{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Okyem S"],"funding":["NIDA NIH HHS","NIA NIH HHS","U.S. Department of Health & Human Services | NIH | National Institute on Drug Abuse (NIDA)","U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS)","NINDS NIH HHS","U.S. Department of Health & Human Services | NIH | National Institute on Aging (U.S. National Institute on Aging)"],"pagination":["72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11890773"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["The isoaspartate residue is a spontaneous, time-dependent post-translational modification (PTM) of proteins and peptides, associated with in vivo protein aggregation and changes in molecule lifetime. While this is considered a slow modification impacting long lived proteins, surprisingly, we observed this PTM at high levels within the relatively short-lived neuropeptide galanin (Gal). The combination of liquid chromatography-trapped ion mobility mass spectrometry and protein Isoaspartyl methyltransferase assays demonstrated that 20 ± 2% of the mature Gal contain L-Isoaspartate residue in the hypothalamus of Rattus norvegicus. Aspartate in Gal isomerizes spontaneously under mildly acidic conditions within 48 h in vitro, much faster than previously assumed. Gal with the L-isoaspartate PTM si"],"journal":["Communications chemistry"],"pubmed_title":["Isoaspartate-containing galanin in rat hypothalamus."],"pmcid":["PMC11890773"],"funding_grant_id":["R01 AG078797","R01 NS031609","R01NS031609","P30 DA018310","P30DA018310","1R01AG078797"],"pubmed_authors":["Mast DH","Okyem S","Romanova EV","Sweedler JV","Rubakhin SS"],"additional_accession":[]},"is_claimable":false,"name":"Isoaspartate-containing galanin in rat hypothalamus.","description":"The isoaspartate residue is a spontaneous, time-dependent post-translational modification (PTM) of proteins and peptides, associated with in vivo protein aggregation and changes in molecule lifetime. While this is considered a slow modification impacting long lived proteins, surprisingly, we observed this PTM at high levels within the relatively short-lived neuropeptide galanin (Gal). The combination of liquid chromatography-trapped ion mobility mass spectrometry and protein Isoaspartyl methyltransferase assays demonstrated that 20 ± 2% of the mature Gal contain L-Isoaspartate residue in the hypothalamus of Rattus norvegicus. Aspartate in Gal isomerizes spontaneously under mildly acidic conditions within 48 h in vitro, much faster than previously assumed. Gal with the L-isoaspartate PTM si","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2025-04-04T08:22:54.71Z","creation":"2025-04-04T08:22:54.71Z"},"accession":"S-EPMC11890773","cross_references":{"pubmed":["40057589"],"doi":["10.1038/s42004-025-01475-5"]}}