The epidermal growth factor receptor ligands at a glance
Abstract
The epidermal growth factor receptor (EGFR) regulates key processes of cell biology, including proliferation, survival, and differentiation during development, tissue homeostasis, and tumorigenesis. Canonical EGFR activation involves the binding of seven peptide growth factors. These ligands are synthesized as transmembrane proteins comprising an N‐terminal extension, the EGF module, a short juxtamembrane stalk, a hydrophobic transmembrane domain, and a carboxy‐terminal fragment. The central structural and functional feature is the EGF module, a sequence containing six cysteines in a conserved spacement which is responsible for binding to the EGFR. While the membrane‐anchored peptide can be biologically active by juxtacrine signaling, in most cases the EGF module is proteolytically cleaved (a process termed ectodomain shedding) to release the soluble growth factor, which may act in an endocrine, paracrine, or autocrine fashion. This review summarizes the structural and functional properties of these fascinating molecules and presents selected examples to illustrate their roles in development, physiology, and pathology. J. Cell. Physiol. 218: 460–466, 2009. © 2008 Wiley‐Liss, Inc.
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Human recombinant HB-EGF consists of amino acids 1-148 of pro-HB-EGF, a membrane-spanning protein that sheds its ectodomain to release a soluble EGF-like domain that binds EGFR.
“Human recombinant HB-EGF is encoded by amino acids 1–148 of pro-HB-EGF which is a membrane spanning protein that undergoes ectodomain shedding, releasing a soluble extracellular portion that contains an EGF-like domain that binds the EGFR”
From HB-EGF is Necessary and Sufficient for Müller Glia Dedifferentiation and Retina Regeneration (2012) · cites this paper as Schneider and Wolf, 2009
Cites
Genes that mediate breast cancer metastasis to lung
Minn, A. J., Gupta, G. P., Siegel, P. M., Bos, P. D., Shu, W., Giri, D. D., Viale, A., Olshen, A. B., Gerald, W. L., & Massagué, J. (2005) · Nature · doi:10.1038/nature03799 · Cited by 2,922 · see citing works
EGF–ERBB signalling: towards the systems level
Citri, A., & Yarden, Y. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1962 · Cited by 2,004 · see citing works
An Essential Role for Ectodomain Shedding in Mammalian Development
Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,606 · see citing works
Prenzel, N., Zwick, E., Daub, H., Leserer, M., Abraham, R., Wallasch, C., & Ullrich, A. (1999) · Nature · doi:10.1038/47260 · Cited by 1,507 · see citing works
Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
Daub, H., Weiß, F. U., Wallasch, C., & Ullrich, A. (1996) · Nature · doi:10.1038/379557a0 · Cited by 1,476 · see citing works
Targeted Disruption of Mouse EGF receptor: Effect of Genetic Background on Mutant Phenotype
Threadgill, D. W., Dlugosz, A. A., Hansen, L. A., Tennenbaum, T., Lichti, U. F., Yee, D., LaMantia, C., Mourton, T., Herrup, K., Harris, R. C., et al. (1995) · Science · doi:10.1126/science.7618084 · Cited by 1,460 · see citing works
Neuregulins: functions, forms, and signaling strategies
Falls, D. L. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00102-7 · Cited by 1,071 · see citing works
EGF-Like Growth Factors As Mediators of LH Action in the Ovulatory Follicle
Park, J.-Y., Su, Y., Ariga, M., Law, E. C., Jin, S.-L. C., & Conti, M. (2004) · Science · doi:10.1126/science.1092463 · Cited by 1,047 · see citing works
Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor
Miettinen, P. J., Berger, J. E., Meneses, J. J., Phung, Y. T., Pedersen, R. A., Werb, Z., & Derynck, R. (1995) · Nature · doi:10.1038/376337a0 · Cited by 1,038 · see citing works
Strain-Dependent Epithelial Defects in Mice Lacking the EGF Receptor
Sibilia, M., & Wagner, E. F. (1995) · Science · doi:10.1126/science.7618085 · Cited by 1,002 · see citing works
Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
Şahin, U., Weskamp, G., Kelly, K., Zhou, H., Higashiyama, S., Peschon, J. J., Hartmann, D., Säftig, P., & Blobel, C. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307137 · Cited by 979 · see citing works
Harris, R. C. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00105-2 · Cited by 786 · see citing works
Sandgren, E. P., Luetteke, N., Palmiter, R. D., Brinster, R. L., & Lee, D. C. (1990) · Cell · doi:10.1016/0092-8674(90)90075-p · Cited by 752 · see citing works
Jhappan, C., Stahle, C., Harkins, R. N., Fausto, N., Smith, G. H., & Merlino, G. T. (1990) · Cell · doi:10.1016/0092-8674(90)90076-q · Cited by 709 · see citing works
Insect cell-expressed p180erbB3 possesses an impaired tyrosine kinase activity.
