Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
Abstract
Epidermal growth factor (EGF) receptor from A-431 cells was purified by affinity chromatography with monoclonal anti-receptor antibodies. The purified radiolabeled receptor was incubated with EGF and then analyzed by gel electrophoresis under nondenaturing conditions. In these gels, the EGF receptor migrates in two forms: a fast-migrating (low) form and an EGF-induced slow-migrating (high) form. On the basis of the various control and calibration experiments described, it is concluded that the low form represents the monomeric 170-kilodalton EGF receptor and the high form represents an EGF receptor dimer. The binding of EGF causes a rapid, temperature-sensitive dimerization of the EGF receptor. Receptor dimerization is fully reversible and involves saturable, noncovalent interactions that are stable at neutral pH and in nonionic detergents. Both the monomeric and dimeric forms of the receptor bind EGF and undergo self-phosphorylation. The dimeric form of the receptor may possess higher ligand binding affinity, and it seems to be phosphorylated earlier than the monomeric form following the addition of EGF and [gamma-32P]ATP. On the basis of these results, it is concluded that receptor oligomerization is an intrinsic property of the occupied EGF receptor and that it may play a role in the activation of the kinase function and the subsequent transmembrane signaling process.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
EGFR is a member of the receptor tyrosine kinase family and a typical transmembrane receptor that initiates signaling cascades upon ligand-stimulated dimerization, thereby activating its tyrosine kinase and multiple downstream effectors.
“Epidermal growth factor receptor (EGFR), a member of the receptor tyrosine kinase family, is a typical transmembrane receptor that initiates signaling cascades upon ligand-stimulated dimerization, thereby activating its tyrosine kinase and multiple downstream effectors.99–101”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [101]
Cites
Ullrich, A., Coussens, L. M., Hayflick, J. S., Dull, T. J., Gray, A., Tam, A. W., Lee, J., Yarden, Y., Libermann, T. A., Schlessinger, J., et al. (1984) · Nature · doi:10.1038/309418a0 · Cited by 2,751 · see citing works
Self-citationHuman insulin receptor and its relationship to the tyrosine kinase family of oncogenes
Ullrich, A., Bell, J. R., Chen, E. Y., Herrera, R., Petruzzelli, L., Dull, T. J., Gray, A., Coussens, L. M., Liao, Y.-C., Tsubokawa, M., et al. (1985) · Nature · doi:10.1038/313756a0 · Cited by 2,251 · see citing works
An enzymic method for the trace iodination of immunoglobulins and other proteins
Marchalonis, J. J. (1969) · Biochemical Journal · doi:10.1042/bj1130299 · Cited by 1,407 · see citing works
Three-Dimensional Structure of Immunoglobulins
Amzel, L. M., & Poljak, R. J. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004525 · Cited by 697 · see citing works
Haigler, H. T., McKanna, J. A., & Cohen, S. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.81.2.382 · Cited by 530 · see citing works
Carpenter, G., King, L. E., & Cohen, S. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30094-7 · Cited by 529 · see citing works
Gill, G. N., Kawamoto, T., Cochet, C., Le, A. D., Sato, J. D., Masui, H., McLeod, C., & Mendelsohn, J. M. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42857-2 · Cited by 455 · see citing works
Schreiber, A. B., Libermann, T. A., Lax, I., Yarden, Y., & Schlessinger, J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33127-2 · Cited by 328 · see citing works
Self-citationKris, R., Lax, I., Gullick, W. J., Waterfield, M. D., Ullrich, A., Fridkin, M., & Schlessinger, J. (1985) · Cell · doi:10.1016/0092-8674(85)90210-7 · Cited by 295 · see citing works
Self-citationProduction of an Epidermal Growth Factor Receptor-Related Protein
Weber, W., Gill, G. N., & Spiess, J. (1984) · Science · doi:10.1126/science.6324343 · Cited by 202 · see citing works
