The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
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.
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
“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]
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-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
An enzymic method for the trace iodination of immunoglobulins and other proteins
Marchalonis, J. J. (1969) · Biochemical Journal · doi:10.1042/bj1130299 · Cited by 1,393
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
Carpenter, G., King, L. E., & Cohen, S. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30094-7 · Cited by 529
Haigler, H. T., McKanna, J. A., & Cohen, S. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.81.2.382 · Cited by 526
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
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
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 629
Synthetic Peptides of CD66a Stimulate Neutrophil Adhesion to Endothelial Cells
Skubitz, K. M., Campbell, K. D., & Skubitz, A. P. N. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4257 · Cited by 30
Modulation of a Mr 175,000 c-neu receptor isoform in G8/DHFR cells by serum starvation.
Epstein, R. J., Druker, B. J., Roberts, T. M., & Stiles, C. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)87010-7 · Cited by 30
Molecular prognostic markers in breast cancer
Dahiya, R., & Deng, G. (1998) · Breast Cancer Research and Treatment · doi:10.1023/a:1006101729631 · Cited by 30
Tsagianni, A., Mars, W. M., Bhushan, B., Bowen, W. C., Orr, A., Stoops, J., Paranjpe, S., Tseng, G. C., Liu, S., & Michalopoulos, G. K. (2018) · The American Journal of Pathology · doi:10.1016/j.ajpath.2018.06.009 · Cited by 29
H. pyloriselectively blocks EGFR endocytosis via the non-receptor kinase c-Abl and CagA
Bauer, B., Bartfeld, S., & Meyer, T. F. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01246.x · Cited by 29
CD95 tyrosine phosphorylation is required for CD95 oligomerization
Eberle, A., Reinehr, R., Becker, S., Keitel, V., & Häussinger, D. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0003-2 · Cited by 29
Wides, R. J., Zak, N. B., & Shilo, B. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15532.x · Cited by 29
Wang, D., Wang, B., Wang, R., Zhang, Z., Lin, Y., Huang, G., Lin, S., Jiang, Y., Wang, W., Wang, L., et al. (2017) · Oncology Letters · doi:10.3892/ol.2017.5827 · Cited by 28
Furuuchi, K., Berezov, A., Kumagai, T., & Greene, M. I. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.2.1021 · Cited by 28
Cao, H., Bangalore, L., Dompé, C., Bormann, B. J., & Stern, D. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)88728-8 · Cited by 28
Carraway, K. L., III, & Cerione, R. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80465-7 · Cited by 28
Kuppuswamy, D., Dalton, M., & PIKE, L. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46744-5 · Cited by 28
Single-molecule functional anatomy of endogenous HER2-HER3 heterodimers
Choi, B., Cha, M., Eun, G. S., Lee, D. H., Lee, S., Ehsan, M., Chae, P. S., Heo, W. D., Park, Y., & Yoon, T. (2020) · eLife · doi:10.7554/elife.53934 · Cited by 27
Khatabi, K. E., El-Mernissi, R., Moukhliss, Y., Hajji, H., Rehman, H. M., Yadav, R., Lakhlifi, T., Ajana, M. A., & Bouachrıne, M. (2022) · Chemical Data Collections · doi:10.1016/j.cdc.2022.100851 · Cited by 27
Lu, K., & Guidotti, G. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.5.679 · Cited by 27
Inhibition of epidermal growth factor receptor activity by retinoic acid in glioma cells
Steck, P. A., Hadi, A., Lotan, R., & Yung, W. K. A. (1990) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240420204 · Cited by 27
