Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5060
pubmed:dateCreated
1992-6-23
pubmed:abstractText
The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Glutamates, http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Glycine, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/N-Methylaspartate, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1217-21
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:1350383-Amino Acid Sequence, pubmed-meshheading:1350383-Animals, pubmed-meshheading:1350383-Base Sequence, pubmed-meshheading:1350383-Brain, pubmed-meshheading:1350383-Cell Line, pubmed-meshheading:1350383-Cloning, Molecular, pubmed-meshheading:1350383-DNA, pubmed-meshheading:1350383-Glutamates, pubmed-meshheading:1350383-Glutamic Acid, pubmed-meshheading:1350383-Glycine, pubmed-meshheading:1350383-Macromolecular Substances, pubmed-meshheading:1350383-Magnesium, pubmed-meshheading:1350383-Membrane Potentials, pubmed-meshheading:1350383-Molecular Sequence Data, pubmed-meshheading:1350383-Multigene Family, pubmed-meshheading:1350383-N-Methylaspartate, pubmed-meshheading:1350383-Oligonucleotide Probes, pubmed-meshheading:1350383-Organ Specificity, pubmed-meshheading:1350383-Peptides, pubmed-meshheading:1350383-RNA, Messenger, pubmed-meshheading:1350383-Rats, pubmed-meshheading:1350383-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:1350383-Recombinant Proteins, pubmed-meshheading:1350383-Sequence Homology, Nucleic Acid, pubmed-meshheading:1350383-Transfection
pubmed:year
1992
pubmed:articleTitle
Heteromeric NMDA receptors: molecular and functional distinction of subtypes.
pubmed:affiliation
Center for Molecular Biology, University of Heidelberg, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't