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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1991-10-3
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pubmed:databankReference | |
pubmed:abstractText |
The complete amino acid sequence of a potassium channel protein of rat brain, Kv3.2b, plus a partial sequence of a related channel, Kv3.2c, are deduced from molecular cloning of the respective cDNA's. Kv3.2b and Kv3.2c share extensive amino acid sequence identity with a previously identified channel, RKShIIIA[1], before diverging to unique carboxy termini. Probes specific for Kv3.2b and RKShIIIA detect similarly sized mRNA's on Northern blots. These two proteins are encoded by a single gene based on genomic Southern blotting, and therefore arise by alternative splicing. In vitro transcribed mRNA for Kv3.2b induces the expression of outward K+ currents in Xenopus oocytes under voltage-clamp conditions.
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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 |
Aug
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
288
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pubmed:geneSymbol |
Kv3.2b
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
163-7
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1879548-Amino Acid Sequence,
pubmed-meshheading:1879548-Animals,
pubmed-meshheading:1879548-Base Sequence,
pubmed-meshheading:1879548-Blotting, Northern,
pubmed-meshheading:1879548-Blotting, Southern,
pubmed-meshheading:1879548-Brain,
pubmed-meshheading:1879548-Cloning, Molecular,
pubmed-meshheading:1879548-Drosophila,
pubmed-meshheading:1879548-Membrane Potentials,
pubmed-meshheading:1879548-Molecular Sequence Data,
pubmed-meshheading:1879548-Oocytes,
pubmed-meshheading:1879548-Potassium Channels,
pubmed-meshheading:1879548-RNA Splicing,
pubmed-meshheading:1879548-Rats,
pubmed-meshheading:1879548-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1879548-Xenopus
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pubmed:year |
1991
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pubmed:articleTitle |
Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.
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pubmed:affiliation |
Department of Pharmacology, Merck, Sharp and Dohme Research Laboratories, West Point, PA 19486.
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pubmed:publicationType |
Journal Article
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