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| http://purl.uniprot.org/citations/24107424 | http://www.w3.org/2000/01/rdf-schema#comment | "The epithelial sodium channel (ENaC) is comprised of three homologous subunits. Channels composed solely of α- and β-subunits (αβ-channels) exhibit a very high open probability (Po) and reduced sensitivity to amiloride, in contrast to channels composed of α- and γ-subunits or of all three subunits (i.e., αγ- and αβγ-channels). A mutant channel comprised of α- and β-subunits, and a chimeric γ-subunit where the region immediately preceding (β12 and wrist) and encompassing the second transmembrane domain (TM2) was replaced with the corresponding region of the β-subunit (γ-βTM2), displayed characteristics reminiscent of αβ-channels, including a reduced amiloride potency of block and a loss of Na(+) self-inhibition (reflecting an increased Po). Substitutions at key pore-lining residues of the γ-βTM2 chimera enhanced the Na(+) self-inhibition response, whereas key γ-subunit substitutions reduced the response. Furthermore, multiple sites within the TM2 domain of the γ-subunit were required to confer high amiloride potency. In summary, we have identified novel pore-lining residues of the γ-subunit of ENaC that are important for proper channel gating and its interaction with amiloride."xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajprenal.00337.2013"xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/author | "Shi S."xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/author | "Kleyman T.R."xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/name | "Am J Physiol Renal Physiol"xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/pages | "F1585-92"xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/title | "Gamma subunit second transmembrane domain contributes to epithelial sodium channel gating and amiloride block."xsd:string |
| http://purl.uniprot.org/citations/24107424 | http://purl.uniprot.org/core/volume | "305"xsd:string |
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