Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries.
Open Access
- 1 December 1988
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 8 (12) , 5541-5544
- https://doi.org/10.1128/mcb.8.12.5541
Abstract
In an attempt to clone protein tyrosine kinases, antiphosphotyrosine antibodies were used to screen lambda gt11 cDNA expression libraries. By this method, a 2.5-kilobase cDNA encoding a novel tyrosine kinase was isolated from a mouse liver cDNA library. This new gene is most closely related to the receptor tyrosine kinases ret, fms, and kit.This publication has 31 references indexed in Scilit:
- Transforming potential of the c-fms proto-oncogene (CSF-1 receptor)Nature, 1987
- Tyr 527 Is Phosphorylated in pp60
c-
src
: Implications for RegulationScience, 1986
- The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF 1Cell, 1985
- The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signallingCell, 1985
- Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sitesNature, 1984
- Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequencesNature, 1984
- Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virusCell, 1983
- Endogenous protein phosphorylation inEscherichia coli extractsBiochemical and Biophysical Research Communications, 1982
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free systemNature, 1982
- Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factorNature, 1982