Diagnostic utility of oncogenes and their products in human cancer
McKenzie, S. J. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(91)90014-c · Cited by 27
Role of heterotrimeric G-proteins in epidermal growth factor signalling
Ramı́rez, I., Tebar, F., Grau, M., & Soley, M. (1995) · Cellular Signalling · doi:10.1016/0898-6568(95)00001-6 · Cited by 27
Alvarado, D., Rice, A. H., & Duffy, J. B. (2004) · Genetics · doi:10.1534/genetics.167.1.187 · Cited by 26
Hematopoietic growth factor receptors
Brizzi, M. F., Avanzi, G. C., & Pegoraro, L. (1991) · The International Journal Of Cell Cloning · doi:10.1002/stem.5530090404 · Cited by 26
Kinoshita, A., Takigawa, M., & Suzuki, F. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91601-l · Cited by 26
Lax, I., Bellot, F., Honegger, A., Schmidt, A., Ullrich, A., Givol, D., & Schlessinger, J. (1990) · Cell Regulation · doi:10.1091/mbc.1.2.173 · Cited by 26
Self-citationSharma, M., Basu, D. A., Nathany, S., Amrith, B. P., & Batra, U. (2022) · Cancer Research Statistics and Treatment · doi:10.4103/crst.crst_222_22 · Cited by 28
Live cell imaging shows hepatocyte growth factor-induced Met dimerization
Koschut, D., Richert, L., Pace, G., Niemann, H. H., Mély, Y., & Orian‐Rousseau, V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.015 · Cited by 25
A Pre-Clinical Assessment of the Pan-ERBB Inhibitor Dacomitinib in Pediatric and Adult Brain Tumors
Endersby, R., Whitehouse, J. P., Hii, H. L., Greenall, S. A., Johns, T. G., & Gottardo, N. G. (2018) · Neoplasia · doi:10.1016/j.neo.2018.02.004 · Cited by 25
Reconstitution of receptor/GTP-binding protein interactions
Cerione, R. A. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(91)90007-j · Cited by 25
Clark, S., Cheng, D. J., Hsuan, J. J., Haley, J. D., & Waterfield, M. D. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041340313 · Cited by 25
Ligand-independent dimerization of oncogenic v-erbB products involves covalent interactions
Adelsman, M. A., Huntley, B. K., & Maihle, N. J. (1996) · Journal of Virology · doi:10.1128/jvi.70.4.2533-2544.1996 · Cited by 25
Ye, Y., Huang, Z., Zhang, M., Li, J., Zhang, Y., & Lou, C. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114183 · Cited by 27
Román, J. V., Galán, M. Á., & del Valle, E. M. M. (2016) · Biomedical Physics & Engineering Express · doi:10.1088/2057-1976/2/3/035015 · Cited by 24
Kumagai, T., Katsumata, M., Hasegawa, A., Furuuchi, K., Funakoshi, T., Kawase, I., & Greene, M. I. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633546100 · Cited by 25
Inhibitory effect of a dimerization-arm-mimetic peptide on EGF receptor activation
Mizuguchi, T., Uchimura, H., Kakizawa, T., Kimura, T., Yokoyama, S., Kiso, Y., & Saito, K. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.080 · Cited by 23
Increased Expression of Epidermal Growth Factor-receptor in an Experimental Model of Colitis in Rats
P. Hoffmann, M. R. (2000) · Scandinavian Journal of Gastroenterology · doi:10.1080/003655200750056655 · Cited by 24
Signal transduction by the neu/ebrB-2 receptor: A potential target for anti-tumor therapy
Stancovski, I., Peles, E., Levy, R. B., Lemprecht, R., Kelman, Z., Goldman-Michael, R., Hurwitz, E., Bacus, S. S., Sela, M., & Yarden, Y. (1992) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(92)90192-l · Cited by 24
Self-citationXia, Z., Bergstrand, A., DePierre, J. W., & N�ssberger, L. (1999) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/(sici)1099-0461(1999)13:6 · Cited by 97
Miyamoto, M. R., Sugawa, H., Mori, T., Hase, K., Kuma, K., & Imura, H. (1988) · PubMed · Cited by 24
SYNTHESIS AND SAR STRATEGY OF THIAZOLIDINEDIONE: A NOVEL APPROACH FOR CANCER TREATMENT