The Drosophila EGF receptor gene homolog: Conservation of both hormone binding and kinase domains
Livneh, E., Glazer, L., Segal, D., Schlessinger, J., & Shilo, B. (1985) · Cell · doi:10.1016/0092-8674(85)90208-9 · Cited by 200 · see citing works
Self-citationSchreiber, A. B., Lax, I., Yarden, Y., Eshhar, Z., & Schlessinger, J. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7535 · Cited by 193 · see citing works
Self-citationGraf, T., & Beug, H. (1983) · Cell · doi:10.1016/0092-8674(83)90130-7 · Cited by 187 · see citing works
Weber, W., Bertics, P. J., & Gill, G. N. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42648-2 · Cited by 185 · see citing works
King, L. E., Carpenter, G. F., & Cohen, S. (1980) · Biochemistry · doi:10.1021/bi00548a040 · Cited by 156 · see citing works
Zidovetzki, R., Yarden, Y., Schlessinger, J., & Jovin, T. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.11.6981 · Cited by 148 · see citing works
Self-citationShechter, Y., Schlessinger, J., Jacobs, S. J., Chang, K., & Cuatrecasas, P. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.5.2135 · Cited by 126 · see citing works
Self-citationHock, R. A., & Hollenberg, M. D. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70368-8 · Cited by 123 · see citing works
Purification of an active EGF receptor kinase with monoclonal antireceptor antibodies.
Yarden, Y., Harari, I., & Schlessinger, J. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89733-2 · Cited by 99 · see citing works
Self-citationBeug, H., & Hayman, M. J. (1984) · Cell · doi:10.1016/0092-8674(84)90046-1 · Cited by 98 · see citing works
Hillman, G. M., & Schlessinger, J. (1982) · Biochemistry · doi:10.1021/bi00536a030 · Cited by 94 · see citing works
Self-citationBiswas, R., Basu, M., Sen-Majumdar, A., & Das, M. (1985) · Biochemistry · doi:10.1021/bi00335a056 · Cited by 89 · see citing works
Fernandez‐Pol, J. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89171-2 · Cited by 62 · see citing works
Chandler, L. P., Chandler, C. E., Hosang, M., & Shooter, E. M. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83629-3 · Cited by 51 · see citing works
Solubilization of membrane receptor for epidermal growth factor
Carpenter, G. F. (1979) · Life Sciences · doi:10.1016/0024-3205(79)90254-6 · Cited by 49 · see citing works
Gool, H. C., Schlessinger, J., Lax, I., Yarden, Y., Libermann, T. A., & Feizi, T. (1983) · Bioscience Reports · doi:10.1007/bf01121031 · Cited by 46 · see citing works
Self-citationDirect linkage of EGF to its receptor: Characterization and biological relevance
Linsley, P. S., & Fox, C. (1980) · Journal of Supramolecular Structure · doi:10.1002/jss.400140404 · Cited by 39 · see citing works
Sequence similarity between EGF receptor and α1-acid glycoprotein
Toh, H., Hayashida, H., Kikuno, R. F., Yasunaga, T., & MIYATA, T. (1985) · Nature · doi:10.1038/314199a0 · Cited by 25 · see citing works
Cr, H., Boothroyd, B., & Gregory, H. (1981) · PubMed · Cited by 25 · see citing works
Linsley, P. S., & Fox, C. (1980) · Journal of Supramolecular Structure · doi:10.1002/jss.400140409 · Cited by 18 · see citing works
Studies on the structure and function of the epidermal-growth-factor receptor
Gregoriou, M., & Rees, A. R. (1984) · Biochemical Society Transactions · doi:10.1042/bst0120160 · Cited by 10 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435 · see citing works
Self-citationEpidermal Growth Factor Receptor Cell Proliferation Signaling Pathways
Wee, P., & Wang, Z. (2017) · Cancers · doi:10.3390/cancers9050052 · Cited by 2,027 · see citing works
Dimerization of cell surface receptors in signal transduction
Heldin, C.-H. (1995) · Cell · doi:10.1016/0092-8674(95)90404-2 · Cited by 1,634 · see citing works
Graus-Porta, D., Beerli, R. R., Daly, J. M., & Hynes, N. E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1647 · Cited by 1,593 · see citing works
Epidermal growth factor receptor: Mechanisms of activation and signalling
Jorissen, R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00098-8 · Cited by 1,565 · see citing works
