Emerging Allosteric Mechanism of EGFR Activation in Physiological and Pathological Contexts
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[1] R. Nussinov,et al. 'Latent drivers' expand the cancer mutational landscape. , 2015, Current opinion in structural biology.
[2] John Kuriyan,et al. An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor , 2006, Cell.
[3] M. Lemmon,et al. Ligand regulation of a constitutively dimeric EGF receptor , 2015, Nature Communications.
[4] D. Shaw,et al. Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor , 2013, Cell.
[5] R. Gniadecki,et al. Ligand-independent activation of the EGFR by lipid raft disruption. , 2006, The Journal of investigative dermatology.
[6] Gavin MacBeath,et al. A quantitative protein interaction network for the ErbB receptors using protein microarrays , 2006, Nature.
[7] J. Schlessinger,et al. Cell Signaling by Receptor Tyrosine Kinases , 2000, Cell.
[8] John G. Koland,et al. Coarse-Grained Molecular Simulation of Epidermal Growth Factor Receptor Protein Tyrosine Kinase Multi-Site Self-Phosphorylation , 2014, PLoS Comput. Biol..
[9] Ozlem Keskin,et al. Principles of K-Ras effector organization and the role of oncogenic K-Ras in cancer initiation through G1 cell cycle deregulation , 2015, Expert review of proteomics.
[10] Y. Sako,et al. Lipid-Protein Interplay in Dimerization of Juxtamembrane Domains of Epidermal Growth Factor Receptor. , 2018, Biophysical journal.
[11] L. Pike,et al. The Membrane-proximal Intracellular Domain of the Epidermal Growth Factor Receptor Underlies Negative Cooperativity in Ligand Binding* , 2011, The Journal of Biological Chemistry.
[12] A. Pozzi,et al. The juxtamembrane region of the EGF receptor functions as an activation domain. , 2009, Molecular cell.
[13] T. Walz,et al. Mechanisms for Kinase-mediated Dimerization of the Epidermal Growth Factor Receptor* , 2012, The Journal of Biological Chemistry.
[14] A. Ullrich,et al. Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells , 1987, Cell.
[15] Anton Arkhipov,et al. Architecture and Membrane Interactions of the EGF Receptor , 2013, Cell.
[16] M. Lemmon,et al. Structural Basis for Negative Cooperativity in Growth Factor Binding to an EGF Receptor , 2010, Cell.
[17] R. Nussinov,et al. Unraveling structural mechanisms of allosteric drug action. , 2014, Trends in pharmacological sciences.
[18] S. Harrison,et al. Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes , 1996, Nature Structural Biology.
[19] Ruth Nussinov,et al. A Unified View of “How Allostery Works” , 2014, PLoS Comput. Biol..
[20] C R King,et al. erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells. , 1987, Science.
[21] L. Pike,et al. The Tethering Arm of the EGF Receptor Is Required for Negative Cooperativity and Signal Transduction* , 2010, The Journal of Biological Chemistry.
[22] Hyun-soo Cho,et al. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. , 2003, Molecular cell.
[23] Susan S. Taylor,et al. Regulation of protein kinases; controlling activity through activation segment conformation. , 2004, Molecular cell.
[24] Anatoly Kiyatkin,et al. The Dark Side of Cell Signaling: Positive Roles for Negative Regulators , 2016, Cell.
[25] M. Resh,et al. Cholesterol Depletion from the Plasma Membrane Triggers Ligand-independent Activation of the Epidermal Growth Factor Receptor* , 2002, The Journal of Biological Chemistry.
[26] M. Sliwkowski,et al. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. , 2003, Molecular cell.
[27] N. Hynes,et al. ErbB receptors and signaling pathways in cancer. , 2009, Current opinion in cell biology.
[28] John Foley,et al. Functional selectivity of EGF family peptide growth factors: implications for cancer. , 2009, Pharmacology & therapeutics.
[29] Y. Yarden,et al. Untangling the ErbB signalling network , 2001, Nature Reviews Molecular Cell Biology.
[30] E. Isacoff,et al. Molecular basis for multimerization in the activation of the epidermal growth factor receptor , 2016, eLife.
[31] A. Kiyatkin,et al. EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics , 2017, Cell.
[32] Ruth Nussinov,et al. Precision medicine review: rare driver mutations and their biophysical classification , 2019, Biophysical Reviews.
[33] Laura C. Zanetti-Domingues,et al. The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers , 2018, Nature Communications.
[34] J. Kuriyan,et al. The Conformational Plasticity of Protein Kinases , 2002, Cell.
[35] G. Kéri,et al. Small Molecule Inhibition of ERK Dimerization Prevents Tumorigenesis by RAS-ERK Pathway Oncogenes. , 2015, Cancer cell.
[36] S. Skvortsov,et al. Quantitative proteomics and phosphoproteomics reveal novel insights into complexity and dynamics of the EGFR signaling network , 2008, Proteomics.
[37] G. Carpenter,et al. Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation , 2007, Proceedings of the National Academy of Sciences.
[38] Shigeyuki Yokoyama,et al. Structural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor Receptor , 2010, Molecular and Cellular Biology.
[39] T. Hunter,et al. The Protein Kinase Complement of the Human Genome , 2002, Science.