Rashid, M., Shrivastava, N., & Husain, A. (2020) · Journal of the Chilean Chemical Society · doi:10.4067/s0717-97072020000204817 · Cited by 23
Rovira, X., Vivó, M., Serra, J. L. I., Roche, D., Strange, P., & Giraldo, J. (2008) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2008.00031.x · Cited by 23
Targeting H19 by lentivirus-mediated RNA interference increases A549 cell migration and invasion
Wang, L., Sun, Y., Yi, J., Wang, X., Liang, J., Pan, Z., Li, L., & Jiang, G. (2016) · Experimental Lung Research · doi:10.1080/01902148.2016.1223229 · Cited by 23
Dong, A., Kong, M., Ma, Z., Qian, J., Cheng, H., & Xu, X. N. (2008) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2008.00429.x · Cited by 23
Zidovetzki, R., Johnson, D. A., Arndt-Jovin, D. J., & Jovin, T. M. (1991) · Biochemistry · doi:10.1021/bi00239a012 · Cited by 23
Structural requirements for signal transduction of the insulin receptor
FLÖRKE, R., Klein, H. W., & Reinauer, H. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19146.x · Cited by 23
Suppression of EGFR Autophosphorylation by FKBP12
Mathea, S., Li, S., Schierhorn, A., Jahreis, G., & Schiene‐Fischer, C. (2011) · Biochemistry · doi:10.1021/bi2013855 · Cited by 20
Huang, C.-M., Chen, H., Chen, D.-C., Huang, Y.-C., Liu, S., Lin, Y.-J., Chang, Y., Lin, H.-W., Chen, S.-Y., & Tsai, F. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180604 · Cited by 22
Oligomeric states of the insulin receptor: binding and autophosphorylation properties
Kubar, J., & OBBERGHEN, E. V. (1989) · Biochemistry · doi:10.1021/bi00429a024 · Cited by 22
Koesling, D., Schultz, G., & Böhme, E. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80317-v · Cited by 22
Insulin binding changes the interface region between .alpha. subunits of the insulin receptor
Waugh, S. M., & Pilch, P. F. (1989) · Biochemistry · doi:10.1021/bi00432a053 · Cited by 22
Kiyokawa, N., Yan, D., Brown, M. E., & Hung, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1092 · Cited by 22
Kwatra, M. M., Bigner, D. D., & Cohn, J. A. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90042-a · Cited by 22
Molecular basis of VEGFR1 autoinhibition at the plasma membrane
Chakraborty, M. P., Das, D., Mondal, P., Kaul, P., Bhattacharyya, S., Das, P. K., & Das, R. (2024) · Nature Communications · doi:10.1038/s41467-024-45499-2 · Cited by 24
Sun, Q., Jackson, R. A., Ng, C., Guy, G. R., & Sivaraman, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012819 · Cited by 21
Windisch, D., Hoffmann, S., Afonin, S., Vollmer, S., Benamira, S., Langer, B., Bürck, J., Muhle‐Goll, C., & Ulrich, A. S. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.073 · Cited by 21
Ligand binding induces a conformational change in epidermal growth factor receptor dimers
Walker, F., Rothacker, J., Henderson, C. A., Nice, E. C., Catimel, B., Zhang, H., Scott, A. M., Bailey, M. F., Orchard, S. G., Adams, T. E., et al. (2012) · Growth Factors · doi:10.3109/08977194.2012.739619 · Cited by 21
Waters, C. M., Overholser, K. A., Sorkin, A. D., & Carpenter, G. F. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041520206 · Cited by 21
Epidermal growth factor reduces HER‐2 protein level in human ovarian carcinoma cells
Marth, C., Lang, T., Cronauer, M. V., Doppler, W., Zeimet, A. G., Bachmair, F., Ullrich, A., & Daxenbichler, G. (1992) · International Journal of Cancer · doi:10.1002/ijc.2910520226 · Cited by 21
Oncogenes, Protein Tyrosine Kinases, and Signal Transduction
Liu, D., & Wang, L. (1994) · Journal of Biomedical Science · doi:10.1007/bf02257980 · Cited by 21
Roy, L. M., Gittinger, C. K., & Landreth, G. E. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041460109 · Cited by 21
