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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1992-6-2
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pubmed:databankReference |
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pubmed:abstractText |
Functional cDNA clones encoding the human neurokinin-3 receptor were isolated from human brain mRNA. The cloned human neurokinin-3 receptor was expressed in COS cells and Xenopus oocytes, where peptide binding affinity and intracellular effector activation were determined. Neurokinin B is the most potent agonist, followed by eledoisin, substance K and substance P. The binding affinities of these peptides at the human neurokinin-3 receptor differ quantitatively from the rat receptor, implying a functional consequence of the sequence divergence between the two species. Heterologous expression in oocytes revealed that, unlike the neurokinin-1 receptor, the efficacy of ion channel activation mediated by the neurokinin-3 receptor does not approximate the binding affinity. The heterologous expression of the human neurokinin-3 receptor will facilitate further investigation into its biochemical functions.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Chloride Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurokinin A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurokinin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurotransmitter,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Substance P
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
966-72
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1374246-Amino Acid Sequence,
pubmed-meshheading:1374246-Animals,
pubmed-meshheading:1374246-Binding, Competitive,
pubmed-meshheading:1374246-Brain,
pubmed-meshheading:1374246-Cell Line,
pubmed-meshheading:1374246-Chloride Channels,
pubmed-meshheading:1374246-Chlorides,
pubmed-meshheading:1374246-Cloning, Molecular,
pubmed-meshheading:1374246-DNA,
pubmed-meshheading:1374246-Gene Expression,
pubmed-meshheading:1374246-Humans,
pubmed-meshheading:1374246-Kinetics,
pubmed-meshheading:1374246-Membrane Proteins,
pubmed-meshheading:1374246-Molecular Sequence Data,
pubmed-meshheading:1374246-Neurokinin A,
pubmed-meshheading:1374246-Oocytes,
pubmed-meshheading:1374246-RNA, Messenger,
pubmed-meshheading:1374246-Rats,
pubmed-meshheading:1374246-Receptors, Neurokinin-2,
pubmed-meshheading:1374246-Receptors, Neurotransmitter,
pubmed-meshheading:1374246-Recombinant Proteins,
pubmed-meshheading:1374246-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1374246-Substance P,
pubmed-meshheading:1374246-Transfection,
pubmed-meshheading:1374246-Xenopus
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pubmed:year |
1992
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pubmed:articleTitle |
cDNA sequence and heterologous expression of the human neurokinin-3 receptor.
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pubmed:affiliation |
Department of Molecular Pharmacology and Biochemistry, Merck Research Laboratories, Rahway, NJ 07065.
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pubmed:publicationType |
Journal Article,
Comparative Study
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