| pubmed-article:8650229 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C0034830 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:8650229 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:8650229 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8650229 | pubmed:dateCreated | 1996-7-25 | lld:pubmed |
| pubmed-article:8650229 | pubmed:abstractText | Binding of agonists to nicotinic acetylcholine receptors generates a sequence of changes that activate a cation-selective conductance. By measuring electrophysiological responses in chimeric alpha7/alpha3 receptors expressed in Xenopus oocytes, we have showed the involvement of the M2-M3 loop in coupling agonist binding to the channel gate. An aspartate residue therein, Asp-266 in the alpha7 subunit, was identified by site-directed mutagenesis as crucial, since mutants at this position exhibited very poor functional responses to three different nicotinic agonists. We have extended this investigation to another neuronal nicotinic receptor (alpha3/beta4), and found that a homologous residue in the beta4 subunit, Asp-268, played a similar role in coupling. These findings are consistent with a hypothesis that the aspartate residue in the M2-M3 loop, which is conserved in all homomer-forming alpha-type subunits and all neuronal beta-type subunits that combine to form functional receptors, is a major determinant of information transmission from binding site to channel gate in all neuronal nicotinic receptors. | lld:pubmed |
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| pubmed-article:8650229 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8650229 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8650229 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8650229 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8650229 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:SalaFF | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:CriadoMM | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:SaloAA | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:BallestaJ JJJ | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:Campos-CaroAA | lld:pubmed |
| pubmed-article:8650229 | pubmed:author | pubmed-author:Vicente-Agull... | lld:pubmed |
| pubmed-article:8650229 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8650229 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:8650229 | pubmed:volume | 93 | lld:pubmed |
| pubmed-article:8650229 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8650229 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8650229 | pubmed:pagination | 6118-23 | lld:pubmed |
| pubmed-article:8650229 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8650229 | pubmed:meshHeading | pubmed-meshheading:8650229-... | lld:pubmed |
| pubmed-article:8650229 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8650229 | pubmed:articleTitle | A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors. | lld:pubmed |
| pubmed-article:8650229 | pubmed:affiliation | Departamento de Neuroquímica, Universidad de Alicante, Spain. | lld:pubmed |
| pubmed-article:8650229 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8650229 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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