Needham, S. R., Zanetti-Domingues, L. C., Hirsch, M., Rolfe, D. J., Tynan, C. J., Roberts, S. K., Martin-Fernandez, M. L., & Clarke, D. T. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130236 · Cited by 20
Zhang, D., Ma, F., Zhang, Q., & Zhang, C. (2017) · Chemical Communications · doi:10.1039/c7cc06823a · Cited by 20
Epidermal Growth Factor-Induced GnRH-II Synthesis Contributes to Ovarian Cancer Cell Invasion
Poon, S. L., Hammond, G. T., & Leung, P. C. K. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0147 · Cited by 20
Samal, B. B., Arakawa, T., Boone, T. C., Jones, T. H. D., Prestrelski, S. J., Narhi, L. O., Wen, J., Stearns, G., Crandall, C. A., Pope, J. A., et al. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)00172-y · Cited by 20
Mizuguchi, T., Ohara, N., Iida, M., Ninomiya, R., Wada, S., Kiso, Y., Saito, K., & Akaji, K. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.08.013 · Cited by 20
Chen, Z., Wang, T., Tu, X., Xie, W., He, H., Wang, M., & Zhang, J. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.03.094 · Cited by 20
Tyrosine kinase signal transduction in rheumatoid synovitis
Williams, W. V., VonFeldt, J. M., Ramanujam, T., & Weiner, D. B. (1992) · Seminars in Arthritis and Rheumatism · doi:10.1016/0049-0172(92)90025-9 · Cited by 20
EGF Family Receptors and Their Ligands in Human Cancer
Tang, C. K., & Lippman, M. E. (1998) · Elsevier eBooks · doi:10.1016/b978-012312411-1/50006-8 · Cited by 20
Growth factors in the gastrointestinal tract.
Lemoine, N. R., Leung, H. Y., & Gullick, W. J. (1992) · Gut · doi:10.1136/gut.33.10.1297 · Cited by 20
Proteolytic generation of constitutive tyrosine kinase activity of the human insulin receptor
Hsuan, J. J., Downward, J., Clark, S., & Waterfield, M. D. (1989) · Biochemical Journal · doi:10.1042/bj2590519 · Cited by 20
Lichtner, R. B., Wiedemuth, M., Kittmann, A., Ullrich, A., Schirrmacher, V., & Khazaie, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49779-2 · Cited by 20
Mechanism of kinase activation in the receptor for colony-stimulating factor 1.
Lee, A. W., & Nienhuis, A. W. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7270 · Cited by 20
van der Heyden, M. A. G., Nievers, M. G., Verkleij, A. J., Boonstra, J., & Henegouwen, P. M. P. V. B. E. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00599-1 · Cited by 20
Yaseen, Y. S., Kubba, A., Shihab, W. A., & Tahtamouni, L. H. (2022) · Pharmacia · doi:10.3897/pharmacia.69.e86504 · Cited by 19
Tang, G., Wang, W., Wang, X., Ding, K., Ngan, S. C., Chen, J.-Y., Sze, S. K., Gao, L., Yuan, P., Lu, X., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115671 · Cited by 20
Carraway, K. L., Koland, J. G., & Cerione, R. A. (1990) · Biochemistry · doi:10.1021/bi00489a034 · Cited by 19
Beech, J. A. (1997) · Bioelectromagnetics · doi:10.1002/(sici)1521-186x(1997)18:5 · Cited by 19
Carlin, C. R., Phillips, P. D., Brooks-Frederich, K. M., Knowles, B. B., & Cristofalo, V. J. (1994) · Journal of Cellular Physiology · doi:10.1002/jcp.1041600305 · Cited by 19
Johansson, S., Andersson, N., & Andersson, G. N. (1990) · Hepatology · doi:10.1002/hep.1840120314 · Cited by 19
Dynamic Protein Allosteric Regulation and Disease
Nussinov, R., Tsai, C.-J., & Jang, H. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-13-8719-7_2 · Cited by 18
Jersey steer ruminal papillae histology and nutrigenomics with diet changes
Novak, T. E., Rodriguez‐Zas, S. L., Southey, B. R., Starkey, J. D., Stockler, R. M., Alfaro, G. F., & Moisá, S. J. (2019) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.13189 · Cited by 18
Drug targets for tumorigenesis: Insights from structural analysis of EGFR signaling network
Tekir, S. D., Arğa, K. Y., & Ülgen, K. Ö. (2008) · Journal of Biomedical Informatics · doi:10.1016/j.jbi.2008.08.008 · Cited by 18