Guy, P. M., Platko, J. V., Cantley, L. C., Cerione, R. A., & Carraway, K. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8132 · Cited by 698 · see citing works
MEMBRANE-ANCHORED GROWTH FACTORS
Massagué, J., & Pandiella, A. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002503 · Cited by 666 · see citing works
TGFα deficiency results in hair follicle and eye abnormalities in targeted and waved-1 mice
Luetteke, N., Qiu, T. H., Peiffer, R. L., Oliver, P. M., Smithies, O., & Lee, D. C. (1993) · Cell · doi:10.1016/0092-8674(93)90228-i · Cited by 658 · see citing works
ErbB Receptors: Directing Key Signaling Networks Throughout Life
Holbro, T., & Hynes, N. E. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121440 · Cited by 642 · see citing works
The deaf and the dumb: the biology of ErbB-2 and ErbB-3
Citri, A. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00101-5 · Cited by 591 · see citing works
Mann, G. B., Fowler, K. J., Gabriel, A., Nice, E. C., Williams, R. L., & Dunn, A. R. (1993) · Cell · doi:10.1016/0092-8674(93)90227-h · Cited by 583 · see citing works
Das, S., Wang, X., Paria, B. C., Damm, D. L., Abraham, J. A., Klagsbrun, M., Andrews, G. K., & Dey, S. K. (1994) · Development · doi:10.1242/dev.120.5.1071 · Cited by 568 · see citing works
Luetteke, N., Qiu, T. H., Fenton, S. E., Troyer, K. L., Riedel, R. F., Chang, A. Y., & Lee, D. C. (1999) · Development · doi:10.1242/dev.126.12.2739 · Cited by 568 · see citing works
Wong, S. T., Winchell, L. F., McCune, B. K., Earp, H. S., Teixidó, J., Massagué, J., Herman, B., & Lee, D. C. (1989) · Cell · doi:10.1016/0092-8674(89)90252-3 · Cited by 475 · see citing works
Klapper, L. N., Glathe, S., Vaisman, N., Hynes, N. E., Andrews, G. C., Sela, M., & Yarden, Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4995 · Cited by 455 · see citing works
The Epidermal Growth Factor Receptor System in Skin Repair and Inflammation
Pastore, S., Mascia, F., Mariani, V., & Girolomoni, G. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5701184 · Cited by 441 · see citing works
Development of mammary hyperplasia and neoplasia in MMTV-TGFα transgenic mice
Matsui, Y., Halter, S. A., Holt, J. T., Hogan, B. L. M., & Coffey, R. J. (1990) · Cell · doi:10.1016/0092-8674(90)90077-r · Cited by 440 · see citing works
Transmembrane TGF-α precursors activate EGF/TGF-α receptors
Brachmann, R. K., Lindquist, P. B., Nagashima, M., Kohr, W. J., Lipari, T., Napier, M. A., & Derynck, R. (1989) · Cell · doi:10.1016/0092-8674(89)90591-6 · Cited by 422 · see citing works
Defective valvulogenesis in HB‐EGF and TACE‐null mice is associated with aberrant BMP signaling
Jackson, L. F., Qiu, T. H., Sunnarborg, S. W., Chang, A., Zhang, C., Patterson, C., & Lee, D. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg264 · Cited by 417 · see citing works
EGFR signal transactivation in cancer cells
Fischer, O. M., Hart, S., Gschwind, A., & Ullrich, A. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311203 · Cited by 412 · see citing works
Vassar, R. J., & Fuchs, E. V. (1991) · Genes & Development · doi:10.1101/gad.5.5.714 · Cited by 411 · see citing works
Autocrine, paracrine and juxtacrine signaling by EGFR ligands
Singh, A. B., & Harris, R. C. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.026 · Cited by 400 · see citing works
Role of the Epidermal Growth Factor Network in Ovarian Follicles
Conti, M., Hsieh, M., Park, J.-Y., & Su, Y. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0185 · Cited by 370 · see citing works
Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia
Groenestege, W. M. T., Thébault, S. C., van der Wijst, J., van den Berg, D. J., Janssen, R., Tejpar, S., van den Heuvel, L. P., Cutsem, E. V., Hoenderop, J. G. J., Knoers, N. V. A. M., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31680 · Cited by 355 · see citing works
Paria, B. C., Ma, W., Tan, J., Raja, S., Das, S. K., Dey, S. K., & Hogan, B. L. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1047 · Cited by 352 · see citing works
Heparin-binding EGF-like growth factor and ErbB signaling is essential for heart function
Iwamoto, R., Yamazaki, S., Asakura, M., Takashima, S., Hasuwa, H., Miyado, K., Adachi, S., Kitakaze, M., Hashimoto, K., Raab, G., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0537588100 · Cited by 341 · see citing works
Hsieh, M., Lee, D., Panigone, S., Horner, K., Chen, R., Theologis, A. A., Lee, D. C., Threadgill, D. W., & Conti, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01919-06 · Cited by 329 · see citing works
Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases
Waterman, H., & Yarden, Y. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02117-2 · Cited by 315 · see citing works
EGF‐like domains in extracellular matrix proteins: Localized signals for growth and differentiation?
Engel, J. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81417-6 · Cited by 305 · see citing works
Tokumaru, S., Higashiyama, S., Endo, T., Nakagawa, T., Miyagawa, J., Yamamori, K., Hanakawa, Y., Ohmoto, H., Yoshino, K., Shirakata, Y., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.2.209 · Cited by 305 · see citing works
Heparin-binding EGF-like growth factor accelerates keratinocyte migration and skin wound healing
Shirakata, Y., Kimura, R., Nanba, D., Iwamoto, R., Tokumaru, S., Morimoto, C., Yokota, K., Nakamura, M., Sayama, K., Mekada, E., et al. (2005) · Journal of Cell Science · doi:10.1242/jcs.02346 · Cited by 301 · see citing works
Mice mutant for Egfr and Shp2 have defective cardiac semilunar valvulogenesis
Chen, B., Bronson, R. T., Klaman, L. D., Hampton, T., Wang, J., Green, P. J., Magnuson, T., Douglas, P. S., Morgan, J. P., & Neel, B. G. (2000) · Nature Genetics · doi:10.1038/73528 · Cited by 300 · see citing works
Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor
Swindle, C. S., Tran, K. T., Johnson, T. D., Banerjee, P., Mayes, A. M., Griffith, L., & Wells, A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103103 · Cited by 286 · see citing works
Dong, J., Opresko, L. K., Dempsey, P. J., Lauffenburger, D. A., Coffey, R. J., & Wiley, H. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6235 · Cited by 263 · see citing works
Anklesaria, P., Teixidó, J., Laiho, M., Pierce, J. H., Greenberger, J. S., & Massagué, J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3289 · Cited by 252 · see citing works
Targeting TACE-dependent EGFR ligand shedding in breast cancer
Kenny, P. A., & Bissell, M. J. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29518 · Cited by 248 · see citing works
Transgenic expression of the human amphiregulin gene induces a psoriasis-like phenotype.
