The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Autophosphorylation sites on the epidermal growth factor receptor
Abstract
The epidermal growth factor (EGF) receptor is a tyrosine-specific protein kinase with autophosphorylating activity. A 300 amino acid-long region of the receptor's cytoplasmic domain matches (35-90% homology) sequences of transforming proteins from the src family and includes a putative nucleotide binding site. Several of the src transforming proteins have tyrosine kinase activity, but v-erb-B, which appears to be a truncated EGF receptor, is virtually identical to the receptor over this region and yet lacks detectable kinase activity. To locate possible acceptor sites in the v-erb-B protein, we have mapped these sites in the human EGF receptor. We report here that three tyrosine sites near the C-terminus are phosphorylated in vitro. In intact cells, we find that EGF stimulates phosphorylation of several sites, the tyrosine 14 residues from the C-terminus being modified the most extensively. The equivalent site is absent in the v-erb-B protein of avian erythroblastosis virus (AEV) and may influence tyrosine kinase activity.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“First, we observed that POS phagocytosis induced activation of EGFR (p-EGFR), as indicated by phosphorylation of its tyrosine residue 1068 (Tyr1068) (Fig. 6A), a major autophosphorylation site of the receptor.36”
From RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye (2017) · cites this paper as [36]
In the citing paper
“a major autophosphorylation site of the receptor.36”
From RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye (2017) · cites this paper as [36]
Citations
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
Self-citationClose similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
Downward, J., Yarden, Y., Mayes, E., Scrace, G., Totty, N., Stockwell, P., Ullrich, A., Schlessinger, J., & Waterfield, M. D. (1984) · Nature · doi:10.1038/307521a0 · Cited by 2,516
Self-citationA gas-liquid solid phase peptide and protein sequenator.
Hewick, R. M., Hunkapiller, M. W., Hood, L., & Dreyer, W. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43377-7 · Cited by 2,218
CELLULAR ONCOGENES AND RETROVIRUSES
Bishop, J. M. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.001505 · Cited by 1,666
Ushiro, H., & Cohen, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43497-7 · Cited by 1,184
[42] Detection and quantification of phosphotyrosine in proteins
Cooper, J. A., Sefton, B. M., & Hunter, T. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99075-4 · Cited by 1,109
A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.
Cohen, S., Ushiro, H., Stoscheck, C. M., & Chinkers, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68224-4 · Cited by 776
Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells
Hunter, T. R., & Cooper, J. A. (1981) · Cell · doi:10.1016/0092-8674(81)90100-8 · Cited by 670
The erbB gene of avian erythroblastosis virus is a member of the src gene family
Yamamoto, T. S., Nishida, T., Miyajima, N., Kawai, S., Ooi, T., & Toyoshima, K. (1983) · Cell · doi:10.1016/0092-8674(83)90209-x · Cited by 371
Smart, J. E., Oppermann, H., Czernilofsky, A. P., Purchio, A. F., Erikson, R. L., & Bishop, J. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6013 · Cited by 358
Flagged first, then by citations
Research works printed but not linked: 2
- Waterfield, M. D., Scrace, G. & Totty, N. in Practical Protein Biochemistry (ed. Darbre, A.) (Wiley, New York, in the press).
- Hunter, T. & Cooper, J. A. UCLA Symp. molec. cell. Biol. 6, 360 (1983).
Cited by
Sorted by citations
Items 101–200 of 705
Schmidt, M. H. H., Furnari, F. B., Cavenee, W. K., & Bögler, O. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031790100 · Cited by 164
Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.
