The EGFR family and its ligands in human cancer. signalling mechanisms and therapeutic opportunities.

By Y. Yarden. European Journal of Cancer, 2001

1,675 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/cf532df8a6277a1be32e60bc298bcfcccf40a3a5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Matthew Meyerson
2. S. Werner
3. William C. Hahn
4. William R. Sellers
5. M. Moasser
6. C. Der
7. R. Grose
8. M. Hasmann

In Oncology

1. P. Jänne
2. T. Friess
3. S. Werner
4. William C. Hahn
5. M. Moasser
6. W. Scheuer
7. C. Der
8. Helmut Burtscher

In Radiology, Nuclear Medicine and Imaging

1. S. Werner
2. M. Moasser
3. C. Der
4. R. Grose
5. M. Wieduwilt
6. P. Roberts
7. Lewis C. Cantley
8. N. Iqbal

Citations in the corpus

• The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “While colorectal cancers are not known to harbor genomic abnormalities that activate EGFR, a number of models suggest that they may be driven by overactivity of wild-type EGFR through persistent autocrine loops [171].”
• The Kinome of Pacific Oyster Crassostrea gigas, Its Expression during Development and in Response to Environmental Factors (2016, neutral): “The EGFR signaling module has been highly conserved throughout the course of evolution [80].”
• Strongly enhanced antitumor activity of trastuzumab and pertuzumab combination treatment on HER2-positive human xenograft tumor models. (2009, background): “As such, the HER proteins have been implicated in oncogenesis (2); in particular, tumors that overexpress the HER2 protein or have amplification of the HER2 gene are associated with aggressive disease and poor prognosis (3–6).”
• Regulation of wound healing by growth factors and cytokines. (2003, background): “Upon ligand binding, these receptors form homo- or heterodimers (303).”
• Evolution of Cancer Pharmacological Treatments at the Turn of the Third Millennium (2018, background): “…directed to tyrosine kinase proteins was represented by Gefitinib (Iressa R©) and Erlotinib (Tarceva R©) both directed to the EGFR ATP-binding site and able to inhibit the abnormal activation of MAPK and PI3K/AKT pathways overexpressed in cancer cells (Nicholson et al., 2001; Yarden, 2001).”
• Predicting ligand-dependent tumors from multi-dimensional signaling features (2017, neutral): “These differences in EGFR homo and heterodimerization with HER2 were previously described.(43,44)”
• Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer (2007, background): “Ligand binding results in the formation of receptor homodomers and heterdimers leading to subsequent receptor activation and ultimately the activation of downstream signal transduction pathways (Yarden, 2001; Wiley, 2003).”
• Oncogenic Transformation by Inhibitor-Sensitive and -Resistant EGFR Mutants (2005, background): “Stimulation of the receptor with EGF or other cognate ligands induces receptor dimerization and autophosphorylation, providing docking sites for SH2containing adaptor proteins that mediate the activation of intracellular signaling pathways [1–3].”