Veillette, A., Bookman, M. A., Horak, E. M., & Bolen, J. B. (1988) · Cell · doi:10.1016/0092-8674(88)90053-0 · Cited by 1,435 · see citing works
Malignant glioma: genetics and biology of a grave matterPreprint
Maher, E. A., Furnari, F. B., Bachoo, R. M., Rowitch, D. H., Louis, D. N., Cavenee, W. K., & DePinho, R. A. (2001) · Genes & Development · doi:10.1101/gad.891601 · Cited by 1,220 · see citing works
A comprehensive pathway map of epidermal growth factor receptor signaling
Oda, K., Matsuoka, Y., Funahashi, A., & Kitano, H. (2005) · Molecular Systems Biology · doi:10.1038/msb4100014 · Cited by 1,163 · see citing works
Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B. J., & Yarden, Y. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5276 · Cited by 1,039 · see citing works
Self-citationThe ERBB network: at last, cancer therapy meets systems biology
Yarden, Y., & Pines, G. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3309 · Cited by 998 · see citing works
Self-citationThe biology of erbB-2/nue/HER-2 and its role in cancer
Hynes, N. E. (1994) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(94)90012-4 · Cited by 974 · see citing works
Single-molecule imaging of EGFR signalling on the surface of living cells
Sako, Y., Minoghchi, S., & Yanagida, T. (2000) · Nature Cell Biology · doi:10.1038/35004044 · Cited by 889 · see citing works
Hébert, T. E., Moffett, S., Morello, J.-P., Loisel, T. P., Bichet, D. G., Barret, C., & Bouvier, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16384 · Cited by 775 · see citing works
Alroy, I., & Yarden, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00412-2 · Cited by 715 · see citing works
Self-citationQuantification of Short Term Signaling by the Epidermal Growth Factor Receptor
Kholodenko, B. Ν., Demin, O. V., Moehren, G., & Hoek, J. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30169 · Cited by 618 · see citing works
Epidermal growth factor receptors: critical mediators of multiple receptor pathways
Hackel, P. O., Zwick, E., Prenzel, N., & Ullrich, A. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80024-6 · Cited by 606 · see citing works
Sabbah, D. A., Hajjo, R., & Sweidan, K. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200303123102 · Cited by 606 · see citing works
Biochemical and Clinical Implications of the ErbB/HER Signaling Network of Growth Factor Receptors
Klapper, L. N., Kirschbaum, M. H., Seta, M., & Yarden, Y. (1999) · Advances in cancer research · doi:10.1016/s0065-230x(08)60784-8 · Cited by 541 · see citing works
Self-citationVoldborg, B. G. R., Damstrup, L., Spang‐Thomsen, M., & Poulsen, H. S. (1997) · Annals of Oncology · doi:10.1023/a:1008209720526 · Cited by 535 · see citing works
The EGFR Family: Not So Prototypical Receptor Tyrosine KinasesPreprint
Lemmon, M. A., Lemmon, M. A., & Ferguson, K. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020768 · Cited by 472 · see citing works
Self-citationStructure of the Extracellular Region of HER3 Reveals an Interdomain Tether
Cho, H., & Leahy, D. J. (2002) · Science · doi:10.1126/science.1074611 · Cited by 447 · see citing works
Localization of Epidermal Growth Factor-stimulated Ras/Raf-1 Interaction to Caveolae Membrane
Mineo, C., James, G. L., Smart, E. J., & Anderson, R. G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.20.11930 · Cited by 447 · see citing works
The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase.Preprint
Luetteke, N. C., Phillips, H. K., Qiu, T. H., Copeland, N. G., Earp, H. S., Jenkins, N. A., & Lee, D. C. (1994) · Genes & Development · doi:10.1101/gad.8.4.399 · Cited by 438 · see citing works
Fluorescence Correlation Spectroscopy: Past, Present, Future
Elson, E. L. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.012 · Cited by 438 · see citing works
Gadella, T. W. J., & Jovin, T. M. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.6.1543 · Cited by 438 · 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
Epidermal growth factor receptor is a cellular receptor for human cytomegalovirus
