rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1987-1-20
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pubmed:databankReference |
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pubmed:abstractText |
A library of recombinant bacteriophage was prepared from ts167 avian erythroblastosis virus-transformed erythroid precursor cells (HD6), and integrated proviruses from three distinct genomic loci were isolated. A subclone of one of these proviruses (pAEV1) was shown to confer temperature-sensitive release from transformation of erythroid precursor cells in vitro. The predicted amino acid sequence of the v-erbB polypeptide from the mutant had a single amino acid change when compared with the wild-type parental virus. When the wild-type amino acid was introduced into the temperature-sensitive avian erythroblastosis virus provirus in pAEV1, all erythroid clones produced in vitro were phenotypically wild type. The mutation is a change from a histidine to an aspartic acid in the temperature-sensitive v-erbB polypeptide. It is located in the center of the tyrosine-specific protein kinase domain and corresponds to amino acid position 826 of the human epidermal growth factor receptor sequence.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2878364-1195397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2878364-158428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2878364-180661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2878364-211440,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2878364-4705382,
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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 |
May
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1751-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2878364-Alpharetrovirus,
pubmed-meshheading:2878364-Amino Acid Sequence,
pubmed-meshheading:2878364-Animals,
pubmed-meshheading:2878364-Avian leukosis virus,
pubmed-meshheading:2878364-Base Sequence,
pubmed-meshheading:2878364-Cell Transformation, Neoplastic,
pubmed-meshheading:2878364-Cells, Cultured,
pubmed-meshheading:2878364-Chick Embryo,
pubmed-meshheading:2878364-Cloning, Molecular,
pubmed-meshheading:2878364-Erythroblasts,
pubmed-meshheading:2878364-Fibroblasts,
pubmed-meshheading:2878364-Genes, Viral,
pubmed-meshheading:2878364-Mutation,
pubmed-meshheading:2878364-Nucleic Acid Hybridization,
pubmed-meshheading:2878364-Oncogene Proteins v-erbB,
pubmed-meshheading:2878364-Phenotype,
pubmed-meshheading:2878364-Transfection,
pubmed-meshheading:2878364-Viral Proteins
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pubmed:year |
1986
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pubmed:articleTitle |
A single amino acid substitution in v-erbB confers a thermolabile phenotype to ts167 avian erythroblastosis virus-transformed erythroid cells.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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