Source:http://linkedlifedata.com/resource/pubmed/id/10998040
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2000-11-13
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pubmed:abstractText |
Inward-rectifier potassium (Kir) channels comprise a superfamily of potassium (K+) channels with unique structural and functional properties. Expressed in virtually all types of cells they are responsible for setting the resting membrane potential, controlling the excitation threshold and secreting K+ ions. All Kir channels present an inwardly rectifying current-voltage relation, meaning that at any given driving force the inward flow of K+ ions exceeds the outward flow for the opposite driving force. This inward-rectification is due to a voltage-dependent block of the channel pore by intracellular polyamines and magnesium. The present molecular-biophysical understanding of inward-rectification and its physiological consequences is the topic of this review. In addition to polyamines, Kir channels are gated by intracellular protons, G-proteins, ATP and phospholipids depending on the respective Kir subfamily as detailed in the following review articles.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Polyamines,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5824-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:10998040-Animals,
pubmed-meshheading:10998040-Cloning, Molecular,
pubmed-meshheading:10998040-Humans,
pubmed-meshheading:10998040-Ion Channel Gating,
pubmed-meshheading:10998040-Ion Transport,
pubmed-meshheading:10998040-Membrane Potentials,
pubmed-meshheading:10998040-Models, Molecular,
pubmed-meshheading:10998040-Polyamines,
pubmed-meshheading:10998040-Potassium,
pubmed-meshheading:10998040-Potassium Channels,
pubmed-meshheading:10998040-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:10998040-Protein Conformation,
pubmed-meshheading:10998040-Recombinant Fusion Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Polyamines as gating molecules of inward-rectifier K+ channels.
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pubmed:affiliation |
Department of Physiology II, University of Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Review
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