{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ek Vitorin JF"],"funding":["NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["127-40"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4805864"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(1)"],"pubmed_abstract":["Separate connexin domains partake in proposed gating mechanisms of gap junction channels. The amino-terminus (NT) domains, which contribute to voltage sensing, may line the channel's cytoplasmic-facing funnel surface, stabilize the channel's overall structure through interactions with the transmembrane domains and each other, and integrate to form a compound particle to gate the channel closed. Interactions of the carboxyl-terminus (CT) and cytoplasmic loop (CL) domains underlie voltage- and low pH-triggered channel closure. To elucidate potential cooperation of these gating mechanisms, we replaced the Cx43NT with the Cx37NT (chimera Cx43(∗)NT37), leaving the remainder of the Cx43 sequence, including the CT and CL, unchanged. Compared to wild-type Cx43 (Cx43WT), Cx43(∗)NT37 junctions exhib"],"journal":["Biophysical journal"],"pubmed_title":["Determinants of Cx43 Channel Gating and Permeation: The Amino Terminus."],"pmcid":["PMC4805864"],"funding_grant_id":["GM086199","R01 HL058732","R01 HL131712"],"pubmed_authors":["Pontifex TK","Burt JM","Ek Vitorin JF"],"additional_accession":[]},"is_claimable":false,"name":"Determinants of Cx43 Channel Gating and Permeation: The Amino Terminus.","description":"Separate connexin domains partake in proposed gating mechanisms of gap junction channels. The amino-terminus (NT) domains, which contribute to voltage sensing, may line the channel's cytoplasmic-facing funnel surface, stabilize the channel's overall structure through interactions with the transmembrane domains and each other, and integrate to form a compound particle to gate the channel closed. Interactions of the carboxyl-terminus (CT) and cytoplasmic loop (CL) domains underlie voltage- and low pH-triggered channel closure. To elucidate potential cooperation of these gating mechanisms, we replaced the Cx43NT with the Cx37NT (chimera Cx43(∗)NT37), leaving the remainder of the Cx43 sequence, including the CT and CL, unchanged. Compared to wild-type Cx43 (Cx43WT), Cx43(∗)NT37 junctions exhib","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jan","modification":"2026-05-05T09:26:38.052Z","creation":"2019-03-27T03:10:11Z"},"accession":"S-EPMC4805864","cross_references":{"pubmed":["26745416"],"doi":["10.1016/j.bpj.2015.10.054"]}}