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dc.contributor.authorFrancis, MM-
dc.contributor.authorChoi, KI-
dc.contributor.authorHorenstein, BA-
dc.contributor.authorPapke, RL-
dc.date.accessioned2024-01-21T17:09:04Z-
dc.date.available2024-01-21T17:09:04Z-
dc.date.created2021-09-01-
dc.date.issued1998-05-
dc.identifier.issn0006-3495-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/143115-
dc.description.abstractSome noncompetitive inhibitors (e.g., ganglionic blockers) exhibit selectivity for the inhibition of neuronal nicotinic acetylcholine receptors (nAChRs). This study characterizes the mechanism of selective long-term inhibition of neuronal and muscle-neuronal chimeric nAChRs by bis(2,2,6,6-tetramethyl-4-piperidinyl) sebacate (bis-TMP-10 or BTMPS), a bifunctional form of the potent ganglionic blocker tetramethylpiperidine. Long-term inhibition of neuronal nAChRs by bis-TMP-10 has been previously demonstrated to arise, at least in part, from the binding of the bis compound to neuronal beta-subunits. In this study, long-term inhibition is demonstrated to be dependent upon the presence of sequence element(s) within the pore-lining second transmembrane domain (tm2) of neuronal beta-subunits; however, the inhibitor binding site itself does not appear to be contained within the segment of the channel pore influenced by the membrane electric field. Specifically, our results imply that bis-TMP-10 interacts with an activation-sensitive element, the availability of which may be regulated by a sequence in the tm2 domain. Furthermore, we demonstrate a compound length requirement for long-term inhibition that would be consistent with binding to multiple sites located on the extracellular portion of the receptor.-
dc.languageEnglish-
dc.publisherBIOPHYSICAL SOCIETY-
dc.subjectAFFINITY BINDING-SITE-
dc.subjectNONCOMPETITIVE ANTAGONIST-
dc.subjectTORPEDO-CALIFORNICA-
dc.subjectNICOTINIC RECEPTOR-
dc.subjectH-3 CHLORPROMAZINE-
dc.subjectKINETIC-PROPERTIES-
dc.subjectXENOPUS OOCYTES-
dc.subjectALPHA-SUBUNIT-
dc.subjectION CHANNEL-
dc.subjectCURRENTS-
dc.titleSensitivity to voltage-independent inhibition determined by pore-lining region of the acetylcholine receptor-
dc.typeArticle-
dc.identifier.doi10.1016/S0006-3495(98)77940-8-
dc.description.journalClass1-
dc.identifier.bibliographicCitationBIOPHYSICAL JOURNAL, v.74, no.5, pp.2306 - 2317-
dc.citation.titleBIOPHYSICAL JOURNAL-
dc.citation.volume74-
dc.citation.number5-
dc.citation.startPage2306-
dc.citation.endPage2317-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000073429700019-
dc.identifier.scopusid2-s2.0-0344701102-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalResearchAreaBiophysics-
dc.type.docTypeArticle-
dc.subject.keywordPlusAFFINITY BINDING-SITE-
dc.subject.keywordPlusNONCOMPETITIVE ANTAGONIST-
dc.subject.keywordPlusTORPEDO-CALIFORNICA-
dc.subject.keywordPlusNICOTINIC RECEPTOR-
dc.subject.keywordPlusH-3 CHLORPROMAZINE-
dc.subject.keywordPlusKINETIC-PROPERTIES-
dc.subject.keywordPlusXENOPUS OOCYTES-
dc.subject.keywordPlusALPHA-SUBUNIT-
dc.subject.keywordPlusION CHANNEL-
dc.subject.keywordPlusCURRENTS-
dc.subject.keywordAuthoracetylcholine-
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