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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 |
1998-2-24
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pubmed:abstractText |
In order to further investigate a G-protein activated inwardly rectifying potassium channel subunit, GIRK1 was expressed in Xenopus oocytes (where it coassembles with the endogenous GIRK5). The mechanism underlying ion permeation and rectification were measured in isolated inside-out patches. Single channel current amplitudes under symmetrical K+ concentrations at different holding potentials were evaluated. Inward-rectification of K+-currents through open GIRK1/GIRK5 channels was removed by washing out polyamines and Mg2+ ions. We developed a simple 'two-sites-three-barrier' (2S3B) Eyring rate theory model of K+ ion permeation for GIRK1/GIRK5 channels. The resulting optimized parameter-set will be used as a working model for subsequent investigation regarding K+ permeation process through the GIRK1/GIRK5 channel.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
1368
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
167-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9459595-Animals,
pubmed-meshheading:9459595-Cations, Divalent,
pubmed-meshheading:9459595-G Protein-Coupled Inwardly-Rectifying Potassium Channels,
pubmed-meshheading:9459595-Ion Channel Gating,
pubmed-meshheading:9459595-Ion Transport,
pubmed-meshheading:9459595-Magnesium,
pubmed-meshheading:9459595-Membrane Potentials,
pubmed-meshheading:9459595-Oocytes,
pubmed-meshheading:9459595-Patch-Clamp Techniques,
pubmed-meshheading:9459595-Polyamines,
pubmed-meshheading:9459595-Potassium,
pubmed-meshheading:9459595-Potassium Channels,
pubmed-meshheading:9459595-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:9459595-Xenopus laevis
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pubmed:year |
1998
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pubmed:articleTitle |
Ion permeation through a G-protein activated (GIRK1/GIRK5) inwardly rectifying potassium channel.
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pubmed:affiliation |
Department of Medical Physics and Biophysics, Graz, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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