EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.

By K. Ferguson, M. B. Berger, J. Mendrola, Hyun-soo Cho, D. Leahy, M. Lemmon. Molecules and Cells, 2003

793 citations recorded by the source corpus.

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

View Paper: https://www.semanticscholar.org/paper/0da95aef23cbd2e622da94cb99f6cbd85986498c

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. R. Roskoski
2. Ping Wee
3. Zhixiang Wang
4. N. Hynes
5. J. Baselga
6. Thomas Holbro
7. M. Lemmon
8. D. Leahy

In Oncology

1. N. Hynes
2. R. Roskoski
3. J. Baselga
4. S. Swain
5. Ping Wee
6. Zhixiang Wang
7. Thomas Holbro
8. D. Leahy

In Radiology, Nuclear Medicine and Imaging

1. N. Hynes
2. J. Baselga
3. R. Roskoski
4. Thomas Holbro
5. S. Swain

Citations in the corpus

• Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “Originally observed by Yarden and Schlessinger [112,113], the ability to visualize crystal structures have shown that mechanistically, prior to ligand binding, domain II is folded into domain IV via disulfide bonds, in a “tethered” conformation that auto-inhibits dimerization [26,114].”
• Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, background): “Receptor dimerization (pairing) is an essential requirement for Erbb function and for the signalling activity of these receptor”
• Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment (2009, positive): “, 2002), with domain IV based on the structure of the inactive EGFR extracellular domain (PDB ID: 1NQL) (Ferguson et al., 2003).”
• Mechanism of activation and inhibition of the HER4/ErbB4 kinase. (2008, background): “Crystallographic studies of the extracellular regions of ErbB1, ErbB3, and ErbB4 show them to be made up of four discrete subdomains that adopt an autoinhibited conformation in the absence of ligand (Bouyain et al., 2005; Burgess et al., 2003; Cho and Leahy, 2002; Ferguson et al., 2003).”
• The ErbB/HER family of protein-tyrosine kinases and cancer. (2014, background): “The X-ray crystal structure of the extracellular segment of EGFR reveals that the leucine-rich domain I resembles domain III and that the cysteine-rich domain II resembles domain IV [34,36,37].”
• Signaling pathways in cancer-associated fibroblasts and targeted therapy for cancer (2021, background): “Specifically, the extracellular region of EGFR is subdivided into four domains, and the intracellular tyrosine kinase domain is highly conserved with variable phosphorylation sites.(241,242) The EGFR signaling pathway is activated by ligand-induced receptor dimerization, in which the tyrosine residu”
• Membranes are more mosaic than fluid (2005, background): “Interactions of the ectodomain structures are known to be functionally important in many cases, such as the tyrosine kinase receptor”
• ErbB receptors: directing key signaling networks throughout life. (2004, background): “This maintains ErbB1 in a “closed” conformation in which the ligand-binding domains I and III are held apart (17).”
• Targeting the EGFR signaling pathway in cancer therapy (2012, background): “As a result, the dimerization arm in domain II then interacts with an identical dimerization arm of another receptor molecule to form a homodimer [4,5].”
• An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. (2006, background): “The structural basis for ligand-induced dimerization of the extracellular region of EGFR family members is now well understood (Cho and Leahy, 2002; Ferguson et al., 2003; Garrett et al., 2002; Ogiso et al., 2002; Schlessinger, 2002).”