Signal transduction by receptors with tyrosine kinase activity

Studies of the HER-2/ neu Proto-Oncogene in Human Breast and Ovarian Cancer

Slamon, D. J., Godolphin, W. J., Jones, L. A., Holt, J. A., Wong, S., Keith, D. E., Levin, W. J., Stuart, S. G., Udove, J. A., Ullrich, A., et al. (1989) · Science · doi:10.1126/science.2470152 · Cited by 6,817 · see citing works

The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains

Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040 · see citing works

The molecular heterogeneity of protein kinase C and its implications for cellular regulation

Nishizuka, Y. (1988) · Nature · doi:10.1038/334661a0 · Cited by 4,213 · see citing works

GROWTH FACTOR RECEPTOR TYROSINE KINASES

Yarden, Y., & Ullrich, A. (1988) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.57.070188.002303 · Cited by 1,837 · see citing works

Single-step induction of mammary adenocarcinoma in transgenic mice bearing the activated c-neu oncogene.

Muller, W., Sinn, E., Pattengale, P., Wallace, R., & Leder, P. (1988) · Cell · doi:10.1016/0092-8674(88)90184-5 · Cited by 1,246 · see citing works

Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185

Bargmann, C. I., Hung, M., & Weinberg, R. A. (1986) · Cell · doi:10.1016/0092-8674(86)90779-8 · Cited by 1,006 · see citing works

Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro

Meisenhelder, J., Suh, P., Rhee, S. G., & Hunter, T. R. (1989) · Cell · doi:10.1016/0092-8674(89)90048-2 · Cited by 955 · see citing works

Recycling receptors: The round-trip itinerary of migrant membrane proteins

Brown, M. S., Anderson, R. G. W., & Goldstein, J. L. (1983) · Cell · doi:10.1016/0092-8674(83)90052-1 · Cited by 792 · see citing works

EGF induces tyrosine phosphorylation of phospholipase C-II: A potential mechanism for EGF receptor signaling

Margolis, B. L., Rhee, S. G., Felder, S., Mervič, M., Lyall, R. M., Levitzki, A., Ullrich, A., Zilberstein, A., & Schlessinger, J. (1989) · Cell · doi:10.1016/0092-8674(89)90047-0 · Cited by 753 · see citing works

Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors.

Kraus, M. H., Issing, W. J., Takashi, M. I. K. I., Popescu, N. C., & Aaronson, S. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.23.9193 · Cited by 737 · see citing works

Signal Transduction by the Platelet-Derived Growth Factor Receptor

Williams, L. T. (1989) · Science · doi:10.1126/science.2538922 · Cited by 644 · see citing works

Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells

Fiore, P. P. D., Pierce, J. H., Fleming, T. P., Hazan, R., Ullrich, A., King, C. R., Schlessinger, J., & Aaronson, S. A. (1987) · Cell · doi:10.1016/0092-8674(87)90592-7 · Cited by 641 · see citing works

Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.

Chou, C. K., Dull, T. J., Russell, D. S., Gherzi, R., Lebwohl, D., Ullrich, A., & Rosen, O. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75716-0 · Cited by 640 · see citing works

Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor

Yarden, Y., & Schlessinger, J. (1987) · Biochemistry · doi:10.1021/bi00379a035 · Cited by 627 · see citing works

Increased expression of the putative growth factor receptor p185HER2 causes transformation and tumorigenesis of NIH 3T3 cells.

Hudziak, R. M., Schlessinger, J., & Ullrich, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.20.7159 · Cited by 616 · see citing works

Two Different Subunits Associate to Create Isoform-Specific Platelet-derived Growth Factor Receptors

Seifert, R. A., Hart, C. E., Phillips, P. E., Forstrom, J. W., Ross, R., Murray, M. J., & Bowen‐Pope, D. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81860-9 · Cited by 610 · see citing works

Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor

Chen, W. S., Lazar, C. S., Poenie, M., Tsien, R. Y., Gill, G. N., & Rosenfeld, M. G. (1987) · Nature · doi:10.1038/328820a0 · Cited by 593 · see citing works

Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor.

