<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Sijia Liang</submitter><species>Homo Sapiens</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0012852000</full_dataset_link><submitter_email>liangsj5@mail.sysu.edu.cn</submitter_email><submitter_affiliation>Sun Yat-Sen University</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>The mass spectrometry data for the identification of eNOS-binding protein</name><description>The activity of endothelial nitric oxide synthase (eNOS) is regulated through intricate crosstalk among transcriptional, post-transcriptional, and post-translational modalities. Translational modification cascades and their downstream signaling relay emerge as pivotal controllers of both eNOS functionality and nitric oxide bioavailability, positioning these pathways as prime therapeutic targets. A deeper elucidation of the molecular machinery governing post-translational regulation of eNOS holds promise for developing innovative approaches to forestall endothelial dysfunction and its consequent hypertensive complications.</description><dates><publication>Sun Aug 03 00:00:00 GMT+01:00 2025</publication></dates><accession>PXD066908</accession><cross_references><TAXONOMY>9606</TAXONOMY></cross_references></HashMap>