An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors.

By Antony W. Burgess, Hyun-soo Cho, C. Eigenbrot, K. Ferguson, Thomas P. J. Garrett, D. Leahy, M. Lemmon, M. Sliwkowski, Colin W. Ward, S. Yokoyama. Molecules and Cells, 2003

955 citations recorded by the source corpus.

Subfields: Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/3aa7888f4fce99005fcf98cd51ef418ec5763ebd

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In Oncology

1. J. Baselga
2. N. Hynes
3. M. Moasser
4. S. Swain
5. Tony Pawson
6. Yigong Shi
7. D. Leahy
8. Ping Wee

In Radiology, Nuclear Medicine and Imaging

1. N. Hynes
2. J. Baselga
3. M. Moasser
4. Yigong Shi
5. S. Swain
6. Z. Du
7. Christine Lovly
8. Lewis C. Cantley

Citations in the corpus

• Post-translational modifications in signal integration (2010, background): “EGFR is primarily internalized through clathrin-mediated endocytosis (CME”
• Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment (2009, neutral): “Crystal structures of the extracellular domains of EGFR show that the active dimer brings the two C-terminal ends of the extracellular domains into close proximity (Burgess et al., 2003).”
• A glimpse of structural biology through X-ray crystallography. (2014, background): “The activation mechanism of EGFR has been elegantly revealed by crystallographic discovery and subsequent biochemical analysis (Burgess et al., 2003; Zhang et al., 2006).”
• Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. (2005, background): “For unliganded sEGFR, some 5% of the receptors are estimated to be untethered and to adopt a range alteration of Q384A results in a z1 ␮M K D in both cases (Figure 5). of extended conformations (Burgess et al., 2003; Ferguson et Figure 6.”
• Targets of curcumin (2011, background): “EGFR and its family members are stimulated by several distinct ligands, including epidermal growth factor (EGF), TGF-α, amphiregulin, betacellulin, epigen, epiregulin, and heparin binding EGF-like growth factor [65,66].”
• GC1118, an Anti-EGFR Antibody with a Distinct Binding Epitope and Superior Inhibitory Activity against High-Affinity EGFR Ligands (2015, background): “6 Structural studies of the EGF-EGFR complex depict the process of EGFR activation after ligand binding (19-22), which triggers a conformational change in EGFR from a tethered form to an open form.”
• An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. (2006, background): “The precise disposition of the C-terminal ends of the extracellular domains in an activated EGFR dimer is unknown, but they are estimated to be $20 A ˚ apart (Burgess et al., 2003).”
• Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “ERBB2 does not contain a ligand-binding domain, and no direct ligand for it has ever been identified, yet ERBB2 appears to be the preferred binding partner to its family members [23–25], as its dimerization arm is constitutively exposed [26].”
• Activity of the dual kinase inhibitor lapatinib (GW572016) against HER-2-overexpressing and trastuzumab-treated breast cancer cells. (2006, background): “On ligand binding, the EGFR can form heterodimeric complexes with neighboring HER-2 receptors (36, 37) and transactivate HER-2.”
• Mechanism of activation and inhibition of the HER4/ErbB4 kinase. (2008, background): “Discovery of the importance of an asymmetric EGFR kinase dimer for regulation of kinase activity provided a satisfying link between ligand-induced receptor dimerization and kinase activation (Burgess et al., 2003; Jeffrey et al., 1995; Zhang et al., 2006).”
• ERBB receptors and cancer: the complexity of targeted inhibitors (2005, background): “Structural studies on ERBB receptors Publications describing the crystal structure of the EGFR, ERBB2 and ERBB3 ectodomains (reviewed in Ref”
• Targeting the EGFR signaling pathway in cancer therapy (2012, background): “1 Anti-EGFR monoclonal antibodies The monoclonal antibodies against EGFR were specifically designed to be directed against the extracellular region of EGFR which creates a ligand competitive inhibition, thus preventing receptor dimerization, auto-phosphorylation and downstream signaling [54].”
• Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, background): “However, Erbb receptors normally exist as inactive monomers with the molecules folded in such a way as to prevent dimerizatio”
• Mechanisms of receptor tyrosine kinase activation in cancer (2018, positive): “With the dimerization arm exposed, the extracellular region of the receptor dimerizes [18], inducing intracellular conformational changes so that they can enable kinase activation [9].”
• JMJD8 Promotes Malignant Progression of Lung Cancer by Maintaining EGFR Stability and EGFR/PI3K/AKT Pathway Activation (2021, background): “The EGFR protein participates in various signaling pathways, and the phosphorylation of tyrosine residues in its intracellular kinase domain can initiate downstream signaling pathways [8] including MAPK/ERK and PI3K/AKT [9].”