A site of tyrosine phosphorylation in the C terminus of the epidermal growth factor receptor is required to activate phospholipase C
暂无分享,去创建一个
S. Rhee | O. Filhol | C. Cochet | Q. Vega | G. Gill | C. P. Chang | Chia-Ping Chang | C. Chang
[1] J. Welsh,et al. A negative feedback loop attenuates EGF-induced morphological changes , 1991, The Journal of cell biology.
[2] T Pawson,et al. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. , 1991, Science.
[3] S. Lev,et al. A specific combination of substrates is involved in signal transduction by the kit‐encoded receptor. , 1991, The EMBO journal.
[4] T. Hunter,et al. Interaction between the epidermal growth factor receptor and phosphoinositide kinases. , 1991, The Journal of biological chemistry.
[5] T. Hunter,et al. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. , 1991, Methods in enzymology.
[6] G. Carpenter,et al. Increase of the catalytic activity of phospholipase C-gamma 1 by tyrosine phosphorylation. , 1990, Science.
[7] I. Parker,et al. Localized all-or-none calcium liberation by inositol trisphosphate. , 1990, Science.
[8] T Pawson,et al. Src homology region 2 domains direct protein-protein interactions in signal transduction. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[9] B. Mayer,et al. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. , 1990, Science.
[10] B. Mayer,et al. Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[11] G. Carpenter,et al. Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro. , 1990, The Journal of biological chemistry.
[12] G. Carpenter,et al. Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells. , 1990, The Journal of biological chemistry.
[13] J. Welsh,et al. Ligand-induced transformation by a noninternalizing epidermal growth factor receptor. , 1990, Science.
[14] A. Ullrich,et al. Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor , 1990, Molecular and cellular biology.
[15] G. M. Walton,et al. Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates. , 1990, The Journal of biological chemistry.
[16] G. M. Walton,et al. Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation , 1989, Cell.
[17] Jonathan A. Cooper,et al. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins , 1989, Cell.
[18] Michael J. Berridge,et al. Inositol phosphates and cell signalling , 1989, Nature.
[19] M. Waterfield,et al. Identification of a novel autophosphorylation site (P4) on the epidermal growth factor receptor. , 1989, The Biochemical journal.
[20] A. Zilberstein,et al. EGF induces tyrosine phosphorylation of phospholipase C-II: A potential mechanism for EGF receptor signaling , 1989, Cell.
[21] G. Carpenter,et al. Tyrosine phosphorylation of phospholipase C-II in vitro by the epidermal growth factor receptor. , 1989, The Journal of biological chemistry.
[22] S. Y. Lee,et al. Studies of inositol phospholipid-specific phospholipase C. , 1989, Science.
[23] P. Libby,et al. PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells , 1989, Cell.
[24] G. Carpenter,et al. Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[25] S. Ryu,et al. Monoclonal antibodies to three phospholipase C isozymes from bovine brain. , 1988, The Journal of biological chemistry.
[26] G. Carpenter,et al. Regulation of epidermal growth factor-stimulated formation of inositol phosphates in A-431 cells by calcium and protein kinase C. , 1988, The Journal of biological chemistry.
[27] J. Glenney,et al. Monoclonal antibodies to phosphotyrosine. , 1988, Journal of immunological methods.
[28] L. Stryer,et al. Highly cooperative opening of calcium channels by inositol 1,4,5-trisphosphate. , 1988, Science.
[29] A. Ullrich,et al. A point mutation at the ATP‐binding site of the EGF‐receptor abolishes signal transduction. , 1988, The EMBO journal.
[30] A. Ullrich,et al. A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis , 1987, Molecular and cellular biology.
[31] T. Lovenberg,et al. Epidermal growth factor stimulates the rapid accumulation of inositol (1,4,5)-trisphosphate and a rise in cytosolic calcium mobilized from intracellular stores in A431 cells. , 1987, The Journal of biological chemistry.
[32] R. Tsien,et al. Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor , 1987, Nature.
[33] R. Tsien,et al. Calcium rises abruptly and briefly throughout the cell at the onset of anaphase. , 1986, Science.
[34] Thomas A. Kunkel,et al. Rapid and efficient site-specific mutagenesis without phenotypic selection. , 1985, Proceedings of the National Academy of Sciences of the United States of America.
[35] J. Downward,et al. Autophosphorylation sites on the epidermal growth factor receptor , 1984, Nature.
[36] M. Berridge,et al. Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides. , 1983, The Biochemical journal.