Lee, P. E., Johnson, D. E., Cousens, L., Fried, V., & Williams, L. (1989) · Science · doi:10.1126/science.2544996 · Cited by 574 · see citing works

Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation

Yarden, Y., & Schlessinger, J. (1987) · Biochemistry · doi:10.1021/bi00379a034 · Cited by 506 · see citing works

Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF β-receptor

Morrison, D. K., Kaplan, D. R., Escobedo, J. A., Rapp, U. R., Roberts, T. M., & Williams, L. T. (1989) · Cell · doi:10.1016/0092-8674(89)90100-1 · Cited by 495 · see citing works

Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins

Kazlauskas, A., & Cooper, J. A. (1989) · Cell · doi:10.1016/0092-8674(89)90510-2 · Cited by 492 · see citing works

Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing

Honegger, A. (1987) · Cell · doi:10.1016/0092-8674(87)90147-4 · Cited by 491 · see citing works

PDGF induction of tyrosine phosphorylation of GTPase activating protein

Molloy, C. J., Bottaro, D. P., Fleming, T. P., Marshall, M. S., Gibbs, W. W., & Aaronson, S. A. (1989) · Nature · doi:10.1038/342711a0 · Cited by 454 · see citing works

Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body

Felder, S., Miller, K., Moehren, G., Ullrich, A., Schlessinger, J., & Hopkins, C. R. (1990) · Cell · doi:10.1016/0092-8674(90)90474-s · Cited by 445 · see citing works

Epidermal-Growth-Factor-Dependent Transformation by a Human EGF Receptor Proto-Oncogene

Velu, T. J., Beguinot, L., Vass, W. C., Willingham, M. C., Merlino, G. T., Pastan, I. H., & Lowy, D. R. (1987) · Science · doi:10.1126/science.3500513 · Cited by 433 · see citing works

A point mutation in the neu oncogene mimics ligand induction of receptor aggregation

Weiner, D. B., Liu, J., Cohen, J. A., Williams, W. V., & Greene, M. I. (1989) · Nature · doi:10.1038/339230a0 · Cited by 424 · see citing works

Signal transduction by allosteric receptor oligomerization

Schlessinger, J. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90219-8 · Cited by 399 · see citing works

A mutant insulin receptor with defective tyrosine kinase displays no biologic activity and does not undergo endocytosis.

McClain, D. A., Maegawa, H., Lee, J., Dull, T. J., Ulrich, A. K., & Olefsky, J. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47847-7 · Cited by 397 · see citing works

Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium.

Wahl, M. I., Nishibe, S., Suh, P., Rhee, S. G., & Carpenter, G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.5.1568 · Cited by 382 · see citing works

Signal transmission by the insulin-like growth factors

Czech, M. (1989) · Cell · doi:10.1016/0092-8674(89)90281-x · Cited by 380 · see citing works

Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity

White, M. F., Livingston, J. N., Backer, J., Lauris, V., Dull, T. J., Ullrich, A., & Kahn, C. R. (1988) · Cell · doi:10.1016/s0092-8674(88)80008-4 · Cited by 369 · see citing works

Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation

Chen, W. S., Lazar, C. S., Lund, K. A., Welsh, J. B., Chang, C.-P., Walton, G. M., Der, C. J., Wiley, H. S., Gill, G. N., & Rosenfeld, M. G. (1989) · Cell · doi:10.1016/0092-8674(89)90867-2 · Cited by 350 · see citing works

Dimerization of B-type Platelet-derived Growth Factor Receptors Occurs After Ligand Binding and Is Closely Associated with Receptor Kinase Activation

Heldin, C., Ernlund, A., Rorsman, C., & Rönnstrand, L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81879-8 · Cited by 349 · see citing works

Novel putative receptor tyrosine kinase encoded by the melanoma-inducing Tu locus in Xiphophorus

Wittbrodt, J., Adam, D., Malitschek, B., Mäueler, W., Raulf, F., Telling, A., Robertson, S. M., & Schartl, M. (1989) · Nature · doi:10.1038/341415a0 · Cited by 330 · see citing works

Transforming potential of the c-fms proto-oncogene (CSF-1 receptor)

Roussel, M. F., Dull, T. J., Rettenmier, C. W., Ralph, P., Ullrich, A., & Sherr, C. J. (1987) · Nature · doi:10.1038/325549a0 · Cited by 324 · see citing works

Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms

Lin, C. R. (1986) · Cell · doi:10.1016/0092-8674(86)90006-1 · Cited by 318 · see citing works

