{"database":"GPMDB","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":59,"searchCount":5},"additional":{"omics_type":["Other"],"submitter":["Jacques S, et al."],"instrument_platform":["Instrument"],"disease":["Not Available"],"brenda_tissue":["Not available"],"species":["Ath1"],"submitter_mail":["kris.gevaert@vib-ugent.be"],"publication":["25693801"],"submitter_affiliation":["UGent/VIB, Belgium, et al."],"model":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014280"],"cell_type":["Not available"],"repository":["GPMDB"],"pubmed_abstract":["Reactive oxygen species such as hydrogen peroxide can modify proteins via direct oxidation of their sulfur-containing amino acids, cysteine and methionine. Methionine oxidation, studied here, is a reversible posttranslational modification that is emerging as a mechanism by which proteins perceive oxidative stress and function in redox signaling. Identification of proteins with oxidized methionines is the first prerequisite toward understanding the functional effect of methionine oxidation on proteins and the biological processes in which they are involved. Here, we describe a proteome-wide study of in vivo protein-bound methionine oxidation in plants upon oxidative stress using Arabidopsis thaliana catalase 2 knock-out plants as a model system. We identified over 500 sites of oxidation in about 400 proteins and quantified the differences in oxidation between wild-type and catalase 2 knock-out plants. We show that the activity of two plant-specific glutathione S-transferases, GSTF9 and GSTT23, is significantly reduced upon oxidation. And, by sampling over time, we mapped the dynamics of methionine oxidation and gained new insights into this complex and dynamic landscape of a part of the plant proteome that is sculpted by oxidative stress."],"pubmed_title":["Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress."],"pubmed_authors":["Jacques Silke S,Ghesquière Bart B,De Bock Pieter-Jan PJ,Demol Hans H,Wahni Khadija K,Willems Patrick P,Messens Joris J,Van Breusegem Frank F,Gevaert Kris K,","Jacques Silke S, Ghesquière Bart B, De Bock Pieter-Jan PJ, Demol Hans H, Wahni Khadija K, Willems Patrick P, Messens Joris J, Van Breusegem Frank F, Gevaert Kris K"],"name_synonyms":["(2S)-isomer, thale cress, Stresses, mouse-ear cress, polypeptide, thale-cress, Oxidative Stresses, (R-(R*, Oxidative, Arbisopsis thaliana, S*))-isomer, methionine sulfoxide, Stress, Oxidative., Arabidopsis thaliana (thale cress), 35S-labeled, (+-)-isomer, proteins, (S-(R*, 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Methionin, methionine, Hmet, Sulfur-16, (2R)-2-amino-3-sulfanylpropanoic acid, Oxygen Radicals, Superoxol, Chlorobionta, Hydrogen peroxide (H2O2), PTM, dioxidane, 14)(H, shelves, Oxidative., Plant, Identifications (Psychology), 6-/m0/s1/f/h12-13, L-Cysteine, projection, [H]OO[H], ridge, GSH, L-Cystein, Manganese Catalase, organ system, wide, higher plants, DMDA, spine, post-translational modification, Acids, Liquimeth, Proteomes, time, bis(hydridooxygen)(O--O), HOOH, 18H, C5H11NO2S, biological signaling, Cysteine Hydrochloride, 2-amino-4-(methylsulfanyl)butanoic acid, Effects, lamellae, Aminocarbonsaeure, L-Zystein, L Isomer, Gene, gamma-L-Glutamyl-L-Cysteinylglycine, broad, Hydrogen Peroxide (H2O2), InChIKey=RWSXRVCMGQZWBV-VSCBVDDUDG, process of organ, body system, TYPE, 11H2, Stresses, protrusion, (H, DAGA4, lamella, N-(N-L-gamma-glutamyl-L-cysteinyl)-, period, Transferase, reduced, subnumerary, Gene Products, L-Methionine, system, Half-Cystine, tiny, MAM, SCG3, Reactive, Pedameth, 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C10H17N3O6S"],"view_count":["59"],"citation_count":["0"],"search_count":["5"],"full_dataset_link":["http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32320014280"],"search_domains":["dbgap_ncbi~0","patentfamilies~0","rfam~0","merops~0","complex-portal~0","uniprot~0","wormbaseparasite~0","embl-covid19~0","reactome~0","emdb~0","wgs_masters~0","ebiweb_resources~0","opentargets_genetics~0","biomodels_all~0","ipd-mhc~0","ebiweb_teams~0","taxonomy~0","genome_assembly~0","sc-experiments~0","ebiweb_people~0","enzymeportal_enzymes~0","ipd-nhkir~0","cellosaurus~0","pdbe~0","chebi~0","patentproteins~0","interpro7~0","uniref~0","chembl~0","pdbekb~0","gpcrdb~0","hgnc~0","sc-genes~0","intact~0","rhea~0","ebiweb_training~0","alphafold~0","imgt-hla~0","patentnucleotides~0","ensemblroot~0","eva_studies~0","non-coding~0","europepmc~0","pubmed~1","identifiers_registry~0","pdbechem~0","hpa-covid19~0","eva-variants-covid19~0","biosamples~0","gwas_catalog~0","biotools~0","tls_masters~0","mesh~0","coding~0","sra~0","opentargets~0","efo~0","embl-pathogen~0","project~0","pride~1","human_diseases~0","geo_datasets~0","embl~0","treefam~0","uniparc~0","ols~0","dgva~0","intenz~0","go~0","tsa_masters~0","biosamples-covid19~0","ebiweb_corporate~0","omim~0","lrg~0","earlycause-molecular-sequences~0","ipd-kir~0","empiar~0","rnacentral~0","orcid_data_claims~0","gpmdb~2","lineage-covid19~0","metagenomics~0","pfam~0","pride 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Experiment: TP3_MetCofr, file: folder summary. Published as part of Mol Cell Proteomics. 2015 Feb 18  . From the Abstract: {{i}} ... Methionine oxidation, studied here, is a reversible posttranslational modification, which is emerging as a mechanism by which proteins perceive oxidative stress and function in redox signaling. Identification of proteins with oxidized methionines is a first prerequisite towards understanding the functional effect of methionine oxidation on proteins and the biological processes in which they are involved. Here, we describe a proteome-wide study of in vivo protein-bound methionine oxidation in plants upon oxidative stress, using Arabidopsis thaliana catalase 2 knock-out plants as a model system ... {{/i}}","dates":{"submission":"2015-03-24"},"accession":"GPM32320014280","cross_references":{"pubmed":["25693801"],"Pride":["PXD001286"],"pride":[],"Pride Archive":["PXD001286"]}}