Wang, X., Huong, S., Chiu, M. L., Raab‐Traub, N., & Huang, E. (2003) · Nature · doi:10.1038/nature01818 · Cited by 417 · see citing works
Maudsley, S. R., Pierce, K. L., Zamah, A. M., Miller, W. E., Ahn, S., Daaka, Y., Lefkowitz, R. J., & Luttrell, L. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9572 · Cited by 408 · see citing works
Why nature really chose phosphate
Kamerlin, S. C. L., Sharma, P. K., Prasad, R. B., & Warshel, A. (2013) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583512000157 · Cited by 403 · 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
Self-citationRecent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works
Antibodies to a soluble form of a tumor necrosis factor (TNF) receptor have TNF-like activity.
Engelmann, H., Holtmann, H., Brakebusch, C., Avni, Y. S., SAROV, I., Nophar, Y., Hadas, E., Leitner, O., & Wallach, D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77330-4 · Cited by 374 · see citing works
A Structural Perspective on the Regulation of the Epidermal Growth Factor Receptor
Kovács, E., Zorn, J. A., Huang, Y., Barros, T. F., & Kuriyan, J. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034402 · Cited by 371 · see citing works
The type 1 (EGFR-related) family of growth factor receptors and their ligands
Prigent, S. A., & Lemoine, N. R. (1992) · Progress in Growth Factor Research · doi:10.1016/0955-2235(92)90002-y · Cited by 369 · see citing works
Two EGF molecules contribute additively to stabilization of the EGFR dimer
Lemmon, M. A., Bu, Z., Ladbury, J. E., Zhou, M., Pinchasi, D., Lax, I., Engelman, D. M., & Schlessinger, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.2.281 · Cited by 368 · see citing works
Self-citationIntermolecular association of the p185 protein and EGF receptor modulates EGF receptor function
Wada, T., Qian, X., & Greene, M. I. (1990) · Cell · doi:10.1016/0092-8674(90)90697-d · Cited by 361 · see citing works
Quantitative Imaging of Lateral ErbB1 Receptor Signal Propagation in the Plasma Membrane
Verveer, P. J., Wouters, F. S., Reynolds, A. R., & Bastiaens, P. I. H. (2000) · Science · doi:10.1126/science.290.5496.1567 · Cited by 351 · see citing works
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
Structural and functional studies on platelet‐derived growth factor.
Heldin, C. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05523.x · Cited by 337 · see citing works
Reith, A. D., Rottapel, R. K., Giddens, E. B., Brady, C., Forrester, L. M., & Bernstein, A. (1990) · Genes & Development · doi:10.1101/gad.4.3.390 · Cited by 335 · see citing works
Oncogenic activation of the neu‐encoded receptor protein by point mutation and deletion.
Bargmann, C. I., & Weinberg, R. A. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03044.x · Cited by 317 · see citing works
Laminin Polymerization Induces a Receptor–Cytoskeleton Network
Colognato, H., Winkelmann, D. A., & Yurchenco, P. D. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.3.619 · Cited by 303 · see citing works
Protein tyrosine kinases and cancer
Kolibaba, K. S., & Druker, B. J. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00022-x · Cited by 295 · see citing works
EGFR family: Structure physiology signalling and therapeutic targets <sup>†</sup>
Burgess, A. W. (2008) · Growth Factors · doi:10.1080/08977190802312844 · Cited by 288 · see citing works
The epidermal growth factor receptor as a multifunctional allosteric protein
Schlessinger, J. (1988) · Biochemistry · doi:10.1021/bi00409a002 · Cited by 279 · see citing works
Self-citationThe Dominant W 42 Spotting Phenotype Results from a Missense Mutation in the c- kit Receptor Kinase
Tan, J. C., Nocka, K. H., Ray, P., Traktman, P., & Besmer, P. (1990) · Science · doi:10.1126/science.1688471 · Cited by 274 · see citing works
Growth factor receptors, lipid rafts and caveolae: An evolving story
PIKE, L. J. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.05.005 · Cited by 269 · see citing works
Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction.
