rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2006-8-18
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pubmed:abstractText |
Identification of rate-limiting steps or components of intracellular second messenger systems holds promise to effectively interfere with these pathways under pathological conditions. The emerging literature on a recently identified family of signalling regulator proteins, called tribbles gives interesting clues for how these proteins seem to link several 'independent' signal processing systems together. Via their unique way of action, tribbles co-ordinate the activation and suppression of the various interacting signalling pathways and therefore appear to be key in determining cell fate while responding to environmental challenges. This review summarises our current understanding of tribbles function and also provides an evolutionary perspective on the various tribbles genes.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRIB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TRIB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TRIB3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/stg protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/tribbles protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1420-682X
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
63
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1632-41
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16715410-Amino Acid Sequence,
pubmed-meshheading:16715410-Animals,
pubmed-meshheading:16715410-Autoimmune Diseases,
pubmed-meshheading:16715410-Biological Evolution,
pubmed-meshheading:16715410-Cell Cycle Proteins,
pubmed-meshheading:16715410-Cell Lineage,
pubmed-meshheading:16715410-Consensus Sequence,
pubmed-meshheading:16715410-Drosophila Proteins,
pubmed-meshheading:16715410-Drosophila melanogaster,
pubmed-meshheading:16715410-Embryonic Development,
pubmed-meshheading:16715410-Evolution, Molecular,
pubmed-meshheading:16715410-Expressed Sequence Tags,
pubmed-meshheading:16715410-Gene Expression Regulation,
pubmed-meshheading:16715410-Humans,
pubmed-meshheading:16715410-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:16715410-Invertebrates,
pubmed-meshheading:16715410-Molecular Sequence Data,
pubmed-meshheading:16715410-Morphogenesis,
pubmed-meshheading:16715410-Neoplasms,
pubmed-meshheading:16715410-Protein Kinases,
pubmed-meshheading:16715410-Protein Structure, Tertiary,
pubmed-meshheading:16715410-Protein Tyrosine Phosphatases,
pubmed-meshheading:16715410-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16715410-Repressor Proteins,
pubmed-meshheading:16715410-Sequence Alignment,
pubmed-meshheading:16715410-Sequence Homology, Amino Acid,
pubmed-meshheading:16715410-Signal Transduction,
pubmed-meshheading:16715410-Species Specificity,
pubmed-meshheading:16715410-Starvation,
pubmed-meshheading:16715410-Vertebrates,
pubmed-meshheading:16715410-Xenopus,
pubmed-meshheading:16715410-Xenopus Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Tribbles: novel regulators of cell function; evolutionary aspects.
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pubmed:affiliation |
Bioinformatics Group, Biological Research Centre, Szeged, Hungary.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review
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