{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gaston B"],"funding":["Children’s Lung Foundation","NIDA NIH HHS","NHLBI NIH HHS","Eli Lilly Foundation","Harrington Discovery Institute","National Institutes of Health","NIH HHS","Other","Riley Children’s Foundation"],"pagination":["134174"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7526540"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(18)"],"pubmed_abstract":["S-nitroso-l-cysteine (L-CSNO) behaves as a ligand. Its soluble guanylate cyclase-independent (sGC-independent) effects are stereoselective - that is, not recapitulated by S-nitroso-d-cysteine (D-CSNO) - and are inhibited by chemical congeners. However, candidate L-CSNO receptors have not been identified. Here, we have used 2 complementary affinity chromatography assays - followed by unbiased proteomic analysis - to identify voltage-gated K+ channel (Kv) proteins as binding partners for L-CSNO. Stereoselective L-CSNO-Kv interaction was confirmed structurally and functionally using surface plasmon resonance spectroscopy; hydrogen deuterium exchange; and, in Kv1.1/Kv1.2/Kvβ2-overexpressing cells, patch clamp assays. Remarkably, these sGC-independent L-CSNO effects did not involve S-nitrosylat"],"journal":["JCI insight"],"pubmed_title":["Voltage-gated potassium channel proteins and stereoselective S-nitroso-l-cysteine signaling."],"pmcid":["PMC7526540"],"funding_grant_id":["INCITE","U01 DA051373","P01HL101871","Endowment","P01 HL128192","Riley Children’s Foundation","P01HL128192","T32 HL125245","T32HL125245","S10 OD026882","Harrington Discovery Institute","P01 HL101871","SIG RR016789"],"pubmed_authors":["Getsy P","Bates JN","Wintrobe P","Strassmaier T","Marozkina N","Smith L","Lewis T","Seckler J","Kunze D","Lewis SJ","Burton ST","Morozkina TS","Kiselar J","McGee K","Bosch J","Hodges CA","Gaston B"],"additional_accession":[]},"is_claimable":false,"name":"Voltage-gated potassium channel proteins and stereoselective S-nitroso-l-cysteine signaling.","description":"S-nitroso-l-cysteine (L-CSNO) behaves as a ligand. Its soluble guanylate cyclase-independent (sGC-independent) effects are stereoselective - that is, not recapitulated by S-nitroso-d-cysteine (D-CSNO) - and are inhibited by chemical congeners. However, candidate L-CSNO receptors have not been identified. Here, we have used 2 complementary affinity chromatography assays - followed by unbiased proteomic analysis - to identify voltage-gated K+ channel (Kv) proteins as binding partners for L-CSNO. Stereoselective L-CSNO-Kv interaction was confirmed structurally and functionally using surface plasmon resonance spectroscopy; hydrogen deuterium exchange; and, in Kv1.1/Kv1.2/Kvβ2-overexpressing cells, patch clamp assays. Remarkably, these sGC-independent L-CSNO effects did not involve S-nitrosylat","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-04-17T11:08:50.633Z","creation":"2025-06-01T03:53:55.164Z"},"accession":"S-EPMC7526540","cross_references":{"pubmed":["32790645"],"doi":["10.1172/jci.insight.134174"]}}