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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1998-3-5
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pubmed:abstractText |
CLC-0, a member of the CLC family of Cl(-)-conducting ion channels, consists of an N-terminal hydrophobic core and a C-terminal region that is thought to be cytoplasmic. This study provides evidence that the C-terminal region is a mechanistically relevant cytoplasmic domain of the CLC-0 ion channel. Both a point mutation and a 37-residue deletion in this region cause drastic alterations in voltage-dependent gating of CLC-0 current expressed in Xenopus oocytes. CLC-0 current is not observed when the entire C-terminal region is deleted, but functional channels are efficiently reconstituted by co-injection of separate cRNA constructs encoding the N-terminal transmembrane and the C-terminal cytoplasmic domains. Moreover, reconstitution of CLC-0 can be achieved by co-injection of cRNA encoding the transmembrane domain along with Escherichia coli-expressed C-terminal domain polypeptide.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1315-21
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:9477958-Animals,
pubmed-meshheading:9477958-Chloride Channels,
pubmed-meshheading:9477958-Cytoplasm,
pubmed-meshheading:9477958-Goats,
pubmed-meshheading:9477958-Membrane Proteins,
pubmed-meshheading:9477958-Microinjections,
pubmed-meshheading:9477958-Mutagenesis, Site-Directed,
pubmed-meshheading:9477958-Oocytes,
pubmed-meshheading:9477958-Patch-Clamp Techniques,
pubmed-meshheading:9477958-Protein Folding,
pubmed-meshheading:9477958-Protein Structure, Tertiary,
pubmed-meshheading:9477958-Xenopus
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pubmed:year |
1998
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pubmed:articleTitle |
Formation of CLC-0 chloride channels from separated transmembrane and cytoplasmic domains.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts, USA.
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pubmed:publicationType |
Journal Article
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