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rdf:type |
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|
lifeskim:mentions |
|
|
pubmed:issue |
1
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pubmed:dateCreated |
1993-4-13
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pubmed:abstractText |
Recent studies have confirmed several predictions concerning the structure and possible function of dystrophin, including a direct interaction with F-actin and an indirect interaction with laminin via linkage through a transmembrane protein complex. The results of the past year support a role for dystrophin in linking the actin cytoskeleton with the extracellular matrix in striated muscle, but they have not explained its function in other tissues.
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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 |
Feb
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pubmed:issn |
0955-0674
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pubmed:author |
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pubmed:issnType |
Print
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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 |
82-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8448034-Actins,
pubmed-meshheading:8448034-Animals,
pubmed-meshheading:8448034-Cytoskeleton,
pubmed-meshheading:8448034-Dystrophin,
pubmed-meshheading:8448034-Glycosylation,
pubmed-meshheading:8448034-Humans,
pubmed-meshheading:8448034-Microfilament Proteins,
pubmed-meshheading:8448034-Models, Molecular,
pubmed-meshheading:8448034-Muscular Dystrophies,
pubmed-meshheading:8448034-Protein Processing, Post-Translational,
pubmed-meshheading:8448034-Sarcolemma,
pubmed-meshheading:8448034-Torpedo
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pubmed:year |
1993
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pubmed:articleTitle |
Dystrophin and the membrane skeleton.
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pubmed:affiliation |
University of Wisconsin, Department of Physiology, Madison 53706.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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