Furdui, C., Lew, E., Schlessinger, J., & Anderson, K. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.01.022 · Cited by 259 · see citing works
Self-citationThe Epidermal Growth Factor Family
Carpenter, G., & Wahl, M. I. (1991) · Springer eBooks · doi:10.1007/978-1-4612-3210-0_4 · Cited by 260 · see citing works
Li, Q., Kuwahara, H., Yin, L., Li, Y., Ren, J., Yu, W., Carraway, K. L., & Kufe, D. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100359200 · Cited by 257 · see citing works
The epidermal growth factor receptor family
Bazley, L., & Gullick, W. J. (2005) · Endocrine Related Cancer · doi:10.1677/erc.1.01032 · Cited by 251 · see citing works
Goldman, R., Levy, R. B., Peles, E., & Yarden, Y. (1990) · Biochemistry · doi:10.1021/bi00502a002 · Cited by 244 · see citing works
Self-citationGlenney, 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
EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation
Reynolds, A. R., Tischer, C., Verveer, P. J., Rocks, O., & Bastiaens, P. I. H. (2003) · Nature Cell Biology · doi:10.1038/ncb981 · Cited by 235 · see citing works
Milligan, D. L., & Koshland, D. E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68781-2 · Cited by 233 · see citing works
African Flora Has the Potential to Fight Multidrug Resistance of Cancer
Kuete, V., & Efferth, T. (2015) · BioMed Research International · doi:10.1155/2015/914813 · Cited by 233 · see citing works
Schejter, E. D., & Shilo, B. (1989) · Cell · doi:10.1016/0092-8674(89)90642-9 · Cited by 230 · see citing works
Kashles, O., Yarden, Y., Fischer, R., Ullrich, A., & Schlessinger, J. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.3.1454 · Cited by 230 · see citing works
Self-citationBivalence of EGF‐like ligands drives the ErbB signaling network
Tzahar, E., Pinkas‐Kramarski, R., Moyer, J. D., Klapper, L. N., Alroy, I., Levkowitz, G., Shelly, M., Henis, S., Eisenstein, M., Ratzkin, B. J., et al. (1997) · The EMBO Journal · doi:10.1093/emboj/16.16.4938 · Cited by 228 · see citing works
Self-citationKing, C. R., Borrello, I., Bellot, F., Comoglio, P. M., & Schlessinger, J. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02991.x · Cited by 225 · see citing works
Self-citationStructural and functional aspects of G protein-coupled receptor oligomerization
Hébert, T. E., & Bouvier, M. (1998) · Biochemistry and Cell Biology · doi:10.1139/bcb-76-1-1 · Cited by 223 · see citing works
Yu, X., Sharma, K. D., Takahashi, T., Iwamoto, R., & Mekada, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-08-0411 · Cited by 222 · see citing works
Molecular analysis of signal transduction by growth factors
Yarden, Y., & Ullrich, A. (1988) · Biochemistry · doi:10.1021/bi00409a001 · Cited by 218 · see citing works
Self-citationMechanisms of Activation of Receptor Tyrosine Kinases: Monomers or Dimers
MARUYAMA, I. N. (2014) · Cells · doi:10.3390/cells3020304 · Cited by 217 · see citing works
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
Self-citationLigand-induced ErbB receptor dimerization
Lemmon, M. A. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.024 · Cited by 216 · see citing works
Lafky, J. M., Wilken, J. A., Baron, A. T., & Maihle, N. J. (2008) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.01.001 · Cited by 215 · see citing works
Tsai, W., Morielli, A. D., & Peralta, E. G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4597 · Cited by 212 · see citing works
Cell biology beyond the diffraction limit: near-field scanning optical microscopy
de Lange, F., Cambi, A., Huijbens, R. J. F., de Bakker, B. I., Rensen, W. H. J., Parajo, M. F. G., van Hulst, N. F., & Figdor, C. G. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.23.4153 · Cited by 207 · see citing works
PlexinA1 Autoinhibition by the Plexin Sema Domain
Takahashi, T., & Strittmatter, S. M. (2001) · Neuron · doi:10.1016/s0896-6273(01)00216-1 · Cited by 207 · see citing works
A model for insulin binding to the insulin receptor
Schäffer, L. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18833.x · Cited by 205 · see citing works
Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding.
