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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 |
2003-12-3
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pubmed:abstractText |
Sam68 is one of the most studied members of the STAR family of RNA-binding proteins since its identification over a decade ago. Since its ascension into prominence, enormous progress has been made to unmask the link between the RNA-binding properties of Sam68 and the regulation of cellular processes including signal transduction, cell cycle regulation and tumorigenesis and RNA biogenesis in general. In this review we provide a detailed description of the functional domains of Sam68 and the possible biological roles that justify its superSTAR status.
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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 |
Dec
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
1653
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
73-86
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14643926-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:14643926-Amino Acid Sequence,
pubmed-meshheading:14643926-Animals,
pubmed-meshheading:14643926-Cell Cycle,
pubmed-meshheading:14643926-Cell Transformation, Neoplastic,
pubmed-meshheading:14643926-DNA-Binding Proteins,
pubmed-meshheading:14643926-Humans,
pubmed-meshheading:14643926-Molecular Sequence Data,
pubmed-meshheading:14643926-Phosphoproteins,
pubmed-meshheading:14643926-Protein Structure, Tertiary,
pubmed-meshheading:14643926-RNA-Binding Proteins,
pubmed-meshheading:14643926-Sequence Homology, Amino Acid,
pubmed-meshheading:14643926-Signal Transduction
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pubmed:year |
2003
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pubmed:articleTitle |
Sam68, the KH domain-containing superSTAR.
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pubmed:affiliation |
Terry Fox Molecular Oncology Group and Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, H3T 1E2 Québec, Canada.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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