Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.

By Hideo Ogiso, R. Ishitani, O. Nureki, S. Fukai, M. Yamanaka, Jae-Hoon Kim, Kazuki Saito, A. Sakamoto, M. Inoue, M. Shirouzu and 1 more. Cell, 2002

1,183 citations recorded by the source corpus.

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

View Paper: https://www.semanticscholar.org/paper/02a97dc99e9fcef809c6c8860d0bed0a052d9541

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

In Molecular Biology

1. N. Hynes
2. J. Baselga
3. C. Blobel
4. Y. Yarden
5. M. Lemmon
6. Yigong Shi
7. M. Sliwkowski
8. S. Swain

In Oncology

1. N. Hynes
2. J. Baselga
3. C. Blobel
4. Y. Yarden
5. S. Swain
6. D. Leahy
7. M. Lemmon
8. M. Sliwkowski

In Radiology, Nuclear Medicine and Imaging

1. N. Hynes
2. J. Baselga
3. C. Blobel
4. S. Swain
5. Y. Yarden
6. M. Sliwkowski
7. Yigong Shi
8. A. Citri

Citations in the corpus

• The R-spondin/Lgr5/Rnf43 module: regulator of Wnt signal strength (2014, neutral): “…each contain three similarly constructed cysteine-knotted b hairpins (Chen et al. 2013; Peng et al. 2013a; Wang et al. 2013a; Xu et al. 2013; Zebisch et al. 2013) with disulfide bond patterns that appear common to Furin domains seen in other proteins (Garrett et al. 1998; Ogiso et al. 2002).”
• Novel anticancer targets: revisiting ERBB2 and discovering ERBB3 (2009, background): “Thus, the binding of growth factors might stabilize these receptors in a conformation that allows dimerizatio”
• A glimpse of structural biology through X-ray crystallography. (2014, background): “Growth factor binding induces conformational changes in the extracellular domain, leading to its dimerization with the two ligands on opposite sides of the heterocomplex (Garrett et al., 2002;Ogiso et al., 2002).”
• The discovery of receptor tyrosine kinases: targets for cancer therapy (2004, result): “Consistent with this — in two recent publications — Ogiso and colleague”
• Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. (2002, background): “Ogiso et al. (2002) crystallizedkey components of the signaling pathways they activate the entire extracellular domain of EGFR in complex withwill result in severe diseases such as cancer, diabetes, EGF and determined the structure at a resolution ofimmune deficiencies, and cardiovascular diseases,…”
• Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2–Tie2 complex (2006, background): “or from ligand-induced conformational changes in the receptor that result in its dimerization (as in EGF”
• ADAMs: key components in EGFR signalling and development (2005, background): “The crystal structures of the soluble EGFR ectodomain with or without a bound soluble ligand (TGFα or EGF) have been solve”
• An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. (2003, methodology): “…no significant (static) structural differences are found between the EGF-bound and The crystal structure of the unphosphorylated EGFR kinase domain (Stamos et al., 2002) suggests one expla-unliganded states of domain III (Ferguson et al., 2003; Ogiso et al., 2002) argues against this possibility.”
• 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”
• EGF–ERBB signalling: towards the systems level (2006, background): “The structures of ligand-occupied ERBB1 reveal a back-to-back dimer, in which a dimerization arm from domain II of one partner binds to a docking site at the base of domain II within the second partne”
• Mechanisms of receptor tyrosine kinase activation in cancer (2018, neutral): “The extracellular regions of the ErbB receptors family include four subdomains (I-IV) [16].”
• Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. (2005, background): “The ligand complex (Ogiso et al., 2002), it is apparent that FabC225 not binding site on domain I is unaffected, but growth factor must only overlaps with the bound EGF but also with parts of doengage sites on both domains I and III for high-affinity binding main I (Figure 6).”