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rdf:type |
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lifeskim:mentions |
umls-concept:C0018787,
umls-concept:C0027769,
umls-concept:C0036450,
umls-concept:C0040549,
umls-concept:C0180683,
umls-concept:C0205409,
umls-concept:C0439799,
umls-concept:C0521425,
umls-concept:C0599295,
umls-concept:C0998342,
umls-concept:C1551083
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pubmed:issue |
8
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pubmed:dateCreated |
1999-5-25
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pubmed:abstractText |
Toxins isolated from a variety of venoms are tools for probing the physiological function and structure of ion channels. The ether-a-go-go-related genes (erg) codify for the K+ channels (ERG), which are crucial in neurons and are impaired in human long-QT syndrome and Drosophila 'seizure' mutants. We have isolated a peptide from the scorpion Centruroides noxius Hoffmann that has no sequence homologies with other toxins, and demonstrate that it specifically inhibits (IC50=16+/-1 nM) only ERG channels of different species and distinct histogenesis. These results open up the possibility of investigating ERG channel structure-function relationships and novel pharmacological tools with potential therapeutic efficacy.
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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/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/Scorpion Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0892-6638
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
953-62
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pubmed:dateRevised |
2008-10-28
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pubmed:meshHeading |
pubmed-meshheading:10224238-Action Potentials,
pubmed-meshheading:10224238-Amino Acid Sequence,
pubmed-meshheading:10224238-Animals,
pubmed-meshheading:10224238-Cation Transport Proteins,
pubmed-meshheading:10224238-Cell Line,
pubmed-meshheading:10224238-DNA-Binding Proteins,
pubmed-meshheading:10224238-Dose-Response Relationship, Drug,
pubmed-meshheading:10224238-Endocrine Glands,
pubmed-meshheading:10224238-Ether-A-Go-Go Potassium Channels,
pubmed-meshheading:10224238-Guinea Pigs,
pubmed-meshheading:10224238-Humans,
pubmed-meshheading:10224238-Kinetics,
pubmed-meshheading:10224238-Mice,
pubmed-meshheading:10224238-Molecular Sequence Data,
pubmed-meshheading:10224238-Myocardium,
pubmed-meshheading:10224238-Neurons,
pubmed-meshheading:10224238-Potassium Channel Blockers,
pubmed-meshheading:10224238-Potassium Channels,
pubmed-meshheading:10224238-Potassium Channels, Voltage-Gated,
pubmed-meshheading:10224238-Rats,
pubmed-meshheading:10224238-Scorpion Venoms,
pubmed-meshheading:10224238-Scorpions,
pubmed-meshheading:10224238-Sequence Homology, Amino Acid,
pubmed-meshheading:10224238-Trans-Activators
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pubmed:year |
1999
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pubmed:articleTitle |
A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom.
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pubmed:affiliation |
Department of Biotechnology and Biosciences, University of Milano-Bicocca, 20126 Milano, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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