Böni‐Schnetzler, M., & Pilch, P. F. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.7832 · Cited by 205 · see citing works
Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The “Rotation Model”
Purba, E. R., Saita, E., & MARUYAMA, I. N. (2017) · Cells · doi:10.3390/cells6020013 · Cited by 201 · see citing works
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
Needham, S. R., Roberts, S. K., Arkhipov, A. S., Mysore, V. P., Tynan, C. J., Zanetti-Domingues, L. C., Kim, E. T., Losasso, V., Korovesis, D., Hirsch, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms13307 · Cited by 203 · see citing works
Regulation of Lymphocyte Function by Protein Phosphorylation
Perlmutter, R. M., Levin, S. D., Appleby, M. W., Anderson, S., & Alberola‐Ila, J. (1993) · Annual Review of Immunology · doi:10.1146/annurev.immunol.11.1.451 · Cited by 202 · see citing works
Saffarian, S., Yu, L., Elson, E. L., & PIKE, L. J. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.105494 · Cited by 201 · see citing works
Agonistic monoclonal antibodies against the Met receptor dissect the biological responses to HGF
Prat, M., Crepaldi, T., Pennacchietti, S., Bussolino, F., & Comoglio, P. M. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.2.237 · Cited by 194 · see citing works
Molecular basis for multimerization in the activation of the epidermal growth factor receptor
Huang, Y., Bharill, S., Karandur, D., Peterson, S. M., Marita, M., Shi, X., Kaliszewski, M. J., Smith, A. W., Isacoff, E. Y., & Kuriyan, J. (2016) · eLife · doi:10.7554/elife.14107 · Cited by 192 · see citing works
Zhang, S., Chen, C., Li, L., Meng, L., Singh, J., Jiang, N., Deng, X., He, Z., & Lemaux, P. G. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.069005 · Cited by 193 · see citing works
The ErbB-2/HER2 oncogenic receptor of adenocarcinomas: from orphanhood to multiple stromal ligands
Tzahar, E. (1998) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00032-2 · Cited by 192 · see citing works
Rodrigues, G. A., & Park, M. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.6711 · Cited by 192 · see citing works
Honegger, A., Kris, R., Ullrich, A., & Schlessinger, J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.925 · Cited by 189 · see citing works
Self-citationStructural Basis for Negative Cooperativity in Growth Factor Binding to an EGF Receptor
Alvarado, D., Klein, D. E., & Lemmon, M. A. (2010) · Cell · doi:10.1016/j.cell.2010.07.015 · Cited by 181 · see citing works
Epidermal growth factor receptor
Jorissen, R. N., Walker, F., Pouliot, N., Garrett, T., Ward, C. W., & Burgess, A. W. (2003) · Elsevier eBooks · doi:10.1016/b978-012160281-9/50004-9 · Cited by 188 · see citing works
Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
Wouters, F. S., & Bastiaens, P. I. H. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80484-9 · Cited by 188 · see citing works
EGFR targeting for cancer therapy: Pharmacology and immunoconjugates with drugs and nanoparticles
Santos, E. D. S., Nogueira, K. A. B., Crisóstomo, L. C. C. F., Martins, J. R. P., Reis, A. V. F., Neto, J. D. B. V., da Silva, I. J., Pessoa, C., Petrilli, R., & Eloy, J. O. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.120082 · Cited by 186 · see citing works
Segatto, O., King, C. R., Pierce, J. H., Fiore, P. P. D., & Aaronson, S. A. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.12.5570 · Cited by 186 · see citing works
HER2/Neu: mechanisms of dimerization/oligomerization
Brennan, P. J., Kumogai, T., Berezov, A., Murali, R., & Greene, M. I. (2000) · Oncogene · doi:10.1038/sj.onc.1203967 · Cited by 185 · see citing works
Chu, C. T., Everiss, K. D., Wikstrand, C. J., Batra, S. K., Kung, H.-J., & Bigner, D. D. (1997) · Biochemical Journal · doi:10.1042/bj3240855 · Cited by 184 · see citing works
Long range propagation of conformational changes in integrin alpha IIb beta 3.