Cook, P. W., Piepkorn, M. W., Clegg, C. H., Plowman, G. D., DeMay, J. M., Brown, J. R., & Pittelkow, M. R. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119766 · Cited by 225 · see citing works
Dempsey, P. J., Goldenring, J. R., Soroka, C. J., Modlin, I. M., McClure, R. W., Lind, C. D., Ahlquist, D. A., Pittelkow, M. R., Lee, D. C., Sandgren, E. P., et al. (1992) · Gastroenterology · doi:10.1016/0016-5085(92)91455-d · Cited by 220 · see citing works
Structure-Function relationships for the EGF/TGF-α family of mitogens
Groenen, L. C., Nice, E. C., & Burgess, A. W. (1994) · Growth Factors · doi:10.3109/08977199409010997 · Cited by 218 · see citing works
Membrane‐anchored growth factors, the epidermal growth factor family: Beyond receptor ligands
Higashiyama, S., Iwabuki, H., Morimoto, C., Hieda, M., Inoue, H., & Matsushita, N. (2008) · Cancer Science · doi:10.1111/j.1349-7006.2007.00676.x · Cited by 213 · see citing works
Amphiregulin: An early trigger of liver regeneration in mice
Berasain, C., García–Trevijano, E. R., Castillo, J., Erroba, E., Lee, D. C., Prìeto, J., & Avila, M. A. (2005) · Gastroenterology · doi:10.1053/j.gastro.2004.11.006 · Cited by 213 · see citing works
SnapShot: EGFR Signaling Pathway
Yarden, Y., & Shilo, B. (2007) · Cell · doi:10.1016/j.cell.2007.11.013 · Cited by 203 · see citing works
The many faces of epidermal growth factor repeats.
Cg, D. (1990) · PubMed · Cited by 199 · see citing works
Ibbotson, K. J., HARROD, J., Gowen, M., D'Souza, S. M., Smith, D. D., Winkler, M. E., Derynck, R., & Mundy, G. R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.7.2228 · Cited by 179 · see citing works
Cloning and Biological Activity of Epigen, a Novel Member of the Epidermal Growth Factor Superfamily
Strachan, L., Murison, J. G., Prestidge, R. L., Sleeman, M. A., Watson, J. D., & Kumble, K. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006935200 · Cited by 171 · see citing works
Human transforming growth factor-alpha stimulates bone resorption in vitro.
Stern, P. H., Krieger, N. S., Nissenson, R. A., Williams, R. D., Winkler, M. E., Derynck, R., & Strewler, G. J. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112202 · Cited by 168 · see citing works
Schneider, M. R., Werner, S., Paus, R., & Wolf, E. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070942 · Cited by 161 · see citing works
Self-citationQin, L., Qiu, P., Wang, L., Li, X., Swarthout, J. T., Soteropoulos, P., Tolias, P. P., & Partridge, N. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212226200 · Cited by 161 · see citing works
Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF
Nanba, D., Mammoto, A., Hashimoto, K., & Higashiyama, S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303017 · Cited by 158 · see citing works
Am, D., Wang, X., King, L. E., Nanney, L., Ta, G., Sellheyer, K., Bundman, D. S., Longley, M., Rothnagel, J. A., & Da, G. (1993) · PubMed · Cited by 153 · see citing works
Hinkle, C. L., Sunnarborg, S. W., Loiselle, D. R., Parker, C. E., Stevenson, M. C., Russell, W. E., & Lee, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312141200 · Cited by 153 · see citing works
Fernández-Larrea, J., Merlos‐Suárez, A., Ureña, J. M., Baselga, J. M., & Arribas, J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80470-0 · Cited by 151 · see citing works
Mice with defects in HB-EGF ectodomain shedding show severe developmental abnormalities
Yamazaki, S., Iwamoto, R., Saeki, K., Asakura, M., Takashima, S., Yamazaki, A., Kimura, R., Mizushima, H., Moribe, H., Higashiyama, S., et al. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200307035 · Cited by 145 · see citing works
Takagi, H., Jhappan, C., Sharp, R., & Merlino, G. T. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115936 · Cited by 141 · see citing works
Maternal heparin-binding-EGF deficiency limits pregnancy success in mice
Xie, H., Wang, H., Tranguch, S. L., Iwamoto, R., Mekada, E., DeMayo, F. J., Lydon, J. P., Das, S. K., & Dey, S. K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707909104 · Cited by 129 · see citing works
Mice humanised for the EGF receptor display hypomorphic phenotypes in skin, bone and heart
Sibilia, M. C., Wagner, B., Hoebertz, A., Elliott, C., Marino, S., Jochum, W., & Wagner, E. F. (2003) · Development · doi:10.1242/dev.00664 · Cited by 129 · see citing works
Ménétrier disease and gastrointestinal stromal tumors: hyperproliferative disorders of the stomach
Coffey, R. J., Washington, M. K., Corless, C. L., & Heinrich, M. C. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30491 · Cited by 126 · see citing works
Zhao, J., Chen, H., Peschon, J. J., Shi, W., Zhang, Y., Frank, S. J., & Warburton, D. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0176 · Cited by 121 · see citing works
Takahashi, N., MacDonald, B. R., Hon, J. K., Winkler, M., Derynck, R., Mundy, G. R., & Roodman, G. D. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112677 · Cited by 120 · see citing works
Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network
Tzahar, E., Moyer, J. D., Waterman, H., Barbacci, E. G., Bao, J., Levkowitz, G., Shelly, M., Strano, S., Pinkas‐Kramarski, R., Pierce, J. H., et al. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.5948 · Cited by 116 · see citing works
TACE is required for fetal murine cardiac development and modeling
Shi, W., Chen, H., Sun, J., Buckley, S., Zhao, J., Anderson, K. D., Williams, R. G., & Warburton, D. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00315-4 · Cited by 115 · see citing works
