Linked Life Data

7993626

Source:http://linkedlifedata.com/resource/pubmed/id/7993626

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-1-18
pubmed:abstractText
We investigated the transmembrane topology of the glutamate receptor GluR1 by introducing N-glycosylation sites as reporter sites for an extracellular location of the respective site. Our data show that the N-terminus is extracellular, whereas the C-terminus is intracellular. Most importantly, we found only three transmembrane domains (designated TMD A, TMD B, and TMD C), which correspond to the previously proposed TMDs I, III, and IV, respectively. Contrary to earlier models, the putative channel-lining hydrophobic domain TMD II does not span the membrane, but either lies in close proximity to the intracellular face of the plasma membrane or loops into the membrane without transversing it. Furthermore, the region between TMDs III and IV, in previous models believed to be intracellular, is an entirely extracellular domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0896-6273
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:geneSymbol
GluR1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1331-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1.
pubmed:affiliation
Molecular Neurobiology Laboratory, Salk Institute, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't