| pubmed-article:8041762 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8041762 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:8041762 | lifeskim:mentions | umls-concept:C0002812 | lld:lifeskim |
| pubmed-article:8041762 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:8041762 | lifeskim:mentions | umls-concept:C0064219 | lld:lifeskim |
| pubmed-article:8041762 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8041762 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:8041762 | pubmed:dateCreated | 1994-8-22 | lld:pubmed |
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| pubmed-article:8041762 | pubmed:abstractText | Glutamate receptors are the primary excitatory neurotransmitter receptors in vertebrate brain and are of critical importance to a wide variety of neurological processes. Recent reports suggest that ionotropic glutamate receptors may have a unique transmembrane topology not shared by other ligand-gated ion channels. We report here the cloning of cDNAs from goldfish brain encoding two homologous kainate receptors with protein molecular masses of 41 kDa. Using a cell-free translation/translocation system, we show that (i) a portion of these receptors previously thought to be a large intracellular loop is actually located extracellularly and (ii) the putative second transmembrane region of the receptor thought to line the ion channel may not be a true membrane-spanning domain. An alternative model for the transmembrane topology of kainate receptors is proposed that could potentially serve as a framework for future detailed study of the structure of this important class of neurotransmitter receptors. | lld:pubmed |
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| pubmed-article:8041762 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8041762 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8041762 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8041762 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8041762 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8041762 | pubmed:author | pubmed-author:OswaldR ERE | lld:pubmed |
| pubmed-article:8041762 | pubmed:author | pubmed-author:YuiTT | lld:pubmed |
| pubmed-article:8041762 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8041762 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:8041762 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:8041762 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8041762 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8041762 | pubmed:pagination | 7154-8 | lld:pubmed |
| pubmed-article:8041762 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8041762 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8041762 | pubmed:articleTitle | Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation. | lld:pubmed |
| pubmed-article:8041762 | pubmed:affiliation | Department of Pharmacology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853. | lld:pubmed |
| pubmed-article:8041762 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8041762 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8041762 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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