_title>Identification of Sulfenylated Cysteines in &lt;i>Arabidopsis thaliana&lt;/i> Proteins Using a Disulfide-Linked Peptide Reporter.</pubmed_title><pmcid>PMC7343964</pmcid><funding_grant_id>01J11311</funding_grant_id><funding_grant_id>201606690036</funding_grant_id><funding_grant_id>1227020N</funding_grant_id><funding_grant_id>G003809N</funding_grant_id><funding_grant_id>G06916N</funding_grant_id><funding_grant_id>G055416N</funding_grant_id><pubmed_authors>Yang J</pubmed_authors><pubmed_authors>Van Breusegem F</pubmed_authors><pubmed_authors>Wei B</pubmed_authors><pubmed_authors>Messens J</pubmed_authors><pubmed_authors>Willems P</pubmed_authors><pubmed_authors>Huang J</pubmed_authors><pubmed_authors>Tian C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of Sulfenylated Cysteines in &lt;i>Arabidopsis thaliana&lt;/i> Proteins Using a Disulfide-Linked Peptide Reporter.</name><description>In proteins, hydrogen peroxide (H&lt;sub>2&lt;/sub>O&lt;sub>2&lt;/sub>) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as &lt;i>S&lt;/i>-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking, conformation, and function. Previously, we had identified &lt;i>S&lt;/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 &lt;i>S&lt;/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 &lt;i>in situ&lt;/i> sulfenylated cystei</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020</publication><modification>2026-04-08T00:32:37.117Z</modification><creation>2020-10-01T07:05:33Z</creation></dates><accession>S-EPMC7343964</accession><cross_references><pubmed>32714340</pubmed><doi>10.3389/fpls.2020.00777</doi></cross_references></HashMap>