<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Lei Fang</submitter><species>Homo Sapiens</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0018766000</full_dataset_link><submitter_email>njfanglei@nju.edu.cn</submitter_email><submitter_affiliation>Nanjing University</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>iTraq proteomics of SARM1-OE/HEK293 cells</name><description>SARM1 (sterile alpha and Toll/interleukin-1 receptor motif-containing protein 1) is an inducible NAD-consuming enzyme that drives axon degeneration and a form of non-apoptotic cell death termed sarmoptosis. Using SARM1-overexpressing HEK293 cells, we previously showed that the cell-permeant NMN mimetic CZ-48 activates SARM1, depletes cellular NAD and ATP, and induces regulated, propidium iodide (PI)-positive, non-apoptotic cell death that is potently suppressed by the HSP70-family ATP-competitive inhibitor VER-155008 (VER). To investigate the proteome-wide changes underlying CZ-48-induced SARM1 activation and VER-mediated rescue, we performed iTRAQ-based quantitative proteomics on SARM1-overexpressing HEK293 cells treated with vehicle control, 20 μM VER alone, 100 μM CZ-48 alone, or CZ-48 plus VER for 16 h, with biological replicates per group. This dataset was used to identify CZ-48-responsive proteins whose abundance changes were reversed by VER co-treatment, focusing on HSP70/chaperone-related proteostasis proteins, mitochondrial and metabolic proteins, and cell-death-related proteins, in order to elucidate mechanisms of SARM1-driven ATP collapse and mitochondrial dysfunction during sarmoptosis.</description><dates><publication>Sat Aug 01 00:00:00 GMT+01:00 2026</publication></dates><accession>PXD082054</accession><cross_references><TAXONOMY>9606</TAXONOMY></cross_references></HashMap>