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rdf:type |
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lifeskim:mentions |
umls-concept:C0002345,
umls-concept:C0006556,
umls-concept:C0017428,
umls-concept:C0027950,
umls-concept:C0031727,
umls-concept:C0205419,
umls-concept:C0597357,
umls-concept:C0678594,
umls-concept:C0681842,
umls-concept:C1414387,
umls-concept:C1514562,
umls-concept:C1522642,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1883712
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pubmed:issue |
17
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pubmed:dateCreated |
1994-9-14
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pubmed:databankReference |
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pubmed:abstractText |
Heterodimers of types I and II serine/threonine kinase receptor monomers compose the active receptor complex for ligands of the transforming growth factor beta family. Here we show that the genomic organization of coding sequences for the intracellular domain of a widely expressed type I serine/threonine kinase receptor is similar to that of the activin type II receptor gene. The genomic structure and cDNA clones indicate that poly(A) addition to alternative exons at each of three carboxyl-terminal coding exon-intron junctions may be a common feature of both type I and II receptor genes. The predicted products are monomers truncated at kinase subdomains VII, IX, and X which vary in kinase activity and potential serine, threonine, and tyrosine phosphorylation sites. These results suggest that combinations of variants that affect the signal-transducing intracellular kinase domain of both type I and II receptor monomers within the transforming growth factor beta ligand family may add to the heterogeneity of biological effects of individual ligands in the family.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1310899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1318045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1319744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1326293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1328888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1330691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1333888,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1646080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-1846977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-7680959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-7682895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8235612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8242742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8242743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8253771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8321198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8333865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8388126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8389353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8389764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8395914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8058741-8397373
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7957-61
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8058741-Alternative Splicing,
pubmed-meshheading:8058741-Amino Acid Sequence,
pubmed-meshheading:8058741-Base Sequence,
pubmed-meshheading:8058741-Carcinoma, Hepatocellular,
pubmed-meshheading:8058741-Cell Line,
pubmed-meshheading:8058741-Cloning, Molecular,
pubmed-meshheading:8058741-Conserved Sequence,
pubmed-meshheading:8058741-DNA, Complementary,
pubmed-meshheading:8058741-DNA Primers,
pubmed-meshheading:8058741-Gene Expression,
pubmed-meshheading:8058741-Genetic Variation,
pubmed-meshheading:8058741-Humans,
pubmed-meshheading:8058741-Liver Neoplasms,
pubmed-meshheading:8058741-Macromolecular Substances,
pubmed-meshheading:8058741-Molecular Sequence Data,
pubmed-meshheading:8058741-Poly A,
pubmed-meshheading:8058741-Polymerase Chain Reaction,
pubmed-meshheading:8058741-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8058741-RNA, Messenger,
pubmed-meshheading:8058741-Receptors, Growth Factor,
pubmed-meshheading:8058741-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:8058741-Sequence Homology, Amino Acid,
pubmed-meshheading:8058741-Transforming Growth Factor beta,
pubmed-meshheading:8058741-Tumor Cells, Cultured
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pubmed:year |
1994
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