rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
15
|
pubmed:dateCreated |
1994-8-22
|
pubmed:databankReference |
|
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.
|
pubmed:grant |
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1314044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1315052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1329206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1337927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1374769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1381042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1382314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1382336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1394433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1674742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1681587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1699567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1717158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-1869570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2166337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2168579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2174719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2174871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2457089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2480525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2543272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2556640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2825805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2828372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-2844410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-3714490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-489565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-7108955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-7685642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-7685711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-7694406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-8094892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-8316301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-8382377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-8389959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8041762-8396474
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0027-8424
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
19
|
pubmed:volume |
91
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
7154-8
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:8041762-Amino Acid Sequence,
pubmed-meshheading:8041762-Animals,
pubmed-meshheading:8041762-Base Sequence,
pubmed-meshheading:8041762-Brain,
pubmed-meshheading:8041762-Cell Membrane,
pubmed-meshheading:8041762-Cell-Free System,
pubmed-meshheading:8041762-Cloning, Molecular,
pubmed-meshheading:8041762-DNA,
pubmed-meshheading:8041762-Glycosylation,
pubmed-meshheading:8041762-Goldfish,
pubmed-meshheading:8041762-Molecular Sequence Data,
pubmed-meshheading:8041762-Mutation,
pubmed-meshheading:8041762-Protein Biosynthesis,
pubmed-meshheading:8041762-Protein Conformation,
pubmed-meshheading:8041762-Receptors, Kainic Acid,
pubmed-meshheading:8041762-Sequence Homology, Amino Acid
|
pubmed:year |
1994
|
pubmed:articleTitle |
Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation.
|
pubmed:affiliation |
Department of Pharmacology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|