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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 |
2011-7-8
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pubmed:abstractText |
The early description of the intercalated disc defined 3 structures, all of them involved in cell-cell communication: desmosomes, gap junctions, and adherens junctions. Current evidence demonstrates that molecules not involved in providing a physical continuum between cells also populate the intercalated disc. Key among them is the voltage-gated sodium channel complex. An important component of this complex is the cytoskeletal adaptor protein Ankyrin-G (AnkG).
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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:month |
Jul
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pubmed:issn |
1524-4571
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
8
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pubmed:volume |
109
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-201
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pubmed:dateRevised |
2011-9-27
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pubmed:meshHeading |
pubmed-meshheading:21617128-Animals,
pubmed-meshheading:21617128-Ankyrins,
pubmed-meshheading:21617128-Cell Communication,
pubmed-meshheading:21617128-Connexin 43,
pubmed-meshheading:21617128-Desmosomes,
pubmed-meshheading:21617128-Gap Junctions,
pubmed-meshheading:21617128-Heart,
pubmed-meshheading:21617128-Ion Channel Gating,
pubmed-meshheading:21617128-Plakophilins,
pubmed-meshheading:21617128-Protein Binding,
pubmed-meshheading:21617128-Rats,
pubmed-meshheading:21617128-Sodium Channels
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pubmed:year |
2011
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pubmed:articleTitle |
Interactions between ankyrin-G, Plakophilin-2, and Connexin43 at the cardiac intercalated disc.
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pubmed:affiliation |
Division of Cardiovascular Medicine, University of Michigan Medical School, Ann Arbor, MI, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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