Lee, D., Pearsall, R. S., Das, S., Dey, S. K., Godfrey, V., & Threadgill, D. W. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8907-8916.2004 · Cited by 115 · see citing works
Selective Inhibition of Type I Collagen Synthesis in Osteoblastic Cells by Epidermal Growth Factor*
Hata, R., Hori, H., Nagai, Y., Tanaka, S., Kondo, M., Hiramatsu, M., Utsumi, N., & Kumegawa, M. (1984) · Endocrinology · doi:10.1210/endo-115-3-867 · Cited by 115 · see citing works
Zhu, J., Jia, X., Xiao, G., Kang, Y., Partridge, N. C., & Qin, L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705064200 · Cited by 108 · see citing works
Merchant, N. B., Voskresensky, I. V., Rogers, C. M., LaFleur, B., Dempsey, P. J., Graves‐Deal, R., Revetta, F. L., Foutch, A. C., Rothenberg, M. L., Washington, M. K., et al. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1216 · Cited by 107 · see citing works
Qin, L., Tamasi, J. A., Raggatt, L. J., Li, X., Feyen, J. H. M., Lee, D. C., DiCicco-Bloom, E. M., & Partridge, N. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409807200 · Cited by 104 · see citing works
Kochupurakkal, B. S., Harari, D., Segni, A. D., Maik-Rachline, G., Lyass, L., Gur, G., Kerber, G., Citri, A., Lavi, S., Eilam, R., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413919200 · Cited by 103 · see citing works
Normanno, N., Luca, A. D., Aldinucci, D., Maiello, M. R., Mancino, M., D’Antonio, A., Filippi, R. D., & Pinto, A. (2005) · Endocrine Related Cancer · doi:10.1677/erc.1.00956 · Cited by 98 · see citing works
Cook, P. W., Brown, J. R., Cornell, K., & Pittelkow, M. R. (2004) · Experimental Dermatology · doi:10.1111/j.0906-6705.2004.00183.x · Cited by 96 · see citing works
Shirasawa, S., Sugiyama, S., Baba, I., Inokuchi, J., Sekine, S., Ogino, K., Kawamura, Y. I., Dohi, T., Fujimoto, M., & Sasazuki, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404217101 · Cited by 95 · see citing works
Effects of epidermal growth factor on osteoblastic cellsin vitro
Kumegawa, M., Hiramatsu, M., HATAKEYAMA, K., Yajima, T., Kodama, H., Osaki, T., & Kurisu, K. (1983) · Calcified Tissue International · doi:10.1007/bf02405091 · Cited by 89 · see citing works
Evolutionary Analysis of the ErbB Receptor and Ligand Families
Stein, R. A., & Staros, J. V. (2000) · Journal of Molecular Evolution · doi:10.1007/s002390010043 · Cited by 88 · see citing works
Overexpression of Epidermal Growth Factor Induced Hypospermatogenesis in Transgenic Mice
Wong, R. W.-C., Kwan, R. W.-P., Mak, P. H. S., Mak, K. K., Sham, M. H., & Chan, S. Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001965200 · Cited by 86 · see citing works
Membrane-anchored growth factor, HB-EGF, on the cell surface targeted to the inner nuclear membrane
Hieda, M., Isokane, M., Koizumi, M., Higashi, C., Tachibana, T., Shudou, M., Taguchi, T., Hieda, Y., & Higashiyama, S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200710022 · Cited by 76 · see citing works
Expression of Epidermal Growth Factor in Transgenic Mice Causes Growth Retardation
Chan, S. Y., & Wong, R. W.-C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004189200 · Cited by 73 · see citing works
Stimulation of DNA synthesis by epidermal growth factor in osteoblast-like cells
Ng, K. W., Partridge, N. C., Niall, M., & Martin, T. J. (1983) · Calcified Tissue International · doi:10.1007/bf02405105 · Cited by 71 · see citing works
Ma, Y. J., Dissen, G. A., Merlino, G. T., Coquelin, A., & Ojeda, S. R. (1994) · Endocrinology · doi:10.1210/endo.135.4.7925101 · Cited by 69 · see citing works
G-protein-coupled receptor signaling and the EGF network in endocrine systems
Hsieh, M., & Conti, M. (2005) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2005.07.005 · Cited by 68 · see citing works
Insights into the evolution of the ErbB receptor family and their ligands from sequence analysis.
Stein, R. A., & Staros, J. V. (2006) · BMC Evolutionary Biology · doi:10.1186/1471-2148-6-79 · Cited by 65 · see citing works
Schneider, M. R., Dahlhoff, M., Herbach, N., Renner‐Müller, I., Dalke, C., Puk, O., Graw, J., Wanke, R., & Wolf, E. (2005) · Endocrinology · doi:10.1210/en.2005-0418 · Cited by 60 · see citing works
Self-citationThe Carboxyl-terminal Fragment of Pro-HB-EGF Reverses Bcl6-mediated Gene Repression
Kinugasa, Y., Hieda, M., Hori, M., & Higashiyama, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611036200 · Cited by 56 · see citing works
Lorenzo, J. A., Quinton, J., Sousa, S., & Raisz, L. G. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112517 · Cited by 51 · see citing works
The EGF domain: Requirements for binding to receptors of the ErbB family
van Zoelen, E. J. J., Stortelers, C., Lenferink, A. E. G., & van de Poll, M. L. M. (2000) · Vitamins and hormones · doi:10.1016/s0083-6729(00)59005-0 · Cited by 46 · see citing works
Dempsey, P. J., Meise, K. S., & Coffey, R. J. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00035-1 · Cited by 44 · see citing works
Schneider, M. R., & Wolf, E. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.003 · Cited by 43 · see citing works
Self-citationBrown, C. L., Coffey, R. J., & Dempsey, P. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102114200 · Cited by 39 · see citing works
Jhappan, C., Takayama, H., Dickson, R. B., & Merlino, G. T. (1994) · PubMed · Cited by 37 · see citing works
