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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 |
2009-2-27
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pubmed:abstractText |
CFTR contributes to HCO(3)(-) transport in epithelial cells both directly (by HCO(3)(-) permeation through the channel) and indirectly (by regulating Cl(-)/HCO(3)(-) exchange proteins). While loss of HCO(3)(-) transport is highly relevant to cystic fibrosis, the relative importance of direct and indirect HCO(3)(-) transport it is currently unknown.
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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 |
Mar
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pubmed:issn |
1873-5010
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-21
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pubmed:meshHeading |
pubmed-meshheading:19019741-Animals,
pubmed-meshheading:19019741-Bicarbonates,
pubmed-meshheading:19019741-Chlorides,
pubmed-meshheading:19019741-Cricetinae,
pubmed-meshheading:19019741-Cystic Fibrosis,
pubmed-meshheading:19019741-Cystic Fibrosis Transmembrane Conductance Regulator,
pubmed-meshheading:19019741-Disease Models, Animal,
pubmed-meshheading:19019741-Ion Transport,
pubmed-meshheading:19019741-Mutation,
pubmed-meshheading:19019741-Patch-Clamp Techniques,
pubmed-meshheading:19019741-Permeability
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pubmed:year |
2009
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|
pubmed:articleTitle |
Mechanism of direct bicarbonate transport by the CFTR anion channel.
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pubmed:affiliation |
Department of Physiology & Biophysics, Dalhousie University, Nova Scotia, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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