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A Structural Perspective on the Regulation of the Epidermal Growth Factor Receptor

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Dual targeting of EGFR can overcome a major drug resistance mutation in mouse models of EGFR mutant lung cancer

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A Glimpse of Structural Biology through X-Ray Crystallography

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Structure-Based View of Epidermal Growth Factor Receptor Regulation

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EGFR signaling pathway as therapeutic target in human cancers

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Oncogenic Mutations Counteract Intrinsic Disorder in the EGFR Kinase and Promote Receptor Dimerization

Shan, Y., Eastwood, M. P., Zhang, X., Kim, E. T., Arkhipov, A. S., Dror, R. O., Jumper, J., Kuriyan, J., & Shaw, D. E. (2012) · Cell · doi:10.1016/j.cell.2012.02.063 · Cited by 360 · see citing works

Update on Epidermal Growth Factor Receptor Mutations in Non–Small Cell Lung Cancer

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Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface

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The structure of P‐TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation

Baumli, S., Lolli, G., Lowe, E. D., Troiani, S., Rusconi, L., Bullock, A. N., Debreczeni, J. E., Knapp, S., & Johnson, L. N. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.121 · Cited by 357 · see citing works

Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor

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Structure and mechanism of human DNA polymerase η

Biertümpfel, C., Zhao, Y., Kondo, Y., Ramón‐Maiques, S., Gregory, M., Lee, J. Y., Masutani, C., Lehmann, A. R., Hanaoka, F., & Yang, W. (2010) · Nature · doi:10.1038/nature09196 · Cited by 349 · see citing works

Molecular Mechanisms of Disease-Causing Missense Mutations

Stefl, S. K., Nishi, H., Petukh, M. G., Panchenko, A. R., & Alexov, E. G. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.07.014 · Cited by 334 · see citing works

Receptor Tyrosine Kinases: Legacy of the First Two DecadesPreprint

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Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3

Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338 · see citing works

Expression and Function of the Epidermal Growth Factor Receptor in Physiology and Disease

Chen, J., Zeng, F., Forrester, S. J., Eguchi, S., Zhang, M., & Harris, R. C. (2016) · Physiological Reviews · doi:10.1152/physrev.00030.2015 · Cited by 330 · see citing works

The many faces of calmodulin in cell proliferation, programmed cell death, autophagy, and cancer

Berchtold, M. W., & Villalobo, A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.021 · Cited by 312 · see citing works

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

Brewer, M. R., Choi, S. H., Alvarado, D., Moravcevic, K., Pozzi, A., Lemmon, M. A., & Carpenter, G. F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.034 · Cited by 314 · see citing works

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

Hohmann, U., Lau, K., & Hothorn, M. (2017) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042916-040957 · Cited by 312 · see citing works

Structure and Clinical Relevance of the Epidermal Growth Factor Receptor in Human Cancer

Kumar, A., Petri, E. T., Halmos, B., & Boggon, T. J. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.12.1178 · Cited by 308 · see citing works

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works

Role of ErbB Receptors in Cancer Cell Migration and Invasion

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Known and putative mechanisms of resistance to EGFR targeted therapies in NSCLC patients with EGFR mutations-a review.

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Structure and Chemical Inhibition of the RET Tyrosine Kinase Domain

Knowles, P. P., Murray‐Rust, J., Kjær, S., Scott, R. P., Hanrahan, S. J., Santoro, M. M., Ibáñez, C. F., & McDonald, N. Q. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605604200 · Cited by 305 · see citing works

Allosteric Activation of Functionally Asymmetric RAF Kinase Dimers

Hu, J., Stites, E. C., Yu, H., Germino, E., Meharena, H. S., Stork, P. A., Kornev, A. P., Taylor, S. S., & Shaw, A. S. (2013) · Cell · doi:10.1016/j.cell.2013.07.046 · Cited by 302 · see citing works

EGFR family: Structure physiology signalling and therapeutic targets ^†

Burgess, A. W. (2008) · Growth Factors · doi:10.1080/08977190802312844 · Cited by 288 · see citing works

Functional selectivity of EGF family peptide growth factors: Implications for cancer

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Dynamics-Driven Allostery in Protein Kinases

Kornev, A. P., & Taylor, S. S. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.09.002 · Cited by 284 · see citing works

Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitorPreprint

Jaillais, Y., Hothorn, M., Belkhadir, Y., Dabi, T., Nimchuk, Z. L., Meyerowitz, E. M., & Chory, J. (2011) · Genes & Development · doi:10.1101/gad.2001911 · Cited by 276 · see citing works

