{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Garg V"],"funding":["NHLBI NIH HHS"],"pagination":["307-24"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3434097"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["140(3)"],"pubmed_abstract":["Ether-à-go-go (EAG) and EAG-related gene (ERG) K(+) channels are close homologues but differ markedly in their gating properties. ERG1 channels are characterized by rapid and extensive C-type inactivation, whereas mammalian EAG1 channels were previously considered noninactivating. Here, we show that human EAG1 channels exhibit an intrinsic voltage-dependent slow inactivation that is markedly enhanced in rate and extent by 1-10 µM 3-nitro-N-(4-phenoxyphenyl) benzamide, or ICA105574 (ICA). This compound was previously reported to have the opposite effect on ERG1 channels, causing an increase in current magnitude by inhibition of C-type inactivation. The voltage dependence of 2 µM ICA-induced inhibition of EAG1 current was half-maximal at -73 mV, 62 mV negative to the half-point for channel a"],"journal":["The Journal of general physiology"],"pubmed_title":["Tuning of EAG K(+) channel inactivation: molecular determinants of amplification by mutations and a small molecule."],"pmcid":["PMC3434097"],"funding_grant_id":["HL55236","R01 HL055236"],"pubmed_authors":["Garg V","Sachse FB","Sanguinetti MC"],"additional_accession":[]},"is_claimable":false,"name":"Tuning of EAG K(+) channel inactivation: molecular determinants of amplification by mutations and a small molecule.","description":"Ether-à-go-go (EAG) and EAG-related gene (ERG) K(+) channels are close homologues but differ markedly in their gating properties. ERG1 channels are characterized by rapid and extensive C-type inactivation, whereas mammalian EAG1 channels were previously considered noninactivating. Here, we show that human EAG1 channels exhibit an intrinsic voltage-dependent slow inactivation that is markedly enhanced in rate and extent by 1-10 µM 3-nitro-N-(4-phenoxyphenyl) benzamide, or ICA105574 (ICA). This compound was previously reported to have the opposite effect on ERG1 channels, causing an increase in current magnitude by inhibition of C-type inactivation. The voltage dependence of 2 µM ICA-induced inhibition of EAG1 current was half-maximal at -73 mV, 62 mV negative to the half-point for channel a","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2026-05-03T05:19:24.245Z","creation":"2019-03-27T00:57:29Z"},"accession":"S-EPMC3434097","cross_references":{"pubmed":["22930803"],"doi":["10.1085/jgp.201210826"]}}