Countaway, J. L., Nairn, A. C., & Davis, R. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48406-2 · Cited by 157
Cuadrado, A., García‐Fernández, L., González, L., Suárez, Y., Losada, A., Alcaide, V., Martı́nez, T., Fernández-Sousa, J. M., Sánchez-Puelles, J.-M., & Múñoz, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201010200 · Cited by 157
Construction of a Novel Oncogene Based on Synthetic Sequences Encoding Epidermal Growth Factor
Stern, D. F., Hare, D. L., Cecchini, M. A., & Weinberg, R. A. (1987) · Science · doi:10.1126/science.3492043 · Cited by 155
Chang, C.-P., Lazar, C. S., Walsh, B. J., Komuro, M., Collawn, J. F., Kuhn, L. A., Tainer, J. A., Trowbridge, I. S., Farquhar, M. G., & Rosenfeld, M. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36515-9 · Cited by 155
Wu, W., Graves, L. M., Gill, G. N., Parsons, S. J., & Samet, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200437200 · Cited by 154
Protein phosphorylation at tyrosine is induced by the v-erbB gene product in vivo and in vitro
Gilmore, T. D., DeClue, J. E., & Martin, G. S. (1985) · Cell · doi:10.1016/0092-8674(85)90209-0 · Cited by 154
Gotoh, N., Toyoda, M., & Shibuya, M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.4.1824 · Cited by 153
Faucher, M., Gironès, N., Hannun, Y. A., Bell, R. M., & Davis, R. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60718-5 · Cited by 151
Differences in the sites of phosphorylation of the insulin receptor in vivo and in vitro.
White, M. F., Takayama, S., & Kahn, C. R. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39389-4 · Cited by 151
Internalized Epidermal Growth Factor Receptors Participate in the Activation of p21 in Fibroblasts
Haugh, J. M., Huang, A. C., Wiley, H. S., Wells, A. H., & Lauffenburger, D. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34350 · Cited by 151
Verbeek, B. S., Adriaansen-slot, S. S., Feltkamp‐Vroom, T. M., Beckers, T. L., & Rijksen, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00224-5 · Cited by 150
Sorkin, A. D., Helin, K., Waters, C. M., Carpenter, G., & Beguinot, L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42495-7 · Cited by 150
Liu, W., Akhand, A. A., Kato, M., Yokoyama, I., Miyata, T., Kurokawa, K., Uchida, K., & Nakashima, I. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.14.2409 · Cited by 149
Recent advancement of piperidine moiety in treatment of cancer- A review
Goel, P., Alam, O., Naim, M. J., Nawaz, F., Iqbal, M., & Alam, I. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.017 · Cited by 150
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
Chattopadhyay, A., Vecchi, M., Ji, Q.-S., Mernaugh, R. L., & Carpenter, G. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26091 · Cited by 150
Slieker, L. J., Martensen, T. M., & Lane, M. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66858-9 · Cited by 145
The RAS signal transduction pathway and its role in radiation sensitivity
McKenna, W. G., Muschel, R. J., Gupta, A., Hahn, S. M., & Bernhard, E. J. (2003) · Oncogene · doi:10.1038/sj.onc.1206699 · Cited by 143
Ferracini, R., Longati, P., Naldini, L., Vigna, E., & Comoglio, P. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55031-6 · Cited by 143
Epidermal growth factor receptors in lung tumours
Berger, M. S., Gullick, W. J., Greenfield, C., Evans, S. W., Addis, B. J., & Waterfield, M. D. (1987) · The Journal of Pathology · doi:10.1002/path.1711520408 · Cited by 142
Self-citationvan der Geer, P., & Hunter, T. R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06211.x · Cited by 139
Westover, E. J., Covey, D. F., Brockman, H. L., Brown, R. E., & PIKE, L. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304332200 · Cited by 138
Shao, H., Cheng, H. Y., Cook, R. G., & Tweardy, D. J. (2003) · PubMed · Cited by 136
Case, R. D., Piccione, E., Wolf, G., Benett, A. M., Lechleider, R. J., Neel, B. G., & Shoelson, S. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34083-8 · Cited by 131
Batzer, A., Blaikie, P., Nelson, K. N., Schlessinger, J., & Margolis, B. L. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4403 · Cited by 131
Thelemann, A., Petti, F., Griffin, G., Iwata, K., Hunt, T., Settinari, T., Fenyö, D., Gibson, N. W., & Haley, J. D. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400118-mcp200 · Cited by 132
