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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2006-2-22
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pubmed:abstractText |
The ternary complex of integrin-linked kinase (ILK), PINCH and parvin functions as a signalling platform for integrins by interfacing with the actin cytoskeleton and many diverse signalling pathways. All these proteins have synergistic functions at focal adhesions, but recent work has indicated that these proteins might also have separate roles within a cell. They function as regulators of gene transcription or cell-cell adhesion.
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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 |
Jan
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pubmed:issn |
1471-0072
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20-31
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16493410-Actinin,
pubmed-meshheading:16493410-Amino Acid Sequence,
pubmed-meshheading:16493410-Animals,
pubmed-meshheading:16493410-DNA-Binding Proteins,
pubmed-meshheading:16493410-Humans,
pubmed-meshheading:16493410-Integrins,
pubmed-meshheading:16493410-Mice,
pubmed-meshheading:16493410-Molecular Sequence Data,
pubmed-meshheading:16493410-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16493410-Signal Transduction,
pubmed-meshheading:16493410-Zinc Fingers
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pubmed:year |
2006
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pubmed:articleTitle |
ILK, PINCH and parvin: the tIPP of integrin signalling.
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pubmed:affiliation |
Department of Molecular Medicine, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsreid, Germany. legate@biochem.mpg.de
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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