Gratão, A. A., Dahlhoff, M., Sinowatz, F., Wolf, E., & Schneider, M. R. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.062588 · Cited by 27 · see citing works
Self-citationAlterations of the p16INK4A gene in human ovarian cancers
Kanuma, T., Nishida, J., Gima, T., Barrett, J. C., & Wake, N. (1997) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199703)18:3 · Cited by 19 · see citing works
Negative Constraints Underlie the ErbB Specificity of Epidermal Growth Factor-like Ligands
van der Woning, S. P., van Rotterdam, W., Nabuurs, S. B., Venselaar, H., Jacobs-Oomen, S., Wingens, M., Vriend, G., Stortelers, C., & van Zoelen, E. J. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603168200 · Cited by 8 · see citing works
Pyka, J., Głogowska, A., Dralle, H., Hoang‐Vu, C., & Klonisch, T. C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-2030 · Cited by 6 · see citing works
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The HCV Life Cycle: In vitro Tissue Culture Systems and Therapeutic Targets
Gerold, G., & Pietschmann, T. (2014) · Digestive Diseases · doi:10.1159/000360830 · Cited by 4,854 · see citing works
Lupberger, J., Zeisel, M., Xiao, F., Thumann, C., Fofana, I., Zona, L., Davis, C., Mee, C., Turek, M., Gorke, S., et al. (2011) · Nature Medicine · doi:10.1038/nm.2341 · Cited by 743 · see citing works
Epidermal growth factor receptor in relation to tumor development: EGFR gene and cancer
Mitsudomi, T., & Yatabe, Y. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07448.x · Cited by 560 · see citing works
Wang, G.-X., Zhao, X.-Y., Meng, Z., Kern, M., Dietrich, A., Chen, Z., Cozacov, Z., Zhou, D., Okunade, A. L., Su, X., et al. (2014) · Nature Medicine · doi:10.1038/nm.3713 · Cited by 508 · 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
The role of HER2, EGFR, and other receptor tyrosine kinases in breast cancer
Hsu, J. L., & Hung, M. (2016) · Cancer and Metastasis Reviews · doi:10.1007/s10555-016-9649-6 · Cited by 451 · see citing works
Coniglio, S. J., Eugenin, E., Dobrenis, K., Stanley, E. R., West, B. L., Symons, M. H., & Segall, J. E. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00217 · Cited by 429 · see citing works
Amphiregulin exosomes increase cancer cell invasion
Higginbotham, J. N., Demory Beckler, M., Gephart, J. D., Franklin, J. L., Bogatcheva, G., Kremers, G.-J., Piston, D. W., Ayers, G. D., McConnell, R. E., Tyska, M. J., et al. (2011) · Current Biology · doi:10.1016/j.cub.2011.03.043 · Cited by 360 · see citing works
Human knockouts and phenotypic analysis in a cohort with a high rate of consanguinity
Saleheen, D., Natarajan, P., Armean, I. M., Zhao, W., Rasheed, A., Khetarpal, S. A., Won, H.-H., Karczewski, K. J., O’Donnell-Luria, A. H., Samocha, K. E., et al. (2017) · Nature · doi:10.1038/nature22034 · Cited by 340 · see citing works
EGFR heterogeneity and implications for therapeutic intervention in glioblastoma
Eskilsson, E., Røsland, G. V., Solecki, G. M., Wang, Q., Harter, P. N., Graziani, G., Verhaak, R. G. W., Winkler, F., Bjerkvig, R., & Miletić, H. (2017) · Neuro-Oncology · doi:10.1093/neuonc/nox191 · Cited by 308 · see citing works
Berasain, C., & Avila, M. A. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.01.005 · Cited by 304 · see citing works
HB-EGF is Necessary and Sufficient for Müller Glia Dedifferentiation and Retina Regeneration
Wan, J., Ramachandran, R., & Goldman, D. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.11.020 · Cited by 262 · see citing works
“Human recombinant HB-EGF is encoded by amino acids 1–148 of pro-HB-EGF which is a membrane spanning protein that undergoes ectodomain shedding, releasing a soluble extracellular portion that contains an EGF-like domain that binds the EGFR (Schneider and Wolf, 2009).”
BackgroundThe epidermal growth factor network: role in oocyte growth, maturation and developmental competence
Richani, D., & Gilchrist, R. B. (2017) · Human Reproduction Update · doi:10.1093/humupd/dmx029 · Cited by 277 · see citing works
The multiple roles of amphiregulin in human cancer
Busser, B., Sancey, L., Brambilla, E. M., Coll, J., & Hurbin, A. (2011) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2011.05.003 · Cited by 251 · see citing works
The Role of EREG/EGFR Pathway in Tumor Progression
Cheng, W., Feng, P., Lee, K., Chen, K.-Y., Sun, W.-L., Hiệp, N. V., Luo, C.-S., & Wu, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312828 · Cited by 241 · see citing works
Gentile, P., Orlandi, A., Scioli, M. G., Pasquali, C. D., Bocchini, I., Curcio, C. B., Floris, M., Fiaschetti, V., Floris, R., & Cervelli, V. (2012) · Stem Cells Translational Medicine · doi:10.5966/sctm.2011-0065 · Cited by 224 · see citing works
EGFR Signaling in Liver Diseases
Komposch, K., & Sibilia, M. C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms17010030 · Cited by 221 · see citing works
Epidermal growth factor, from gene organization to bedside
Zeng, F., & Harris, R. C. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.01.011 · Cited by 217 · see citing works
Role of EGFR in the Nervous System
Romanò, R., & Bucci, C. (2020) · Cells · doi:10.3390/cells9081887 · Cited by 204 · see citing works
EGFR-mutated lung cancer: a paradigm of molecular oncology
Zhang, Z., Stiegler, A. L., Boggon, T. J., Kobayashi, S., & Halmos, B. (2010) · Oncotarget · doi:10.18632/oncotarget.186 · Cited by 197 · see citing works
Epiregulin: Roles in normal physiology and cancer
Riese, D. J., & Cullum, R. L. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.005 · Cited by 194 · see citing works