Honegger, A., Schmidt, A., Ullrich, A., & Schlessinger, J. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4035 · Cited by 132
Chylek, L. A., Harris, L. A., Tung, C., Faeder, J. R., Lopez, C. F., & Hlavacek, W. S. (2013) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1245 · Cited by 133
Panayotou, G., Bax, B. D., Gout, I. T., Federwisch, M., Wroblowski, B., Dhand, R., Fry, M., Blundell, T. L., Wollmer, A., & Waterfield, M. D. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05524.x · Cited by 128
Self-citation4. The role of the epidermal growth factor receptor and the c-erbB-2 protein in breast cancer
Gullick, W. J. (1990) · International Journal of Cancer · doi:10.1002/ijc.2910460708 · Cited by 128
Gotoh, N., Tojo, A., Hino, M., Yazaki, Y., & Shibuya, M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90812-y · Cited by 126
Characterization of Glycosylation Sites of the Epidermal Growth Factor Receptor
Zhen, Y., Caprioli, R. M., & Staros, J. V. (2003) · Biochemistry · doi:10.1021/bi027101p · Cited by 126
Akiyama, T., Matsuda, S., Namba, Y., Saito, T., Toyoshima, K., & Yamamoto, T. S. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.2.833 · Cited by 126
Macdonald-Obermann, J. L., & PIKE, L. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586826 · Cited by 125
Cussac, D., Frech, M., & Chardin, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06717.x · Cited by 125
Anti-Oncogenic Activity of Signalling-Defective Epidermal Growth Factor Receptor Mutants
Redemann, N. H., Holzmann, B., von Rüden, T., Wagner, E. F., Schlessinger, J., & Ullrich, A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.491 · Cited by 125
Lund, K. A., Lazar, C. S., Chen, W. S., Walsh, B. J., Welsh, J. B., Herbst, J. J., Walton, G. M., Rosenfeld, M. G., Gill, G. N., & Wiley, H. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30533-1 · Cited by 123
Gotoh, N., Tojo, A., Muroya, K., Hashimoto, Y., Hattori, S., Nakamura, S., Takenawa, T., Yazaki, Y., & Shibuya, M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.167 · Cited by 123
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
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 121
Sasaki, N., Rees-Jones, R. W., Zick, Y., Nissley, S. P., & Rechler, M. M. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39306-7 · Cited by 121
APP-BP1, a Novel Protein That Binds to the Carboxyl-terminal Region of the Amyloid Precursor Protein
Chow, N., Korenberg, J. R., Chen, X.-N., & Neve, R. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11339 · Cited by 118
Okabayashi, Y., Kido, Y., Okutani, T., Sugimoto, Y., Sakaguchi, K., & Kasuga, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32363-3 · Cited by 118
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
Sorkin, A. D., Waters, C. M., Overholser, K. A., & Carpenter, G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92983-2 · Cited by 116
Structure of platelet glycoprotein IIIa. A common subunit for two different membrane receptors.
Zimrin, A. B., Eisman, R., Vilaire, G., Schwartz, E., BENNETT, J. S., & Poncz, M. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113478 · Cited by 114
EGFR gene amplification ‐ rearrangement in human glioblastomas
Schwechheimer, K., Huang, S., & Cavenee, W. K. (1995) · International Journal of Cancer · doi:10.1002/ijc.2910620206 · Cited by 111
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
Molecular Recognition of Gangliosides and Their Potential for Cancer Immunotherapies
Krengel, U., & Bousquet, P. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00325 · Cited by 111
Molecular mechanisms of tubulointerstitial hypertrophy and hyperplasia
Wolf, G., & Neilson, E. G. (1991) · Kidney International · doi:10.1038/ki.1991.52 · Cited by 108
Cellular Functions Regulated by Phosphorylation of EGFR on Tyr845
Sato, K.-I. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140610761 · Cited by 107
Greenfield, C., Patel, G., Clark, S., Jones, N., & Waterfield, M. D. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02793.x · Cited by 109
Self-citationEpidermal growth factor receptor threonine and serine residues phosphorylated in vivo.
