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PMID: 3006340 Published · ppublish English Journal Article

Analysis of the autophosphorylation activity of transformation defective mutants of avian erythroblastosis virus.

Virology ·Vol. 150 ·No. 1 ·1986-04-15 ·Pages 270-5

Hayman MJ, Kitchener G, Knight J, McMahon J, Watson R, Beug H

Abstract

The v-erb B protein of avian erythroblastosis virus (AEV) possesses an associated protein kinase activity in vitro. Analysis of temperature-sensitive mutants, and nonconditional host range mutants of AEV demonstrated that there was no simple correlation between this autophosphorylation activity and the transformation ability of the various AEV mutants. These data suggest that although this kinase activity may be central to transformation by AEV it is in itself insufficient.

MeSH Terms
Alpharetrovirus/genetics Animals Avian Leukosis Virus/genetics Cell Membrane/metabolism Cell Transformation, Viral Cells, Cultured Endoplasmic Reticulum/metabolism ErbB Receptors Mutation Oncogene Proteins, Viral/metabolism Oncogenes Phosphorylation Protein-Tyrosine Kinases/metabolism Receptors, Cell Surface/metabolism Temperature
Chemicals
Oncogene Proteins, Viral Receptors, Cell Surface ErbB Receptors Protein-Tyrosine Kinases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hayman M J
Kitchener G
Knight J
McMahon J
Watson R
Beug H
Article Info
Journal
Virology
Abbr.
Virology
ISSN
0042-6822
Published
1986-04-15
Pages
270-5
Language
English
Region
United States
NLM ID
0110674
Subset
IM
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