Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.

By Thomas P. J. Garrett, N. Mckern, M. Lou, T. Elleman, T. Adams, G. Lovrecz, Hong-Jian Zhu, F. Walker, M. J. Frenkel, P. Hoyne and 4 more. 2002

827 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Oncology

How researchers see this paper

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

In Cellular and Molecular Neuroscience

1. R. Roskoski
2. Y. Yarden
3. N. Hynes
4. Yigong Shi
5. A. Citri

In Molecular Biology

1. R. Roskoski
2. N. Hynes
3. C. Blobel
4. M. Moasser
5. M. Lemmon
6. Yigong Shi
7. M. Wieduwilt
8. Y. Yarden

In Oncology

1. R. Roskoski
2. N. Hynes
3. M. Moasser
4. C. Blobel
5. M. Lemmon
6. M. Wieduwilt
7. Y. Yarden
8. A. Citri

Citations in the corpus

• Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. (2002, background): “It was proposed that loop prevents EGF-induced signaling via EGFR (Ogiso domains I and III form the ligand binding domain of EGFR et al., 2002; Garrett et al., 2002) while other parts of the extracellular domain mediate Dimerization of EGFR requires the binding of two molreceptor dimerization and…”
• 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).”
• The deaf and the dumb: the biology of ErbB-2 and ErbB-3. (2003, background): “Most previous lines of evidence relate to the interaction of EGF with ErbB-1 (reviewed by Groenen et al. [37]).”
• 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).”
• Epidermal growth factor receptor: mechanisms of activation and signalling. (2003, background): “The sidechain of the EGFR residue Asn 12 also makes a hydrogen bond with the mainchain nitrogen atom of Gly 40 of TGF [18] (Fig.”
• Mechanism of activation and inhibition of the HER4/ErbB4 kinase. (2008, background): “Ligand binding promotes a domain rearrangement that exposes previously obscured surfaces and allows them to mediate dimerization (Burgess et al., 2003; Garrett et al., 2002; Ogiso et al., 2002).”
• Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. (2005, background): “There is no simple correlation between the is a salt bridge between an arginine on the ligand (R41 in EGF number of hydrogen bonds or salt bridges in a protein-protein and R42 in TGFα) and an aspartate (D355) near the N-terminal interaction and the observed affinity of a complex.”
• The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “A 2:2 complex is formed by this interaction in which the ligands face outward from the interaction face of the two ectodomains [33,34].”