The colony stimulating factor-1 receptor associates with and activates phosphatidylinositol-3 kinase

Varticovski, L., Druker, B. J., Morrison, D. K., Cantley, L. C., & Roberts, T. M. (1989) · Nature · doi:10.1038/342699a0 · Cited by 313 · see citing works

Ligand-induced endocytosis of the EGF receptor is blocked by mutational inactivation and by microinjection of anti-phosphotyrosine antibodies

Glenney, J. R., Chen, W. S., Lazar, C. S., Walton, G. M., Zokas, L., Rosenfeld, M. G., & Gill, G. N. (1988) · Cell · doi:10.1016/0092-8674(88)90405-9 · Cited by 242 · see citing works

Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system.

Wiley, H. S. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.2.801 · Cited by 232 · see citing works

Primary Structure of a Putative Receptor for a Ligand of the Insulin Family

Shier, P., & Watt, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63737-8 · Cited by 224 · see citing works

A point mutation in the extracellular domain of the human CSF-1 receptor (c-fms proto-oncogene product) activates its transforming potential

Roussel, M. F., Downing, J. R., Rettenmier, C. W., & Sherr, C. J. (1988) · Cell · doi:10.1016/0092-8674(88)90243-7 · Cited by 223 · see citing works

Differential signalling potential of insulin‐ and IGF‐1‐receptor cytoplasmic domains.

Lammers, R., Gray, A., Schlessinger, J., & Ullrich, A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03517.x · Cited by 221 · see citing works

Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent.

Cochet, C., Kashles, O., CHAMBAZ, E. M., Borrello, I., King, C. R., & Schlessinger, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69070-2 · Cited by 217 · see citing works

Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C.

Kumjian, D. A., Wahl, M. I., Rhee, S. G., & Daniel, T. O. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.21.8232 · Cited by 217 · see citing works

A point mutation at the ATP‐binding site of the EGF‐receptor abolishes signal transduction.

Moolenaar, W. H., Bierman, A. J., Tilly, B. C., et al. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02866.x · Cited by 215 · see citing works

All Autophosphorylation Sites of Epidermal Growth Factor (EGF) Receptor and HER2/neu Are Located in Their Carboxyl-terminal Tails

Margolis, B. L., Lax, I., Kris, R., Dombalagian, M., Honegger, A., Howk, R. S., Givol, D., Ullrich, A., & Schlessinger, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81674-x · Cited by 211 · see citing works

Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells.

Livneh, E., Prywes, R., Kashles, O., Reiss, N. A., Sasson, I., Mory, Y. Y., Ullrich, A., & Schlessinger, J. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67114-5 · Cited by 202 · see citing works

Receptor for acidic fibroblast growth factor is related to the tyrosine kinase encoded by the fms-like gene (FLG).

Ruta, M., Burgess, W. H., Givol, D., et al. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8722 · Cited by 202 · see citing works

Immunological relationships between receptors for insulin and insulin-like growth factor I. Evidence for structural heterogeneity of insulin-like growth factor I receptors involving hybrids with insulin receptors

Soos, M. A., & Siddle, K. (1989) · Biochemical Journal · doi:10.1042/bj2630553 · Cited by 198 · see citing works

Functional analysis of the ligand binding site of EGF‐receptor utilizing chimeric chicken/human receptor molecules.

Lax, I., Bellot, F., Howk, R. S., Ullrich, A., Givol, D., & Schlessinger, J. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03393.x · Cited by 195 · see citing works

A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF

Escobedo, J. A., & Williams, L. T. (1988) · Nature · doi:10.1038/335085a0 · Cited by 194 · see citing works

A Mutant Epidermal Growth Factor Receptor with Defective Protein Tyrosine Kinase Is Unable To Stimulate Proto-Oncogene Expression and DNA Synthesis

Honegger, A., Szapary, D., Schmidt, A., Lyall, R. M., OBBERGHEN, E. V., Dull, T. J., Ullrich, A., & Schlessinger, J. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.12.4568 · Cited by 189 · see citing works

Isoform‐specific induction of actin reorganization by platelet‐derived growth factor suggests that the functionally active receptor is a dimer.

Hammacher, A., Mellström, K., Heldin, C., & Westermark, B. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08385.x · Cited by 189 · see citing works

Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.