Du, X., Gu, M., Weisel, J. W., Nagaswami, C., BENNETT, J. S., Bowditch, R. D., & Ginsberg, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49429-5 · Cited by 183 · see citing works
Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system
MacDonald, J. L., & PIKE, L. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707080105 · Cited by 179 · see citing works
FRS2α attenuates FGF receptor signaling by Grb2- mediated recruitment of the ubiquitin ligase Cbl
Wong, A., Lamothe, B., Lee, A., Schlessinger, J., & Lax, I. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.052138899 · Cited by 204 · see citing works
Self-citationThe Epidermal Growth Factor Family
Carpenter, G., & Wahl, M. I. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-49295-2_4 · Cited by 173 · see citing works
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
Nagy, P., Claus, J., Jovin, T. M., & Arndt‐Jovin, D. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002642107 · Cited by 164 · see citing works
Analysis of gain-of-function mutations of the lin-12 gene of Caenorhabditis elegans
Greenwald, I., & Seydoux, G. (1990) · Nature · doi:10.1038/346197a0 · Cited by 159 · see citing works
Qian, X., LeVea, C., Freeman, J. K., Dougall, W. C., & Greene, M. I. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.4.1500 · Cited by 157 · see citing works
Blechman, J. M., Lev, S., Barg, J., Eisenstein, M., Vaks, B., Vogel, Z., Givol, D., & Yarden, Y. (1995) · Cell · doi:10.1016/0092-8674(95)90455-7 · Cited by 156 · see citing works
Self-citationKrause, C. D., Mei, E., Xie, J., Jia, Y., Bopp, M. A., Hochstrasser, R. M., & Pestka, S. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200065-mcp200 · Cited by 155 · see citing works
Extracellular domains drive homo‐ but not hetero‐dimerization of erbB receptors
Ferguson, K. M., Darling, P. J., Mohan, M. J., Macatee, T. L., & Lemmon, M. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4632 · Cited by 153 · see citing works
- Authors
- Yarden, Y., & Schlessinger, J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1987-03-01
- Volume
- 26
- Issue
- 5
- Pages
- 1443-1451
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2095381863
- Cited by
- 627
- References
- 31
- Citations by year
- 2026: 15 · 2025: 11 · 2024: 8 · 2023: 16 · 2022: 21 · 2021: 5 · 2020: 13 · 2019: 12 · 2018: 14 · 2017: 13 · 2016: 14 · 2015: 19 · 2014: 16 · 2013: 12 · 2012: 11
- FWCI
- 21.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 25820)
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- epidermal growth factor receptor, receptor dimerization, receptor oligomerization, epidermal growth factor, A431 cells, receptor phosphorylation, ligand binding affinity, kinase activation, transmembrane signaling
- MeSH terms
- Allosteric Regulation, Cell Line, Cross-Linking Reagents, Epidermal Growth Factor, Humans, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Structure-Activity Relationship, Temperature, Macromolecular Substances, ErbB Receptors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
