{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Sijia Liang"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0012852000"],"submitter_email":["liangsj5@mail.sysu.edu.cn"],"submitter_affiliation":["Sun Yat-Sen University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"The mass spectrometry data for the identification of eNOS-binding protein","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.","dates":{"publication":"Sun Aug 03 00:00:00 GMT+01:00 2025"},"accession":"PXD066908","cross_references":{"TAXONOMY":["9606"]}}