| pubmed-article:2878364 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C0005595 | lld:lifeskim |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C1257751 | lld:lifeskim |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C0272138 | lld:lifeskim |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
| pubmed-article:2878364 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:2878364 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2878364 | pubmed:dateCreated | 1987-1-20 | lld:pubmed |
| pubmed-article:2878364 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2878364 | 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. | lld:pubmed |
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| pubmed-article:2878364 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2878364 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2878364 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2878364 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2878364 | pubmed:month | May | lld:pubmed |
| pubmed-article:2878364 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2878364 | pubmed:author | pubmed-author:GradJJ | lld:pubmed |
| pubmed-article:2878364 | pubmed:author | pubmed-author:BeugHH | lld:pubmed |
| pubmed-article:2878364 | pubmed:author | pubmed-author:EngelJ DJD | lld:pubmed |
| pubmed-article:2878364 | pubmed:author | pubmed-author:TrainorCC | lld:pubmed |
| pubmed-article:2878364 | pubmed:author | pubmed-author:ChoiO ROR | lld:pubmed |
| pubmed-article:2878364 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2878364 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:2878364 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2878364 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2878364 | pubmed:pagination | 1751-9 | lld:pubmed |
| pubmed-article:2878364 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2878364 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2878364 | pubmed:articleTitle | A single amino acid substitution in v-erbB confers a thermolabile phenotype to ts167 avian erythroblastosis virus-transformed erythroid cells. | lld:pubmed |
| pubmed-article:2878364 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2878364 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2878364 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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