Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Francis, MM | - |
dc.contributor.author | Choi, KI | - |
dc.contributor.author | Horenstein, BA | - |
dc.contributor.author | Papke, RL | - |
dc.date.accessioned | 2024-01-21T17:09:04Z | - |
dc.date.available | 2024-01-21T17:09:04Z | - |
dc.date.created | 2021-09-01 | - |
dc.date.issued | 1998-05 | - |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.uri | https://pubs.kist.re.kr/handle/201004/143115 | - |
dc.description.abstract | Some 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.language | English | - |
dc.publisher | BIOPHYSICAL SOCIETY | - |
dc.subject | AFFINITY BINDING-SITE | - |
dc.subject | NONCOMPETITIVE ANTAGONIST | - |
dc.subject | TORPEDO-CALIFORNICA | - |
dc.subject | NICOTINIC RECEPTOR | - |
dc.subject | H-3 CHLORPROMAZINE | - |
dc.subject | KINETIC-PROPERTIES | - |
dc.subject | XENOPUS OOCYTES | - |
dc.subject | ALPHA-SUBUNIT | - |
dc.subject | ION CHANNEL | - |
dc.subject | CURRENTS | - |
dc.title | Sensitivity to voltage-independent inhibition determined by pore-lining region of the acetylcholine receptor | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/S0006-3495(98)77940-8 | - |
dc.description.journalClass | 1 | - |
dc.identifier.bibliographicCitation | BIOPHYSICAL JOURNAL, v.74, no.5, pp.2306 - 2317 | - |
dc.citation.title | BIOPHYSICAL JOURNAL | - |
dc.citation.volume | 74 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 2306 | - |
dc.citation.endPage | 2317 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.wosid | 000073429700019 | - |
dc.identifier.scopusid | 2-s2.0-0344701102 | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | AFFINITY BINDING-SITE | - |
dc.subject.keywordPlus | NONCOMPETITIVE ANTAGONIST | - |
dc.subject.keywordPlus | TORPEDO-CALIFORNICA | - |
dc.subject.keywordPlus | NICOTINIC RECEPTOR | - |
dc.subject.keywordPlus | H-3 CHLORPROMAZINE | - |
dc.subject.keywordPlus | KINETIC-PROPERTIES | - |
dc.subject.keywordPlus | XENOPUS OOCYTES | - |
dc.subject.keywordPlus | ALPHA-SUBUNIT | - |
dc.subject.keywordPlus | ION CHANNEL | - |
dc.subject.keywordPlus | CURRENTS | - |
dc.subject.keywordAuthor | acetylcholine | - |
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