Specific and saturable binding of pp60v-src to plasma membranes: Evidence for a myristyl-src receptor
- 1 July 1989
- Vol. 58 (2) , 281-286
- https://doi.org/10.1016/0092-8674(89)90842-8
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- In vitro synthesis of pp60v-src: myristylation in a cell-free system.Molecular and Cellular Biology, 1988
- Myristylation of picornavirus capsid protein VP4 and its structural significanceNature, 1987
- Processing of p60v-src to its myristylated membrane-bound form.Molecular and Cellular Biology, 1985
- N-terminal deletions in Rous sarcoma virus p60src: effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene.Molecular and Cellular Biology, 1985
- Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein.Molecular and Cellular Biology, 1984
- A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation.Molecular and Cellular Biology, 1984
- [4] Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNAPublished by Elsevier ,1983
- Avian sarcoma virus-transforming protein, pp60src shows protein kinase activity specific for tyrosineNature, 1980
- Identification of a transformation-specific antigen induced by an avian sarcoma virusNature, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970