Matches in SemOpenAlex for { <https://semopenalex.org/work/W4324013584> ?p ?o ?g. }
Showing items 1 to 84 of
84
with 100 items per page.
- W4324013584 endingPage "5333" @default.
- W4324013584 startingPage "5328" @default.
- W4324013584 abstract "GABA type A (GABA<sub>A</sub>) receptors are functionally regulated by external protons in a manner dependent on the receptor subunit composition. Although H<sup>+</sup> can regulate the open probability of single GABA ion channels, exactly what residues and receptor subunits are responsible for proton-induced modulation remain unknown. This study resolves this issue by using recombinant α1βi subunit GABA<sub>A</sub> receptors expressed in human embryonic kidney cells. The potentiating effect of low external pH on GABA responses exhibited p<sub>Ka</sub> in accord with the involvement of histidine and/or cysteine residues. The exposure of GABA<sub>A</sub> receptors to the histidine-modifying reagent DEPC ablated regulation by H<sup>+</sup>, implicating the involvement of histidine residues rather than cysteines in proton regulation. Site-specific substitution of all conserved external histidines to alanine on the β subunits revealed that H267 alone, in the TM2 domain, is important for H<sup>+</sup> regulation. These results are interpreted as a direct protonation of H267 on α1βi receptors rather than an involvement in signal transduction. The opposing functional effects induced by Zn<sup>2+</sup> and H<sup>+</sup> at this single histidine residue most likely reflect differences in charge delocalization on the imidazole rings in the mouth of the GABA<sub>A</sub> receptor ion channel. Additional substitutions of H267 in β subunits with other residues possessing charged side chains (glutamate and lysine) reveal that this area of the ion channel can profoundly influence the functional properties of GABA<sub>A</sub> receptors." @default.
- W4324013584 created "2023-03-14" @default.
- W4324013584 creator A5027416589 @default.
- W4324013584 creator A5080391986 @default.
- W4324013584 creator A5091031492 @default.
- W4324013584 date "2002-07-01" @default.
- W4324013584 modified "2023-10-10" @default.
- W4324013584 title "Identification of a β Subunit TM2 Residue Mediating Proton Modulation of GABA Type A Receptors" @default.
- W4324013584 doi "https://doi.org/10.1523/jneurosci.22-13-05328.2002" @default.
- W4324013584 hasPublicationYear "2002" @default.
- W4324013584 type Work @default.
- W4324013584 citedByCount "30" @default.
- W4324013584 countsByYear W43240135842012 @default.
- W4324013584 countsByYear W43240135842014 @default.
- W4324013584 countsByYear W43240135842015 @default.
- W4324013584 countsByYear W43240135842016 @default.
- W4324013584 countsByYear W43240135842017 @default.
- W4324013584 countsByYear W43240135842021 @default.
- W4324013584 countsByYear W43240135842022 @default.
- W4324013584 crossrefType "journal-article" @default.
- W4324013584 hasAuthorship W4324013584A5027416589 @default.
- W4324013584 hasAuthorship W4324013584A5080391986 @default.
- W4324013584 hasAuthorship W4324013584A5091031492 @default.
- W4324013584 hasBestOaLocation W43240135841 @default.
- W4324013584 hasConcept C104292427 @default.
- W4324013584 hasConcept C104317684 @default.
- W4324013584 hasConcept C12554922 @default.
- W4324013584 hasConcept C168258287 @default.
- W4324013584 hasConcept C170493617 @default.
- W4324013584 hasConcept C185592680 @default.
- W4324013584 hasConcept C19876734 @default.
- W4324013584 hasConcept C2778460671 @default.
- W4324013584 hasConcept C2779570518 @default.
- W4324013584 hasConcept C49051014 @default.
- W4324013584 hasConcept C50254741 @default.
- W4324013584 hasConcept C515207424 @default.
- W4324013584 hasConcept C55493867 @default.
- W4324013584 hasConcept C61174792 @default.
- W4324013584 hasConcept C71240020 @default.
- W4324013584 hasConcept C80161118 @default.
- W4324013584 hasConcept C82617044 @default.
- W4324013584 hasConcept C86803240 @default.
- W4324013584 hasConcept C88272193 @default.
- W4324013584 hasConceptScore W4324013584C104292427 @default.
- W4324013584 hasConceptScore W4324013584C104317684 @default.
- W4324013584 hasConceptScore W4324013584C12554922 @default.
- W4324013584 hasConceptScore W4324013584C168258287 @default.
- W4324013584 hasConceptScore W4324013584C170493617 @default.
- W4324013584 hasConceptScore W4324013584C185592680 @default.
- W4324013584 hasConceptScore W4324013584C19876734 @default.
- W4324013584 hasConceptScore W4324013584C2778460671 @default.
- W4324013584 hasConceptScore W4324013584C2779570518 @default.
- W4324013584 hasConceptScore W4324013584C49051014 @default.
- W4324013584 hasConceptScore W4324013584C50254741 @default.
- W4324013584 hasConceptScore W4324013584C515207424 @default.
- W4324013584 hasConceptScore W4324013584C55493867 @default.
- W4324013584 hasConceptScore W4324013584C61174792 @default.
- W4324013584 hasConceptScore W4324013584C71240020 @default.
- W4324013584 hasConceptScore W4324013584C80161118 @default.
- W4324013584 hasConceptScore W4324013584C82617044 @default.
- W4324013584 hasConceptScore W4324013584C86803240 @default.
- W4324013584 hasConceptScore W4324013584C88272193 @default.
- W4324013584 hasIssue "13" @default.
- W4324013584 hasLocation W43240135841 @default.
- W4324013584 hasLocation W43240135842 @default.
- W4324013584 hasLocation W43240135843 @default.
- W4324013584 hasOpenAccess W4324013584 @default.
- W4324013584 hasPrimaryLocation W43240135841 @default.
- W4324013584 hasRelatedWork W1894940769 @default.
- W4324013584 hasRelatedWork W1968856852 @default.
- W4324013584 hasRelatedWork W2008709624 @default.
- W4324013584 hasRelatedWork W2046755082 @default.
- W4324013584 hasRelatedWork W2047273628 @default.
- W4324013584 hasRelatedWork W2067719391 @default.
- W4324013584 hasRelatedWork W2102437900 @default.
- W4324013584 hasRelatedWork W2119616461 @default.
- W4324013584 hasRelatedWork W2803898079 @default.
- W4324013584 hasRelatedWork W4242690077 @default.
- W4324013584 hasVolume "22" @default.
- W4324013584 isParatext "false" @default.
- W4324013584 isRetracted "false" @default.
- W4324013584 workType "article" @default.