<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Xiaojun Xu</submitter><species>Mus Musculus</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0019907000</full_dataset_link><submitter_email>xuxj26@mail2.sysu.edu.cn</submitter_email><submitter_affiliation>The Eighth Affiliated Hospital, Sun Yat-Sen University</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>HDAC1 K412 lactylation acts as an intrinsic metabolic barrier against p53-dependent osteoblast apoptosis in glucocorticoid-induced osteoporosis</name><description>4D Label-free Lactylomics: Primary osteoblasts derived from Dex- or Dex/NaLa-treated mice were lysed in lysis buffer containing 8 M urea and protease/phosphatase inhibitors. After reduction and alkylation, proteins were digested with trypsin overnight. Peptides were incubated with pan-anti-lactyllysine antibody beads (PTM Biolabs, Cat# PTM-1401R) for enrichment. Enriched peptides were eluted, desalted, and analyzed using a Q Exactive HF-X mass spectrometer (Thermo Fisher Scientific) coupled to an Easy-nLC 1200 system. Raw data were searched against the Mus musculus UniProt database using MaxQuant software. A localization probability > 0.75 was used as the cutoff for modification site identification.</description><dates><publication>Fri Sep 25 00:00:00 BST 2026</publication></dates><accession>PXD084853</accession><cross_references><TAXONOMY>10090</TAXONOMY></cross_references></HashMap>