{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zerbini E"],"funding":["Ministero dell'Università e della Ricerca","Ministero dell'Università e della Ricerca"],"pagination":["e70505"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12917857"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(3)"],"pubmed_abstract":["Emerging evidence suggests that sex-specific differences in L-serine (L-Ser) metabolism play a key role in Alzheimer's disease (AD). While disruptions in amino acid balance are well known, recent findings point to a dimorphic regulation of the serine biosynthetic pathway. To explore this, we examined post-translational modifications (PTMs) of D-3-phosphoglycerate dehydrogenase (PHGDH)-the rate-limiting enzyme for de novo L-Ser synthesis-as a potentialmechanism underlying this difference. PHGDH was immunoprecipitated from hippocampal tissue of healthy and AD-affected males and females and analyzed by mass spectrometry. Five phosphorylation sites (S55, T60, T78, S383, and S473) were shared across all groups, but a unique deacetylation at K289 appeared exclusively in AD males. Functional assa"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Post-translational regulation of human D-3-phosphoglycerate dehydrogenase in Alzheimer's disease."],"pmcid":["PMC12917857"],"funding_grant_id":["PRIN 2017 (2017H4J3AS)"],"pubmed_authors":["Pollegioni L","Sacchi S","Maffioli E","Riva D","Zerbini E","Tedeschi G"],"additional_accession":[]},"is_claimable":false,"name":"Post-translational regulation of human D-3-phosphoglycerate dehydrogenase in Alzheimer's disease.","description":"Emerging evidence suggests that sex-specific differences in L-serine (L-Ser) metabolism play a key role in Alzheimer's disease (AD). While disruptions in amino acid balance are well known, recent findings point to a dimorphic regulation of the serine biosynthetic pathway. To explore this, we examined post-translational modifications (PTMs) of D-3-phosphoglycerate dehydrogenase (PHGDH)-the rate-limiting enzyme for de novo L-Ser synthesis-as a potentialmechanism underlying this difference. PHGDH was immunoprecipitated from hippocampal tissue of healthy and AD-affected males and females and analyzed by mass spectrometry. Five phosphorylation sites (S55, T60, T78, S383, and S473) were shared across all groups, but a unique deacetylation at K289 appeared exclusively in AD males. Functional assa","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Mar","modification":"2026-07-16T09:15:58.907Z","creation":"2026-07-09T10:46:41.412Z"},"accession":"S-EPMC12917857","cross_references":{"pubmed":["41711160"],"doi":["10.1002/pro.70505"]}}