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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 |
2011-4-13
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pubmed:abstractText |
CLC anion transport proteins function as Cl (-) channels and Cl (-) /H (+) exchangers and are found in all major groups of life including archaebacteria. Early electrophysiological studies suggested that CLC anion channels have two pores that are opened and closed independently by a "fast" gating process operating on a millisecond timescale, and a "common" or "slow" gate that opens and closes both pores simultaneously with a timescale of seconds (Figure 1A). Subsequent biochemical and molecular experiments suggested that CLC channels/transporters are homodomeric proteins ( 1-3) .
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
1933-6969
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
101-5
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pubmed:meshHeading |
pubmed-meshheading:21317557-Adenosine Triphosphate,
pubmed-meshheading:21317557-Animals,
pubmed-meshheading:21317557-Caenorhabditis elegans,
pubmed-meshheading:21317557-Chloride Channels,
pubmed-meshheading:21317557-Crystallography, X-Ray,
pubmed-meshheading:21317557-Cystathionine beta-Synthase,
pubmed-meshheading:21317557-Ligands,
pubmed-meshheading:21317557-Membrane Potentials,
pubmed-meshheading:21317557-Molecular Conformation,
pubmed-meshheading:21317557-Mutagenesis,
pubmed-meshheading:21317557-Protein Binding,
pubmed-meshheading:21317557-Protein Conformation,
pubmed-meshheading:21317557-Protein Structure, Tertiary
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pubmed:articleTitle |
Putting the pieces together: a crystal clear window into CLC anion channel regulation.
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pubmed:affiliation |
Boylan Center for Cellular and Molecular Physiology, Mount Desert Island Biological Laboratory; Salisbury Cove, ME, USA. kstrange@mdibl.org
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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