Margolis, B. L., Bellot, F., Honegger, A., Ullrich, A., Schlessinger, J., & Zilberstein, A. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.435 · Cited by 184 · see citing works

The protein-tyrosine kinase activity of the insulin receptor is necessary for insulin-mediated receptor down-regulation.

Russell, D., Gherzi, R., Johnson, E., Chou, C., & Rosen, O. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60889-0 · Cited by 175 · see citing works

Epidermal growth factor binding induces a conformational change in the external domain of its receptor.

Greenfield, C., Hiles, I., Waterfield, M. D., Federwisch, M., Wollmer, A., Blundell, T. L., & McDonald, N. Q. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08596.x · Cited by 169 · see citing works

Mutations in the cytoplasmic domain of EGF receptor affect EGF binding and receptor internalization.

Prywes, R., Livneh, E., Ullrich, A., et al. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04482.x · Cited by 166 · see citing works

Identification of a developmentally regulated protein-tyrosine kinase by using anti-phosphotyrosine antibodies to screen a cDNA expression library.

Pasquale, E. B., & Singer, S. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5449 · Cited by 165 · see citing works

A chimaeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor

Riedel, H., Dull, T. J., Schlessinger, J., et al. (1986) · Nature · doi:10.1038/324068a0 · Cited by 164 · see citing works

Effect of Phospholipase C-γ Overexpression on PDGF-induced Second Messengers and Mitogenesis

Margolis, B. L., Zilberstein, A., Franks, C., Felder, S., Kremer, S., Ullrich, A., Rhee, S. G., Skorecki, K. L., & Schlessinger, J. (1990) · Science · doi:10.1126/science.2333512 · Cited by 161 · see citing works

Independent mechanisms account for the regulation by protein kinase C of the epidermal growth factor receptor affinity and tyrosine-protein kinase activity.

Davis, R. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76563-6 · Cited by 160 · see citing works

Oncogenic Activation of p185neu Stimulates Tyrosine Phosphorylation In Vivo

Stern, D. F., Kamps, M. P., & Cao, H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3969-3973.1988 · Cited by 147 · see citing works

Activation of the feline c-fms proto-oncogene: Multiple alterations are required to generate a fully transformed phenotype

Woolford, J., McAuliffe, A., & Rohrschneider, L. R. (1988) · Cell · doi:10.1016/0092-8674(88)90242-5 · Cited by 147 · see citing works

Phospholipase C‐gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF‐1.

Downing, J. R., Margolis, B. L., Zilberstein, A., et al. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08496.x · Cited by 145 · see citing works

HER2 cytoplasmic domain generates normal mitogenic and transforming signals in a chimeric receptor.

Lee, J., Dull, T. J., Lax, I., et al. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03361.x · Cited by 140 · see citing works

Evidence for Epidermal Growth Factor (EGF)-Induced Intermolecular Autophosphorylation of the EGF Receptors in Living Cells

Honegger, A., Schmidt, A., Ullrich, A., & Schlessinger, J. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4035 · Cited by 132 · see citing works

Ligand activation of overexpressed epidermal growth factor receptors transforms NIH 3T3 mouse fibroblasts.

Riedel, H., Massoglia, S. L., Schlessinger, J., & Ullrich, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.5.1477 · Cited by 130 · see citing works

Ca2+-mobilizing actions of platelet-derived growth factor differ from those of bombesin and vasopressin in Swiss 3T3 mouse cells.

López‐Rivas, A., Mendoza, S. A., Nånberg, E., et al. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5768 · Cited by 125 · see citing works

Biological activities of EGF‐receptor mutants with individually altered autophosphorylation sites.

Honegger, A., Dull, T. J., Bellot, F., OBBERGHEN, E. V., Szapary, D., Schmidt, A., Ullrich, A., & Schlessinger, J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03169.x · Cited by 123 · see citing works

Truncation of the human EGF receptor leads to differential transforming potentials in primary avian fibroblasts and erythroblasts.

Khazaie, K., Dull, T. J., Graf, T., Schlessinger, J., Ullrich, A., Beug, H., & Vennström, B. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03171.x · Cited by 122 · see citing works

Kinetic parameters of the protein tyrosine kinase activity of EGF‐receptor mutants with individually altered autophosphorylation sites.