Heisermann, G. J., & Gill, G. N. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37684-1 · Cited by 108
Amos, S., Martin, P. M., Polar, G. A., Parsons, S. J., & Hussaini, I. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409056200 · Cited by 107
Ravid, T., Sweeney, C. A., Gee, P., Carraway, K. L., & Goldkorn, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204677200 · Cited by 106
Mechanisms ofegfrGene Transcription Modulation: Relationship to Cancer Risk and Therapy Response
Brandt, B., Meyer-Staeckling, S., Schmidt, H., Agelopoulos, K., & Buerger, H. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-0626 · Cited by 105
Palombella, V. J., Yamashiro, D. J., Maxfield, F. R., Decker, S. J., & Vilček, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61602-3 · Cited by 105
Abl Tyrosine Kinase Regulates Endocytosis of the Epidermal Growth Factor Receptor
Tanos, B. E., & Pendergast, A. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603126200 · Cited by 103
6 Viral Oncogenes and Tyrosine Phosphorylation
Hunter, T. R., & Cooper, J. A. (1986) · The Enzymes · doi:10.1016/s1874-6047(08)60431-x · Cited by 103
Okutani, T., Okabayashi, Y., Kido, Y., Sugimoto, Y., Sakaguchi, K., Matuoka, K., Takenawa, T., & Kasuga, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47424-8 · Cited by 101
Smith, K., Fennelly, J. A., Neal, D. E., Hall, R., & Harris, A. L. (1989) · PubMed · Cited by 101
Veillette, A., Bolen, J. B., & Bookman, M. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.10.4441 · Cited by 101
Currier, M. G., Lee, S., Stobart, C. C., Hotard, A. L., Villenave, R., Meng, J., Pretto, C. D., Shields, M. D., Nguyen, M. T., Todd, S. O., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005622 · Cited by 107
Gullick, W. J., Downward, J., & Waterfield, M. D. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04016.x · Cited by 100
Self-citationCancer Cell Motility—On the Road from c-erbB-2 Receptor Steered Signaling to Actin Reorganization
Feldner, J., & Brandt, B. (2002) · Experimental Cell Research · doi:10.1006/excr.2001.5385 · Cited by 99
Phosphorylation of Cell Surface Receptors: A Mechanism for Regulating Signal Transduction Pathways
Sibley, D. R., Benovic, J., Caron, M. G., & Lefkowitz, R. J. (1988) · Endocrine Reviews · doi:10.1210/edrv-9-1-38 · Cited by 99
Morandell, S., Stasyk, T., Skvortsov, S., Ascher, S., & Huber, L. A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800204 · Cited by 102
Davis, R. J., & Czech, M. P. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4080 · Cited by 97
Jones, N., & Dumont, D. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80458-8 · Cited by 97
Lewis, R. E., Wu, G. P., MacDonald, R. G., & Czech, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40141-5 · Cited by 97
Soler, C., Beguinot, L., & Carpenter, G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32718-7 · Cited by 97
Livneh, E., Benveniste, M., Prywes, R., Felder, S., Kam, Z., & Schlessinger, J. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.2.327 · Cited by 97
Vega, Q. C., Cochet, C., Filhol, O., Chang, C.-P., Rhee, S. G., & Gill, G. N. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.1.128 · Cited by 96
Bird, T. A., & Saklatvala, J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40221-4 · Cited by 95
Expression and activation of epidermal growth factor receptors in meningiomas
Carroll, R. S., Black, P. M., Zhang, J., Kirsch, M., Percec, I., Lau, N. C., & Guha, A. (1997) · Journal of neurosurgery · doi:10.3171/jns.1997.87.2.0315 · Cited by 93
Nair, V. D., & Sealfon, S. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303364200 · Cited by 93
Autophosphorylation: a salient feature of protein kinases
Smith, J. A., Francis, S. H., & Corbin, J. D. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076757 · Cited by 93
Martin-Fernandez, M. L., Clarke, D. T., Roberts, S. K., Zanetti-Domingues, L. C., & Gervasio, F. L. (2019) · Cells · doi:10.3390/cells8040316 · Cited by 96
Dasgupta, S., Soudry, E., Mukhopadhyay, N. D., Shao, C., Yee, J., Lam, S., Lam, W. L., Zhang, W. Y., Gazdar, A. F., Fisher, P. B., et al. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22980 · Cited by 92
