<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Shenhai Gong</submitter><species>Mus Musculus</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0010355000</full_dataset_link><submitter_email>gsh930526@163.com</submitter_email><submitter_affiliation>Southern Medical University</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol><name_synonyms>liquid chromatography tandem mass spectroscopy, LC-MS2, PAFABP, EFABP, LC/MS/MS, LCMSMS, E-FABP, mal1, liquid chromatography-tandem mass spectroscopy, Klbp, LC-MSMS, LC-MS/MS, liquid chromatography tandem mass spectrometry, LC-MS-MS., Fabpe, FABP5, KFABP, PA-FABP, Mal1</name_synonyms><description_synonyms>PAFABP, Plays, E-FABP, Playthings, Toys, Fabpe, KFABP, PA-FABP, Mal1, Concept, extracellular, EFABP, Puppets, Role Concept, Redox, Playthings and Play, Roles, mal1, Klbp, Role Concepts, Role, Plaything, Play, Concepts, FABP5, Oxidation Reduction., Oxidation Reduction, Puppet, Toy</description_synonyms></additional><is_claimable>false</is_claimable><name>Detection of oxidatively modified FABP5 by LC-MS/MS</name><description>A variety of studies have indicated that the redox state plays a crucial role in regulating DAMPs functions. This led us to explore whether the differing effects of extracellular and cytoplasmic FABP5 are influenced by their redox state.</description><dates><publication>Wed Nov 27 00:00:00 GMT 2024</publication></dates><accession>PXD058361</accession><cross_references><TAXONOMY>10090</TAXONOMY></cross_references></HashMap>