Honegger, A., Dull, T. J., Szapary, D., Komoriya, A., Kris, R., Ullrich, A., & Schlessinger, J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03170.x · Cited by 117 · see citing works

Alteration of epidermal growth factor receptor activity by mutation of its primary carboxyl-terminal site of tyrosine self-phosphorylation.

Bertics, P. J., Chen, W. S., Hubler, L., Lazar, C. S., Rosenfeld, M. G., & Gill, G. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68968-9 · Cited by 111 · see citing works

Relationship of site-specific beta subunit tyrosine autophosphorylation to insulin activation of the insulin receptor (tyrosine) protein kinase activity.

Tornqvist, H. E., & Avruch, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68823-4 · Cited by 104 · see citing works

Cytoplasmic domains determine signal specificity, cellular routing characteristics and influence ligand binding of epidermal growth factor and insulin receptors.

Riedel, H., Dull, T. J., Honegger, A., Schlessinger, J., & Ullrich, A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08444.x · Cited by 87 · see citing works

Separate endocytic pathways of kinase-defective and -active EGF receptor mutants expressed in same cells.

Honegger, A., Schmidt, A. G., Ullrich, A., et al. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.5.1541 · Cited by 84 · see citing works

Activation of the epidermal growth factor receptor tyrosine protein kinase in the absence of receptor oligomerization.

Northwood, I. C., & Davis, R. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68517-5 · Cited by 83 · see citing works

Release of a Phorbol Ester-Induced Mitogenic Block by Mutation at Thr-654 of the Epidermal Growth Factor Receptor

Livneh, E., Dull, T. J., Berent, E., Prywes, R., Ullrich, A., & Schlessinger, J. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.6.2302 · Cited by 83 · see citing works

Hormone Binding Site of the Insulin Receptor: Analysis Using Photoaffinity-Mediated Avidin Complexing

Wedekind, F., Baer-Pontzen, K., Bala-Mohan, S., et al. (1989) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1989.370.1.251 · Cited by 81 · see citing works

An insertional mutant of epidermal growth factor receptor allows dissection of diverse receptor functions.

Livneh, E., Reiss, N. A., Berent, E., Ullrich, A., & Schlessinger, J. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02558.x · Cited by 80 · see citing works

Identification of autophosphorylation sites of HER2/neu.

Hazan, R. B., Margolis, B. L., Dombalagian, M., Ullrich, A., Zilberstein, A., & Schlessinger, J. (1990) · PubMed · Cited by 75 · see citing works

Selectivity of phospholipase C phosphorylation by the epidermal growth factor receptor, the insulin receptor, and their cytoplasmic domains.

Nishibe, S., Wahl, M. I., Wedegaertner, P., et al. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.424 · Cited by 67 · see citing works

The unique insert of cellular and viral fms protein tyrosine kinase domains is dispensable for enzymatic and transforming activities.

Taylor, G. R., Reedijk, M., Rothwell, V. M., Rohrschneider, L. R., & Pawson, T. J. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03611.x · Cited by 66 · see citing works

Intermolecular transphosphorylation between insulin receptors and EGF‐insulin receptor chimerae.

Ballotti, R., Lammers, R., Scimeca, J., et al. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08491.x · Cited by 65 · see citing works

Growth factors in biology and medicine

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Functional Heterogeneity of Proto-Oncogene Tyrosine Kinases: the C Terminus of the Human Epidermal Growth Factor Receptor Facilitates Cell Proliferation

Velu, T. J., Vass, W. C., Lowy, D. R., & Beguinot, L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1772 · Cited by 55 · see citing works

Analysis of mammalian fibroblast transformation by normal and mutated human EGF receptors.

Jd, H., Hsuan, J. J., & Waterfield, M. D. (1989) · PubMed · Cited by 53 · see citing works

Signal Transduction in Hamster Fibroblasts Overexpressing the Human EGF Receptor

L’Allemain, G., Seuwen, K., Velu, T. J., et al. (1989) · Growth Factors · doi:10.3109/08977198909000255 · Cited by 24 · see citing works

A Close-Up Look at a Secret Soviet Radar

Norman, C. A. (1987) · Science · doi:10.1126/science.237.4821.1408 · Cited by 10 · see citing works

Critical nodes in signalling pathways: insights into insulin action

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Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer

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Melanin pigmentation in mammalian skin and its hormonal regulation

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Insulin Resistance and the Polycystic Ovary Syndrome Revisited: An Update on Mechanisms and Implications

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