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rdf:type |
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lifeskim:mentions |
umls-concept:C0071746,
umls-concept:C0080093,
umls-concept:C0900627,
umls-concept:C1152805,
umls-concept:C1333226,
umls-concept:C1514562,
umls-concept:C1704675,
umls-concept:C1705335,
umls-concept:C1711351,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
5231
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pubmed:dateCreated |
1995-10-25
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P02719,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P07174,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08510,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08511,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08909,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08953,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P10499,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P12526,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P14842,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P15389,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P15390,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P18090,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P25445,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P26591,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P29534,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P30083,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P34082,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P35331,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P35353,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P35439,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/Q00960
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pubmed:abstractText |
The N-methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal tSXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1737-40
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7569905-Amino Acid Sequence,
pubmed-meshheading:7569905-Animals,
pubmed-meshheading:7569905-Base Sequence,
pubmed-meshheading:7569905-Cells, Cultured,
pubmed-meshheading:7569905-Cytoplasm,
pubmed-meshheading:7569905-Genes, Reporter,
pubmed-meshheading:7569905-Hippocampus,
pubmed-meshheading:7569905-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:7569905-Membrane Proteins,
pubmed-meshheading:7569905-Molecular Sequence Data,
pubmed-meshheading:7569905-Nerve Tissue Proteins,
pubmed-meshheading:7569905-Neuronal Plasticity,
pubmed-meshheading:7569905-Neurons,
pubmed-meshheading:7569905-RNA Splicing,
pubmed-meshheading:7569905-Rats,
pubmed-meshheading:7569905-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:7569905-Recombinant Fusion Proteins,
pubmed-meshheading:7569905-Signal Transduction
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pubmed:year |
1995
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pubmed:articleTitle |
Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.
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pubmed:affiliation |
Center for Molecular Biology (ZMBH), University of Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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