Tollefsen, S. E., Stoszek, R. M., & Thompson, K. (1991) · Biochemistry · doi:10.1021/bi00215a008 · Cited by 18
Computational Study of the Binding Mode of Epidermal Growth Factor Receptor Kinase Inhibitors
Chen, H. (2008) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2008.00656.x · Cited by 18
Targeting gallbladder cancer: a pathway based perspective
Baichan, P., Naicker, P., Devar, J., Smith, M., Candy, G. P., & Nweke, E. E. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05269-x · Cited by 17
Wåhlén, E., Olsson, F. K. S., Raykova, D., Söderberg, O., Heldin, J., & Lennartsson, J. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.099 · Cited by 17
Receptor tyrosine kinases (RTKs)
Batool, Z., Azfal, A., Liaquat, L., Sadir, S., Nisar, R., Inamullah, A., Ghalib, A. U. F., & Haider, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18677-6.00012-9 · Cited by 17
Banerjee, K., Das, S., Sarkar, A., Chatterjee, M., Biswas, J., & Choudhuri, S. K. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.08.056 · Cited by 17
Oksvold, M. P., Thien, C. B. F., Widerberg, J., Chantry, A., Huitfeldt, H. S., & Langdon, W. Y. (2004) · Radiation Research · doi:10.1667/rr3185 · Cited by 17
A new temperature-dependent strategy to modulate the epidermal growth factor receptor
Li, Z., Tyrpak, D. R., Park, M.-C., Okamoto, C. T., & MacKay, J. A. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.07.063 · Cited by 17
The Role of Schwann Cell in Nerve Regeneration
Verdú, E., & Navarro, X. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5737-1_17 · Cited by 17
Kinetic characterization of atrial natriuretic factor-sensitive particulate guanylate cyclase
Ivanova, K., Heim, J.-M., & Gerzer, R. (1990) · European Journal of Pharmacology Molecular Pharmacology · doi:10.1016/0922-4106(90)90125-h · Cited by 17
Eaton, C. L., Davies, P. J., Harper, M. E., France, T., Rushmere, N. K., & Griffiths, K. (1991) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(91)90180-d · Cited by 17
Gonzalez-Magaldi, M., Gullapalli, A., Papoulas, O., Liu, C., Leung, A. Y.-H., Guo, L., Brilot, A. F., Marcotte, E. M., Ke, Z., & Leahy, D. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424678122 · Cited by 17
The Tethering Arm of the EGF Receptor Is Required for Negative Cooperativity and Signal Transduction
Adak, S., DeAndrade, D. S., & PIKE, L. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182899 · Cited by 16
Negative co-operativity in the EGF receptor
PIKE, L. J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110610 · Cited by 16
Cui, X., Su, L., Li, T., Pang, X., Zhang, S., Jin, J., Hu, J., Liu, C., Yang, L., Peng, H., et al. (2014) · PubMed Central · Cited by 16
Russo, A. J. (2015) · Biomarker Insights · doi:10.4137/bmi.s21946 · Cited by 15
Sheth, P. R., Hays, J. L., Elferink, L. A., & Watowich, S. J. (2008) · Biochemistry · doi:10.1021/bi701892f · Cited by 16
The Role of Molecular Diagnostics in Cancer Diagnosis and Treatment
Ozretić, L., Heukamp, L. C., Odenthal, M., & Buettner, R. (2012) · Onkologie · doi:10.1159/000334823 · Cited by 16
Conjugate Chemistry and Cellular Processing of EGF-Dextran
Carlsson, E. B. J. (1999) · Acta Oncologica · doi:10.1080/028418699431384 · Cited by 16
Antibody-induced mitogenicity mediated by a chimeric CD2-c-fms receptor.
Roussel, M. F., Transy, C., Kato, J., Reinherz, E. L., & Sherr, C. J. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2407 · Cited by 16
Signal transduction processes leading to acrosomal exocytosis in mammalian spermatozoa
Kopf, G. S., & Wilde, M. W. (1990) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(90)90085-h · Cited by 16
Metadata
- 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