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.
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“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
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Cites
Genes that mediate breast cancer metastasis to lung
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EGF–ERBB signalling: towards the systems level
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An Essential Role for Ectodomain Shedding in Mammalian Development
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Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
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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
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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
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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 4,871
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
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