rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
6
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pubmed:dateCreated |
1990-7-18
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pubmed:abstractText |
The v-erbA oncogene, one of the two oncogenes of the avian erythroblastosis virus, efficiently blocks erythroid differentiation and suppresses erythrocyte-specific gene transcription. Here we show that the overexpressed thyroid hormone receptor c-erbA effectively modulates erythroid differentiation and erythrocyte-specific gene expression in a T3-dependent fashion, when introduced into erythroid cells via a retrovirus. In contrast, the endogenous thyroid hormone receptor does not detectably affect erythroid differentiation. The analysis of a series of chimeric v-/c-erbA proteins suggests that the v-erbA oncoprotein has lost one type of thyroid hormone receptor function (regulating erythrocyte gene transcription in response to T3), but constitutively displays another function: it represses transcription in the absence of T3. The region responsible for the loss of hormone-dependent regulator activity of v-erbA has been mapped to the very C-terminus of c-erbA, encompassing a cluster of highly conserved amino acid residues with the potential to form an amphipathic alpha-helix.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins v-erbA,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retroviridae Proteins, Oncogenic,
http://linkedlifedata.com/resource/pubmed/chemical/Triiodothyronine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1035-49
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1972036-Alpharetrovirus,
pubmed-meshheading:1972036-Amino Acid Sequence,
pubmed-meshheading:1972036-Animals,
pubmed-meshheading:1972036-Antigens, Surface,
pubmed-meshheading:1972036-Avian leukosis virus,
pubmed-meshheading:1972036-Cell Transformation, Neoplastic,
pubmed-meshheading:1972036-Cells, Cultured,
pubmed-meshheading:1972036-Chick Embryo,
pubmed-meshheading:1972036-Clone Cells,
pubmed-meshheading:1972036-Erythroblasts,
pubmed-meshheading:1972036-Erythrocytes,
pubmed-meshheading:1972036-Gene Expression Regulation,
pubmed-meshheading:1972036-Genetic Vectors,
pubmed-meshheading:1972036-Hemoglobins,
pubmed-meshheading:1972036-Molecular Sequence Data,
pubmed-meshheading:1972036-Oncogene Proteins v-erbA,
pubmed-meshheading:1972036-Oncogenes,
pubmed-meshheading:1972036-Protein Conformation,
pubmed-meshheading:1972036-Protein-Tyrosine Kinases,
pubmed-meshheading:1972036-Receptors, Thyroid Hormone,
pubmed-meshheading:1972036-Recombinant Fusion Proteins,
pubmed-meshheading:1972036-Retroviridae Proteins, Oncogenic,
pubmed-meshheading:1972036-Suppression, Genetic,
pubmed-meshheading:1972036-Transcription, Genetic,
pubmed-meshheading:1972036-Triiodothyronine
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pubmed:year |
1990
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pubmed:articleTitle |
v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA.
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pubmed:affiliation |
Institute of Molecular Pathology, Vienna, Austria.
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pubmed:publicationType |
Journal Article
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