The DOI matches its Crossref record; 100 of the 102 references it cites were found in a registry or an index.
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.
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
“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
Citations
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
EGF–ERBB signalling: towards the systems level
Citri, A., & Yarden, Y. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1962 · Cited by 2,056
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 1,622
Prenzel, N., Zwick, E., Daub, H., Leserer, M., Abraham, R., Wallasch, C., & Ullrich, A. (1999) · Nature · doi:10.1038/47260 · Cited by 1,507
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
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., Yee, D., LaMantia, C., Mourton, T., Herrup, K., Harris, R. C., et al. (1995) · Science · doi:10.1126/science.7618084 · Cited by 1,179
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
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
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
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 1,013
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
Harris, R. C. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00105-2 · Cited by 802
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
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
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
MEMBRANE-ANCHORED GROWTH FACTORS
Massagué, J., & Pandiella, A. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.002503 · Cited by 665
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 660
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
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 603
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
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 570
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 563
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
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
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 449
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
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 427
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
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 416
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
Vassar, R. J., & Fuchs, E. V. (1991) · Genes & Development · doi:10.1101/gad.5.5.714 · Cited by 411
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
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 360
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
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 347
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 340
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
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 306
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
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
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 303
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
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 262
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 253
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
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 231
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
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
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
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 207
SnapShot: EGFR Signaling Pathway
Yarden, Y., & Shilo, B. (2007) · Cell · doi:10.1016/j.cell.2007.11.013 · Cited by 203
The many faces of epidermal growth factor repeats.
Cg, D. (1990) · PubMed · Cited by 199
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
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
Schneider, M. R., Werner, S., Paus, R., & Wolf, E. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070942 · Cited by 168
Self-citationHuman 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
Qin, 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
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
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 156
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
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
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 149
Takagi, H., Jhappan, C., Sharp, R., & Merlino, G. T. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115936 · Cited by 141
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 130
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
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 125
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
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
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 116
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
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
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
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
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
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 103
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
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
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
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
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 89
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
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
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
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 74
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
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 69
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
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
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
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 58
Lorenzo, J. A., Quinton, J., Sousa, S., & Raisz, L. G. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112517 · Cited by 51
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
Schneider, M. R., & Wolf, E. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.003 · Cited by 45
Self-citationDempsey, P. J., Meise, K. S., & Coffey, R. J. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00035-1 · Cited by 44
Brown, C. L., Coffey, R. J., & Dempsey, P. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102114200 · Cited by 39
Jhappan, C., Takayama, H., Dickson, R. B., & Merlino, G. T. (1994) · PubMed · Cited by 37
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
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
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
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
Flagged first, then by citations
2 of the 102 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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 4,871
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
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
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 515
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
Metadata
- 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
- Life Sciences › Immunology and Microbiology › Immunology › 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
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