Venkataraman, T., & Frieman, M. B. (2017) · Antiviral Research · doi:10.1016/j.antiviral.2017.03.022 · Cited by 193 · see citing works
The Human Airway Epithelial Basal Cell Transcriptome
Hackett, N. R., Shaykhiev, R., Walters, M. S., Wang, R., Zwick, R. K., Ferris, B., Witover, B., Salit, J., & Crystal, R. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018378 · Cited by 184 · see citing works
Na, K., Mok, J., Kim, J. Y., Rho, C. R., & Joo, C. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-9417 · Cited by 183 · see citing works
Role of Epidermal Growth Factor Receptor (EGFR) and Its Ligands in Kidney Inflammation and Damage
Rayego‐Mateos, S., Rodrigues-Díez, R. R., Morgado‐Pascual, J. L., Valentijn, F. A., Valdivielso, J. M., Goldschmeding, R., & Ruiz-Ortega, M. (2018) · Mediators of Inflammation · doi:10.1155/2018/8739473 · Cited by 177 · see citing works
The EGFR signalling system in the liver: from hepatoprotection to hepatocarcinogenesis
Berasain, C., & Avila, M. A. (2013) · Journal of Gastroenterology · doi:10.1007/s00535-013-0907-x · Cited by 175 · see citing works
Chen, Z., Wang, G.-X., Ma, S. L., Jung, D. Y., Ha, H., Altamimi, T., Zhao, X.-Y., Guo, L., Zhang, P., Hu, C.-R., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.03.016 · Cited by 152 · see citing works
Wang, Y. X., Feige, P., Brun, C. E., Hekmatnejad, B., Dumont, N. A., Renaud, J., Faulkes, S., Guindon, D. E., & Rudnicki, M. A. (2019) · Cell stem cell · doi:10.1016/j.stem.2019.01.002 · Cited by 150 · see citing works
Wu, W. K. K., Wang, G., Coffelt, S. B., Betancourt, A. M., Lee, C. W., Fan, D., Wu, K., Yu, J. Q., Sung, J. J. �., & Cho, C. H. (2010) · International Journal of Cancer · doi:10.1002/ijc.25489 · Cited by 136 · see citing works
The Epidermal Growth Factor Receptor: A Link Between Inflammation and Liver Cancer
Berasain, C., Perugorria, M. J., Latasa, M. U., Castillo, J., Goñi, S., Santamaría, M., Prìeto, J., & Avila, M. A. (2009) · Experimental Biology and Medicine · doi:10.3181/0901-mr-12 · Cited by 132 · see citing works
Solc, P., Schultz, R. M., & Motlík, J. (2010) · Molecular Human Reproduction · doi:10.1093/molehr/gaq034 · Cited by 132 · see citing works
Mechanisms underlying skin disorders induced by EGFR inhibitors
Holcmann, M., & Sibilia, M. C. (2015) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1004969 · Cited by 128 · see citing works
The epidermal growth factor receptor pathway in chronic kidney diseases
Harskamp, L. R., Gansevoort, R. T., van Goor, H., & Meijer, E. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.91 · Cited by 121 · see citing works
Radisky, E. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107347 · Cited by 112 · see citing works
Adema, C. M., Hanington, P. C., Lun, C.-M., Rosenberg, G. H., Aragon, A. D., Stout, B. A., Richard, M. L., Gross, P. S., & Loker, E. S. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.10.019 · Cited by 117 · see citing works
Schröder, S., Herker, E., Itzen, F., He, D. X., Thomas, S., Gilchrist, D. A., Kaehlcke, K., Cho, S., Pollard, K. S., Capra, J. A., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.009 · Cited by 115 · see citing works
Wang, Y., Chen, L., Zhang, M., Li, X., Yang, X., Huang, T., Ban, Y., Li, Y., Li, Q., Zheng, Y., et al. (2023) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2023.05.009 · Cited by 117 · see citing works
Venkataraman, T., Coleman, C. M., & Frieman, M. B. (2017) · Journal of Virology · doi:10.1128/jvi.00182-17 · Cited by 113 · see citing works
Breast Reconstruction With Autologous Fat Graft Mixed With Platelet-Rich Plasma
Gentile, P., Pasquali, C. D., Bocchini, I., Floris, M., Tati, E., Fiaschetti, V., Floris, R., & Cervelli, V. (2012) · Surgical Innovation · doi:10.1177/1553350612458544 · Cited by 112 · see citing works
MiRNA-34a inhibits EGFR-signaling-dependent MMP7 activation in gastric cancer
Liu, G., Jiang, C., Li, D., Wang, R., & Wang, W. (2014) · Tumor Biology · doi:10.1007/s13277-014-2273-6 · Cited by 110 · see citing works
Paudyal, A., Damrau, C., Patterson, V. L., Ermakov, A. S., Formstone, C. J., Tymowska‐Lalanne, Z., Wells, S. E., Lu, X., Norris, D. P., Dean, C. H., et al. (2010) · BMC Developmental Biology · doi:10.1186/1471-213x-10-87 · Cited by 106 · see citing works
He, M., Jin, Q., Chen, C., Liu, Y., Ye, X., Jiang, Y., Ji, F., Qian, H., Gan, D., Yue, S., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0817-3 · Cited by 109 · see citing works
Epidermal growth factor receptor: Structure-function informing the design of anticancer therapeutics
Mitchell, R. A., Luwor, R. B., & Burgess, A. W. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.08.009 · Cited by 101 · see citing works
Ribeiro, F. A. P., Noguti, J., Oshima, C. T. F., & Ribeiro, D. A. (2014) · PubMed · Cited by 103 · see citing works
Wang, F., Xiao, W., Sun, J., Han, D.-H., & Zhu, Y.-H. (2014) · Tumor Biology · doi:10.1007/s13277-014-2131-6 · Cited by 102 · see citing works
RetractedNanba, D., Toki, F., Barrandon, Y., & Higashiyama, S. (2013) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2013.05.009 · Cited by 100 · see citing works
The biologic effects of cigarette smoke on cancer cells
Sobus, S. L., & Warren, G. W. (2014) · Cancer · doi:10.1002/cncr.28904 · Cited by 98 · see citing works
Receptor-based Targeting of Therapeutics
Mehra, N. K., Mishra, V. K., & Jain, N. K. (2013) · Therapeutic Delivery · doi:10.4155/tde.13.6 · Cited by 97 · see citing works
