◀ Back to EGF

EGF — PTK7

Text-mined interactions from Literome

Countaway et al., J Biol Chem 1992 : Increased protein-tyrosine kinase activity is observed following the binding of EGF to the receptor
Gilliland et al., J Biol Chem 1992 : Epidermal growth factor (EGF) or platelet derived growth factor binding to their receptor on fibroblasts induces tyrosine phosphorylation of PLC gamma 1 and stable association of PLC gamma 1 with the receptor protein tyrosine kinase
Sambhi et al., Biochem Med Metab Biol 1992 : The specific binding of 125I labeled EGF to aortic membranes also increased ( 11,429 +/- 728 vs 8630 +/- 420 cpm/mg protein, P less than 0.05 ) with a parallel increase in the protein tyrosine kinase activity of the membranes indicating that the enhanced EGFR mRNA expression resulted in increased activity of a functional receptor
Zhang et al., Dev Biol 1992 : EGF stimulated protein tyrosine kinase activity about 1.6-fold over basal levels
Kang et al., Med Hypotheses 2008 : In the process of promoting wound healing, epidermal growth factor (EGF) activates protein kinase C, protein tyrosine kinase and ERK MAPK ( mitogen activated protein kinase )
Carpenter et al., J Biol Chem 1991 : All receptors bound EGF and exhibited EGF stimulated protein tyrosine kinase activity in vivo as assayed using a 125I labeled monoclonal anti-phosphotyrosine antibody
Honegger et al., Mol Cell Biol 1990 : In response to epidermal growth factor (EGF) stimulation, the intrinsic protein tyrosine kinase of EGF receptor is activated, leading to tyrosine phosphorylation of several cellular substrate proteins, including the EGF receptor molecule itself
Defize et al., J Cell Biol 1989 : We show that blocking of low affinity EGFR by mAb 2E9 has almost no effect on the activation of the receptor protein-tyrosine kinase by EGF , suggesting that EGFR kinase activation occurs exclusively through the subclass of high affinity EGFR ( 5-10 % )
Seger et al., J Biol Chem 1988 : The 140-kDa fragment retains its EGF binding site and its EGF dependent protein tyrosine kinase activity on exogenous substrates, but it loses its capacity to undergo self-phosphorylation
Martin et al., Cancer Surv 1986 (Neoplasms) : Binding of EGF to the external domain of the receptor activates the protein-tyrosine kinase activity of the receptor, and this elevated kinase activity is presumed to be involved in the activation of cell growth
Gullick et al., Eur J Biochem 1986 : Antibodies to the ATP binding site of the human epidermal growth factor (EGF) receptor as specific inhibitors of EGF stimulated protein-tyrosine kinase activity
Clark et al., J Cell Physiol 1988 (Chromosome Deletion) : Despite the loss of these sites the EGF receptor from CHO 11 cells binds EGF, demonstrates protein tyrosine kinase activity in response to EGF , and transduces a mitogenic signal
Honegger et al., Mol Cell Biol 1987 : Unlike the wild-type EGF-receptor expressed in these cells, which exhibited EGF dependent protein tyrosine kinase activity, the mutant receptor lacked protein tyrosine kinase activity and was unable to undergo autophosphorylation and to phosphorylate exogenous substrates
Das et al., Endocrinology 1994 : Affinity cross linking studies ascertained the size of the EGF-R, and its bioactivity was examined by determining EGF dependent subcellular protein tyrosine kinase activity and receptor autophosphorylation
Gronowski et al., Endocrinology 1995 : To assess how this association can influence receptor function, EGF stimulated protein-tyrosine kinase activity was examined in the detergent-soluble and -insoluble ( cytoskeletal ) fractions of human A431 epidermoid carcinoma cells
Lemmon et al., Trends Biochem Sci 1994 : Receptor oligomerization was initially proposed as a mechanism by which epidermal growth factor activates the protein tyrosine kinase activity of its receptor
Paria et al., Biol Reprod 1994 : The size of EGF-R was determined by affinity cross linking studies, and its bioactivity was examined by determining EGF dependent subcellular protein tyrosine kinase ( PTK ) activity ... However, EGF induced PTK activity was significantly elevated above background levels during the period of renewed embryonic development, but not during arrested embryonic development
Chen et al., J Med Chem 1994 : Potent inhibitors of EGF dependent protein tyrosine kinase ( PTK ) activity were synthesized in a series of 5- [ ( 2,5-dihydroxybenzyl ) amino ] salicylates
Hishinuma et al., Endocr J 1994 (Cystadenoma, Papillary...) : This study shows that stimulation of the protein tyrosine kinase activity by basic FGF, EGF , and IGF-1 promoted DNA replication by the human thyroid cancer cell line
Sherrill et al., Biochemistry 1996 : The binding of epidermal growth factor (EGF) to epidermal growth factor receptor ( EGF receptor ) induces dimerization of the receptor and activation of its protein tyrosine kinase
Wiederholt et al., Invest Ophthalmol Vis Sci 1998 : Protein tyrosine kinase ( PTK ) was stimulated by epidermal growth factor (EGF) and was inhibited by genistein or tyrphostin 51