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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2001-12-28
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pubmed:abstractText |
We show here that ergtoxin (ErgTx) is a bona fide, specific blocker of the human ether-a-go-go-related gene (HERG) channels. It does not affect the function of either M-eag or M-elk channels. A chimeric construction containing a segment of the P-region of M-eag channel inserted into the HERG channel drastically diminished or completely abolished the inhibitory effect of ErgTx, whereas chimeras of the P-region of HERG channel into M-eag channels recovered the inhibitory effect. From the P-region point mutants of HERG channel assays, only the mutant N598Q shows about 25% decrement of the ErgTx inhibitory effect. ErgTx recognizes the P-region of HERG channels, blocking the channel function with a K(d) in the order of 12 nM.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ERG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ERG1 potassium channel,
http://linkedlifedata.com/resource/pubmed/chemical/Ether-A-Go-Go Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/KCNH6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnh1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Scorpion Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/ergotoxin, Centruroides noxius
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
510
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
45-9
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pubmed:dateRevised |
2008-10-28
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pubmed:meshHeading |
pubmed-meshheading:11755529-Amino Acid Sequence,
pubmed-meshheading:11755529-Animals,
pubmed-meshheading:11755529-Binding Sites,
pubmed-meshheading:11755529-Cation Transport Proteins,
pubmed-meshheading:11755529-Chromosome Mapping,
pubmed-meshheading:11755529-DNA-Binding Proteins,
pubmed-meshheading:11755529-Electrophysiology,
pubmed-meshheading:11755529-Ether-A-Go-Go Potassium Channels,
pubmed-meshheading:11755529-Female,
pubmed-meshheading:11755529-Gene Expression,
pubmed-meshheading:11755529-Humans,
pubmed-meshheading:11755529-Ligands,
pubmed-meshheading:11755529-Molecular Sequence Data,
pubmed-meshheading:11755529-Mutagenesis, Site-Directed,
pubmed-meshheading:11755529-Oocytes,
pubmed-meshheading:11755529-Potassium Channel Blockers,
pubmed-meshheading:11755529-Potassium Channels,
pubmed-meshheading:11755529-Potassium Channels, Voltage-Gated,
pubmed-meshheading:11755529-Recombinant Fusion Proteins,
pubmed-meshheading:11755529-Scorpion Venoms,
pubmed-meshheading:11755529-Trans-Activators,
pubmed-meshheading:11755529-Xenopus laevis
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pubmed:year |
2002
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pubmed:articleTitle |
Mapping the receptor site for ergtoxin, a specific blocker of ERG channels.
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pubmed:affiliation |
Department of Molecular Recognition and Structural Biology, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad 2001, P.O. Box 510-3, Cuernavaca 62210, Mexico.
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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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