The Chlamydia pneumoniae Invasin Protein Pmp21 Recruits the EGF Receptor for Host Cell Entry
Mölleken, K., Becker, E., & Hegemann, J. H. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003325 · Cited by 97 · see citing works
IGFBP2 potentiates nuclear EGFR–STAT3 signaling
Chua, C. Y. X., Liu, Y., Granberg, K. J., Hu, L., Haapasalo, H., Annala, M., Cogdell, D. E., Verploegen, M. F. A., Moore, L. M., Fuller, G. N., et al. (2015) · Oncogene · doi:10.1038/onc.2015.131 · Cited by 96 · see citing works
Epithelial Inflammation Resulting from an Inherited Loss-of-Function Mutation in EGFR
Campbell, P. H., Morton, P. E., Takeichi, T., Salam, A., Roberts, N., Proudfoot, L. E., Mellerio, J. E., Aminu, K., Wellington, C. L., Patil, S. N., et al. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.164 · Cited by 95 · see citing works
Hanington, P. C., Lun, C.-M., Adema, C. M., & Loker, E. S. (2010) · International Journal for Parasitology · doi:10.1016/j.ijpara.2009.12.005 · Cited by 94 · see citing works
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 94 · see citing works
Laurie, S. A., & Goss, G. D. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.43.4522 · Cited by 91 · see citing works
The EGFR network in bone biology and pathology
Schneider, M. R., Sibilia, M. C., & Erben, R. G. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.06.008 · Cited by 91 · see citing works
Self-citationLigand-Targeted Delivery of Photosensitizers for Cancer Treatment
Gierlich, P., Mata, A. I., Donohoe, C. L., Brito, R. M. M., Senge, M. O., & Gomes-da-Silva, L. C. (2020) · Molecules · doi:10.3390/molecules25225317 · Cited by 91 · see citing works
Interdependent epidermal growth factor receptor signalling and trafficking
Jones, S., & Rappoport, J. Z. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.03.014 · Cited by 90 · see citing works
Guo, Q., Manolopoulou, M., Bian, Y., Schilling, A. B., & Tang, W. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.072 · Cited by 87 · see citing works
Understanding cytokine and growth factor receptor activation mechanisms
Atanasova, M., & Whitty, A. (2012) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2012.729561 · Cited by 87 · see citing works
Dai, Y.-N., Zhu, J.-Z., Fang, Z., Zhao, D.-J., Wan, X.-Y., Zhu, H.-T., Yu, C.-H., & Li, Y.-M. (2015) · Metabolism: Clinical and Experimental · doi:10.1016/j.metabol.2015.08.013 · Cited by 81 · see citing works
Neuregulins in Neurodegenerative Diseases
Ou, G., Lin, W., & Zhao, W. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.662474 · Cited by 84 · see citing works
Dang, Y., He, Q. H., Yang, S., Sun, H., Liu, Y., Li, W., Tang, Y., Zheng, Y., & Wu, T. (2022) · Pharmaceuticals · doi:10.3390/ph15101177 · Cited by 82 · see citing works
Antonyak, M. A., Wilson, K. F., & Cerione, R. A. (2012) · Small GTPases · doi:10.4161/sgtp.20755 · Cited by 84 · see citing works
Epidermal growth factor signalling and bone metastasis
Lü, X., & Kang, Y. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605490 · Cited by 83 · see citing works
Regulated ADAM17-dependent EGF family ligand release by substrate-selecting signaling pathways
Dang, M., Armbruster, N. S., Miller, M. A., Cermeño, E. A., Hartmann, M., Bell, G. W., Root, D. E., Lauffenburger, D. A., Lodish, H. F., & Herrlich, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307478110 · Cited by 83 · see citing works
Nishimura, M., Shin, M.-S., Singhirunnusorn, P., Suzuki, S., Kawanishi, M., Koizumi, K., Saiki, I., & Sakurai, H. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00375-09 · Cited by 83 · see citing works
Epidermal Growth Factor Receptor (EGFR) Crosstalks in Liver Cancer
Berasain, C., Latasa, M. U., Urtasun, R., Goñi, S., Elizalde, M., García‐Irigoyen, O., Azcona, M., Prìeto, J., & Avila, M. A. (2011) · Cancers · doi:10.3390/cancers3022444 · Cited by 81 · see citing works
Liang, D., Chen, H., Zhao, L., Zhang, W., Hu, J., Liu, Z., Zhong, P., Wang, W., Wang, J., & Liang, G. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.10.016 · Cited by 79 · see citing works
Zhang, T., He, M., Zhang, J., Tong, Y., Chen, T., Wang, C., Pan, W., & Xiao, Z. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1113684 · Cited by 77 · see citing works
From wavy hair to naked proteins: The role of transforming growth factor alpha in health and disease
Singh, B., & Coffey, R. J. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.003 · Cited by 75 · see citing works
Saint-Jean, A., de la Maza, M. S., Morral, M., Torras, J., Quintana, R., Molina, J. J., & Molina-Prat, N. (2012) · Ophthalmology · doi:10.1016/j.ophtha.2012.03.002 · Cited by 76 · see citing works
Pastore, S., Lulli, D., & Girolomoni, G. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1244-4 · Cited by 76 · see citing works
Muniz-Feliciano, L., Doggett, T. A., Zhou, Z., & Ferguson, T. A. (2017) · Autophagy · doi:10.1080/15548627.2017.1380124 · Cited by 73 · see citing works
Mechanisms of Invasion in Head and Neck Cancer
Jimenez, L., Jayakar, S. K., Ow, T. J., & Segall, J. E. (2015) · Archives of Pathology & Laboratory Medicine · doi:10.5858/arpa.2014-0498-ra · Cited by 74 · see citing works
Signaling pathways in liver cancer: pathogenesis and targeted therapy
Xue, Y., Ruan, Y., Wang, Y., Xiao, P., & Xu, J. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00184-0 · Cited by 81 · see citing works
Bone Marrow Endothelial Cells Regulate Myelopoiesis in Diabetes Mellitus
