| pubmed-article:1696637 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1696637 | lifeskim:mentions | umls-concept:C0000742 | lld:lifeskim |
| pubmed-article:1696637 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:1696637 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:1696637 | lifeskim:mentions | umls-concept:C1150607 | lld:lifeskim |
| pubmed-article:1696637 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:1696637 | pubmed:dateCreated | 1990-9-14 | lld:pubmed |
| pubmed-article:1696637 | pubmed:abstractText | The effect of two missense mutations in abl on transformation by Abelson murine leukemia virus was evaluated. These mutations led to the substitution of a histidine for Tyr-590 and a glycine for Lys-536. Both changes gave rise to strains that were temperature dependent for transformation of both NIH 3T3 cells and lymphoid cells when expressed in the context of a truncated Abelson protein. In the context of the prototype P120 v-abl protein, the Gly-536 substitution generated a host range mutant that induced conditional transformation in lymphoid cells but had only a subtle effect on NIH 3T3 cells. The combination of both substitutions gave rise to a P120 strain that was temperature sensitive for both NIH 3T3 and lymphoid cell transformation. The Abelson proteins encoded by the temperature-sensitive strain displayed in vitro kinase activities that were reduced when compared with those of wild-type proteins. In vivo, levels of phosphotyrosine were reduced only at the restrictive temperature. Analysis of cells expressing either the wild-type P160 v-abl protein or the P210 bcr/abl protein and an Abelson protein encoded by a temperature-sensitive strain failed to correct this defect, suggesting either that tyrosine phosphorylation in vivo is an intramolecular reaction or that the protein encoded by the temperature-sensitive strain is a poor substrate for tyrosine phosphorylation in vivo. These results raise the possibility that tyrosine phosphorylation of Abelson protein plays a role in transformation. | lld:pubmed |
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| pubmed-article:1696637 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1696637 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1696637 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1696637 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1696637 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1696637 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:1696637 | pubmed:author | pubmed-author:RosenbergNN | lld:pubmed |
| pubmed-article:1696637 | pubmed:author | pubmed-author:EngelmanAA | lld:pubmed |
| pubmed-article:1696637 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1696637 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:1696637 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1696637 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1696637 | pubmed:pagination | 4242-51 | lld:pubmed |
| pubmed-article:1696637 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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