| pubmed-article:9144255 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9144255 | lifeskim:mentions | umls-concept:C0164198 | lld:lifeskim |
| pubmed-article:9144255 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:9144255 | lifeskim:mentions | umls-concept:C0597360 | lld:lifeskim |
| pubmed-article:9144255 | lifeskim:mentions | umls-concept:C1150299 | lld:lifeskim |
| pubmed-article:9144255 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:9144255 | pubmed:dateCreated | 1997-6-5 | lld:pubmed |
| pubmed-article:9144255 | pubmed:abstractText | The functional expression of homo-oligomeric alpha7 neuronal nicotinic and type 3 serotonin receptors is dependent on the activity of a cyclophilin. In this paper we demonstrate that the mechanism of cyclophilin action during functional homo-oligomeric receptor expression in Xenopus oocytes is distinct from the calcineurin-dependent immunosuppressive mechanism by showing that a nonimmunosuppressive analog of cyclosporin A (CsA), SDZ 211-811, reduces functional receptor expression to the same extent as CsA. The cytoplasmic subtype of cyclophilin, cyclophilin A (CyPA), appears to be required for functional receptor expression. This is because overexpression of CyPA and a CyPA mutant that is deficient in CsA binding activity reverses CsA-induced reduction in functional receptor expression. The mechanism of action of CyPA is likely to involve its prolyl isomerase activity because a mutant CyPA with a single amino acid substitution (arginine 55 to alanine) that is predicted to produce a 1000-fold attenuation in isomerase activity fails to reverse the cyclosporin A effect. Our data also suggest that CyPA does not form a stable complex with receptor subunits. | lld:pubmed |
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| pubmed-article:9144255 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9144255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9144255 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9144255 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9144255 | pubmed:month | May | lld:pubmed |
| pubmed-article:9144255 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9144255 | pubmed:author | pubmed-author:PatrickJJ | lld:pubmed |
| pubmed-article:9144255 | pubmed:author | pubmed-author:HelekarS ASA | lld:pubmed |
| pubmed-article:9144255 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9144255 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:9144255 | pubmed:volume | 94 | lld:pubmed |
| pubmed-article:9144255 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9144255 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9144255 | pubmed:pagination | 5432-7 | lld:pubmed |
| pubmed-article:9144255 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9144255 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9144255 | pubmed:articleTitle | Peptidyl prolyl cis-trans isomerase activity of cyclophilin A in functional homo-oligomeric receptor expression. | lld:pubmed |
| pubmed-article:9144255 | pubmed:affiliation | Division of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA. shelekar@bcm.tmc.edu | lld:pubmed |
| pubmed-article:9144255 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9144255 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:9144255 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9144255 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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