Hoyer, F. F., Zhang, X., Coppin, E., Vasamsetti, S. B., Modugu, G., Schloss, M. J., Rohde, D., McAlpine, C. S., Iwamoto, Y., Libby, P., et al. (2020) · Circulation · doi:10.1161/circulationaha.120.046038 · Cited by 70 · see citing works
Xiao, X., He, H., Lin, Z., Luo, P., He, H., Zhou, T., Zhou, Y., & Liu, Z. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-8553 · Cited by 70 · see citing works
Roth, P., & Weller, M. (2014) · Neuro-Oncology · doi:10.1093/neuonc/nou222 · Cited by 70 · see citing works
Ai, S., Duan, J., Liu, X., Bock, S., Tian, Y., & Huang, Z. (2011) · Molecular Pharmaceutics · doi:10.1021/mp100243j · Cited by 69 · see citing works
EGFR signaling patterns are regulated by its different ligands
Knudsen, S. L. J., Mac, A. S. W., Henriksen, L., van Deurs, B., & Grøvdal, L. M. (2014) · Growth Factors · doi:10.3109/08977194.2014.952410 · Cited by 70 · see citing works
How hepatitis C virus invades hepatocytes: The mystery of viral entry
Zhu, Y. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i13.3457 · Cited by 69 · see citing works
SEMA4B inhibits growth of non-small cell lung cancer in vitro and in vivo
Jian, H., Zhao, Y., Liu, B., & Lü, S. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.027 · Cited by 68 · see citing works
Anti-Angiogenic and Anti-Inflammatory Effects of SERPINA3K on Corneal Injury
Liu, X., Lin, Z., Zhou, T., Zong, R., He, H., Liu, Z., Ma, J., Liu, Z., & Zhou, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016712 · Cited by 68 · see citing works
Schneider, M. R., & Yarden, Y. (2015) · Oncogene · doi:10.1038/onc.2015.372 · Cited by 66 · see citing works
Self-citationThe roles of receptor tyrosine kinases and their ligands in the wound repair process.
Müller, A.-K., Meyer, M., & Werner, S. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.09.015 · Cited by 70 · see citing works
Inhibition of EGFR Signaling Protects from Mucormycosis
Watkins, T. N., Gebremariam, T., Swidergall, M., Shetty, A. C., Graf, K. T., Alqarihi, A., Alkhazraji, S., Alsaadi, A. I., Edwards, V. L., Filler, S. G., et al. (2018) · mBio · doi:10.1128/mbio.01384-18 · Cited by 67 · see citing works
Humtsoe, J. O., & Kramer, R. H. (2009) · Oncogene · doi:10.1038/onc.2009.419 · Cited by 66 · see citing works
ErbB-2 nuclear function in breast cancer growth, metastasis and resistance to therapy.
Elizalde, P., Russo, R. C., Chervo, M. F., & Schillaci, R. (2016) · Endocrine-Related Cancer · doi:10.1530/erc-16-0360 · Cited by 54 · see citing works
Gerold, G., Moeller, R. A., & Pietschmann, T. (2019) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a036830 · Cited by 63 · see citing works
GLUT1 Regulation of the Pro-Sclerotic Mediators of Diabetic Nephropathy
Heilig, C. W., Deb, D. K., Abdul, A., Riaz, H., James, L. R., Salameh, J., & Nahman, N. S. (2013) · American Journal of Nephrology · doi:10.1159/000351989 · Cited by 61 · see citing works
Pei, J., Lou, Y., Zhong, R., & Han, B. (2014) · Tumor Biology · doi:10.1007/s13277-014-1850-z · Cited by 60 · see citing works
RetractedNerella, S. G., Joshi, R. K., Bharath, R. D., & Kumar, P. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111979 · Cited by 60 · see citing works
Emerging picture of the distinct traits and functions of microvesicles and exosomes
Antonyak, M. A., & Cerione, R. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1502590112 · Cited by 60 · see citing works
Jedliński, A., Ansell, A., Johansson, A., & Roberg, K. B. (2012) · Journal of Oral Pathology and Medicine · doi:10.1111/j.1600-0714.2012.01177.x · Cited by 58 · see citing works
Quijia, C. R., & Chorilli, M. (2021) · Phytotherapy Research · doi:10.1002/ptr.7291 · Cited by 57 · see citing works
Angiogenesis in Lung Cancer: Understanding the Roles of Growth Factors
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Dong, Y., He, Y., de Boer, L., Stack, M. S., Lumley, J. W., Clements, J. A., & Hooper, J. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.335448 · Cited by 55 · see citing works
Kang, Y. E., Kim, J. M., Choung, S., Joung, K. H., Lee, J. H., Kim, H. J., & Ku, B. J. (2016) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2016.04.007 · Cited by 55 · see citing works
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Leroy, M. C., Perroud, J., Darbellay, B., Bernheim, L., & König, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071770 · Cited by 54 · see citing works
- Authors
- Schneider, M. R., & Wolf, E.
- Affiliations
- Ludwig-Maximilians-Universität München (DE)
- Corresponding author
- Schneider, Marlon R.
- Venue
- Journal of Cellular Physiology
- Publisher
- Wiley
- Published
- 2008-11-12
- Volume
- 218
- Issue
- 3
- Pages
- 460-466
- ISSN
- 0021-9541 (ISSN-L)
- 1097-4652
- OpenAlex
- W1992913621
- Cited by
- 447
- References
- 102
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 28 · 2023: 24 · 2022: 24 · 2021: 22 · 2020: 23 · 2019: 23 · 2018: 27 · 2017: 27 · 2016: 19 · 2015: 31 · 2014: 50 · 2013: 28 · 2012: 26
- FWCI
- 2.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cellular Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Keywords
- epidermal growth factor receptor, EGF ligands, juxtacrine signaling, ectodomain shedding, soluble growth factors, transmembrane proteins, cell proliferation, tissue homeostasis, carcinogenesis, development (biology)
- MeSH terms
- Amino Acid Sequence, Animals, Humans, Ligands, Molecular Sequence Data, Structure-Activity Relationship, Evolution, Molecular, ErbB Receptors
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