Activation of the Purified Protein Tyrosine Kinase Domain of the Epidermal Growth Factor Receptor
Wedegaertner, P., & Gill, G. N. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60470-3 · Cited by 92
Cui, W., Zhang, S., Shan, C., Zhou, L., & Zhou, Z. (2013) · FEBS Journal · doi:10.1111/febs.12398 · Cited by 93
CSN6 controls the proliferation and metastasis of glioblastoma by CHIP-mediated degradation of EGFR
Hou, J., Deng, Q., Zhou, J., Zou, J.-X., Zhang, Y., Tan, P., Zhang, W., & Cui, H. (2016) · Oncogene · doi:10.1038/onc.2016.280 · Cited by 90
Lewis, R. E., Cao, L., Perregaux, D. G., & Czech, M. P. (1990) · Biochemistry · doi:10.1021/bi00459a020 · Cited by 90
Matsuda, N., Yokoyama, K., Takeshita, S., & Watanabe, M. (1998) · Archives of Oral Biology · doi:10.1016/s0003-9969(98)00079-x · Cited by 89
Heisermann, G. J., Wiley, H. S., Walsh, B. J., Ingraham, H. A., Fiol, C. J., & Gill, G. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38233-x · Cited by 89
Stoscheck, C. M., & King, L. E. (1986) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240310206 · Cited by 89
Wang, X.-Q., Sun, P., & Paller, A. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308818200 · Cited by 87
Albert, P. R., & Tashjian, A. H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39415-2 · Cited by 88
Pöhler, E., Mamaï, O., Hirst, J., Zamiri, M., Horn, H. M., Nomura, T., Irvine, A. D., Moran, B., Wilson, N. J., Smith, F. J. D., et al. (2012) · Nature Genetics · doi:10.1038/ng.2444 · Cited by 85
The EGFR variant III mutant as a target for immunotherapy of glioblastoma multiforme
Chistiakov, D. A., Chekhonin, I. V., & Chekhonin, V. P. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.05.064 · Cited by 88
Whiteley, B. J., & Glaser, L. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.4.1355 · Cited by 87
Expression of Epidermal Growth Factor Receptor in Carcinoma of the Cervix
Kim, J. W., Kim, Y. T., Kim, D. K., Song, C. H., & Lee, J. W. (1996) · Gynecologic Oncology · doi:10.1006/gyno.1996.0039 · Cited by 86
Targeting EGFR‐mediated autophagy as a potential strategy for cancer therapy
Sooro, M. A., Zhang, N., & Zhang, P. (2018) · International Journal of Cancer · doi:10.1002/ijc.31398 · Cited by 88
Optically Stable Biocompatible Flame-Made SiO2-Coated Y2O3:Tb3+ Nanophosphors for Cell Imaging
Sotiriou, G. A., Franco, D., Dimos Poulikakos, A., & Ferrari, A. (2012) · ACS Nano · doi:10.1021/nn205035p · Cited by 85
Carpentier, J. L., White, M. F., Orci, L., & Kahn, R. C. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.6.2751 · Cited by 85
Macdonald-Obermann, J. L., & PIKE, L. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001487 · Cited by 84
Mechanism of hydrogen peroxide-induced keratinocyte migration in a scratch-wound model
Loo, A. E. K., Ho, R., & Halliwell, B. B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.001 · Cited by 85
Morimatsu, M., Takagi, H., Ota, K., Iwamoto, R., Yanagida, T., & Sako, Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701330104 · Cited by 83
Ismail, R. S. M., Ismail, N. S. M., Abuserii, S., & Ella, D. A. A. E. (2016) · Future Journal of Pharmaceutical Sciences · doi:10.1016/j.fjps.2016.02.001 · Cited by 83
Metadata
- Authors
- Downward, J., Parker, P., & Waterfield, M. D.
- Venue
- Nature
- Published
- 1984-10
- Volume
- 311
- Issue
- 5985
- Pages
- 483-485
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2056681493
- Cited by
- 704
- References
- 22
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 5 · 2022: 11 · 2021: 14 · 2020: 9 · 2019: 9 · 2018: 11 · 2017: 16 · 2016: 15 · 2015: 13 · 2014: 17 · 2013: 18 · 2012: 15
- FWCI
- 22.58
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
- Keywords
- epidermal growth factor receptor, autophosphorylation, tyrosine kinase, autophosphorylation sites, avian erythroblastosis virus, receptor cytoplasmic domain, kinase activity, transforming protein
- MeSH terms
- Amino Acid Sequence, Epidermal Growth Factor, Humans, Phosphorylation, Receptors, Cell Surface, Tyrosine, 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