Cited by 447HER2/EGFR in Cancer ResearchFibroblast Growth Factor ResearchCytokine Signaling Pathways and Interactions

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The epidermal growth factor receptor ligands at a glance

Schneider, Marlon R., Wolf, Eckhard·2009·Journal of Cellular Physiology

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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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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
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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
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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
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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
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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
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Nerella, 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
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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 59
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Authors: Schneider, M. R., & Wolf, E.
Affiliations: Ludwig-Maximilians-Universität München (DE)
Corresponding author: Schneider, Marlon R.
ORCID: Schneider, Marlon R.
Wolf, Eckhard
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
DOI: 10.1002/jcp.21635
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
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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