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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-11-4
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L13266,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L13267,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L13268,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24523,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24524,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24525,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24526,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24527,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24528,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/L24529
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pubmed:abstractText |
Several cDNA clones encoding human N-methyl-D-aspartate receptor (hNR1) subunit polypeptides were isolated from a human hippocampus library. Degenerate oligodeoxyribonucleotide (oligo) primers based on the published rat NR1 (rNR1) amino acid (aa) sequence [K. Moriyoshi et al. Nature 354 (1991) 31-37] amplified a 0.7-kb fragment from a human hippocampus cDNA library, via the polymerase chain reaction (PCR). This fragment was used as a probe for subsequent hybridization screening. DNA sequence analysis of 28 plaque-purified clones indicated three distinct classes, designated hNR1-1, hNR1-2 and hNR1-3, presumably generated by alternative RNA splicing. One of these clones, hNR1-1(5A), was isolated as a full-length cDNA. The hNR1-2 and hNR1-3 cDNAs represented 66.8 and 98.9%, respectively, of the total aa coding information predicted for the polypeptides. The hNR1 cDNAs demonstrated an 84-90.8% nucleotide (nt) identity with the corresponding rodent cDNAs. The nt sequences of hNR1-1, hNR1-2 and hNR1-3 would encode 885-, 901- and 938-aa proteins, respectively, that have 99.1-99.8% identity with the corresponding rodent NR1 (roNR1) subunits. The changes between the predicted aa sequences of hNR1 and the corresponding roNR1 subunits are confined to the extracellular N-terminal regions. We have also identified two possible allelic variations of the hNR1-3 cDNA that result in aa substitutions in the extracellular N- and C-terminal regions. One of these naturally occurring aa variations is situated within a potential glutamate-binding site.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0378-1119
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
131
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pubmed:geneSymbol |
hNR1-1,
hNR1-2,
hNR1-3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
293-8
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8406025-Alternative Splicing,
pubmed-meshheading:8406025-Amino Acid Sequence,
pubmed-meshheading:8406025-Animals,
pubmed-meshheading:8406025-Base Sequence,
pubmed-meshheading:8406025-Cloning, Molecular,
pubmed-meshheading:8406025-DNA,
pubmed-meshheading:8406025-Hippocampus,
pubmed-meshheading:8406025-Humans,
pubmed-meshheading:8406025-Molecular Sequence Data,
pubmed-meshheading:8406025-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:8406025-Sequence Analysis, DNA,
pubmed-meshheading:8406025-Sequence Homology, Amino Acid,
pubmed-meshheading:8406025-Sequence Homology, Nucleic Acid
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pubmed:year |
1993
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pubmed:articleTitle |
Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing.
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pubmed:affiliation |
Allelix Biopharmaceuticals Inc., Mississauga, Ontario, Canada.
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pubmed:publicationType |
Journal Article
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