Signalling scaffolds and local organization of cellular behaviour

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ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding

Low-Nam, S. T., Lidke, K. A., Cutler, P. J., Roovers, R. C., Henegouwen, P. M. P. V. B. E., Wilson, B. S., & Lidke, D. S. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2135 · Cited by 273 · see citing works

Transformable peptide nanoparticles arrest HER2 signalling and cause cancer cell death in vivo

Zhang, L., Jing, D., Jiang, N., Rojalin, T., Baehr, C. M., Zhang, D., Xiao, W., Wu, Y., Cong, Z., Li, J. J., et al. (2020) · Nature Nanotechnology · doi:10.1038/s41565-019-0626-4 · Cited by 273 · see citing works

Protein kinase inhibitors: contributions from structure to clinical compounds

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The molecular circuitry of brassinosteroid signaling

Belkhadir, Y., & Jaillais, Y. (2015) · New Phytologist · doi:10.1111/nph.13269 · Cited by 255 · see citing works

A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment

Okatsu, K., Uno, M., Koyano, F., Go, E., Kimura, M., Oka, T., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.509653 · Cited by 248 · see citing works

The Mad2 Conformational Dimer: Structure and Implications for the Spindle Assembly Checkpoint

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Tailoring T-cell receptor signals by proximal negative feedback mechanisms

Acuto, O., Bartolo, V. D., & Michel, F. (2008) · Nature reviews. Immunology · doi:10.1038/nri2397 · Cited by 245 · see citing works

Abscisic acid perception and signaling: structural mechanisms and applications

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Bronchial and Peripheral Murine Lung Carcinomas Induced by T790M-L858R Mutant EGFR Respond to HKI-272 and Rapamycin Combination Therapy

Li, D., Shimamura, T., Ji, H., Chen, L., Haringsma, H. J., McNamara, K. L., Liang, M., Perera, S. A., Zaghlul, S., Borgman, C. L., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.06.005 · Cited by 242 · see citing works

The ERBB3 receptor in cancer and cancer gene therapy

Sithanandam, G., & Anderson, L. M. (2008) · Cancer Gene Therapy · doi:10.1038/cgt.2008.15 · Cited by 240 · see citing works

Ligand-Specific c-Fos Expression Emerges from the Spatiotemporal Control of ErbB Network Dynamics

Nakakuki, T., Birtwistle, M. R., Saeki, Y., Yumoto, N., Ide, K., Nagashima, T., Brusch, L., Ogunnaike, B. A., Okada, M., & Kholodenko, B. Ν. (2010) · Cell · doi:10.1016/j.cell.2010.03.054 · Cited by 241 · see citing works

Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation

Hsu, J.-M., Chen, C., Chou, C., Kuo, H.-P., Li, L., Lin, C.-Y., Lee, H.-J., Wang, Y., Liu, M., Liao, H.-W., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2158 · Cited by 240 · see citing works

International Union of Basic and Clinical Pharmacology. XC. Multisite Pharmacology: Recommendations for the Nomenclature of Receptor Allosterism and Allosteric Ligands

Christopoulos, A., Changeux, J., Catterall, W. A., Fabbro, D., Burris, T. P., Cidlowski, J. A., Olsen, R. W., Peters, J. A., Neubig, R. R., Pin, J., et al. (2014) · Pharmacological Reviews · doi:10.1124/pr.114.008862 · Cited by 238 · see citing works

Structure and function of VEGF receptors

Stuttfeld, E., & Ballmer‐Hofer, K. (2009) · IUBMB Life · doi:10.1002/iub.234 · Cited by 238 · see citing works

The Chemical Biology of Protein Phosphorylation

Tarrant, M. K., & Cole, P. A. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103047 · Cited by 238 · see citing works

Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70

Deindl, S., Kadlecek, T. A., Brdička, T., Cao, X., Weiss, A., & Kuriyan, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.039 · Cited by 237 · see citing works

Differential Inhibitor Sensitivity of Anaplastic Lymphoma Kinase Variants Found in Neuroblastoma

Bresler, S. C., Wood, A., Haglund, E. A., Courtright, J., Belcastro, L. T., Plegaria, J. S., Cole, K. A., Toporovskaya, Y., Zhao, H., Carpenter, E. L., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002950 · Cited by 237 · see citing works

p95HER2 and Breast Cancer

Arribas, J., Baselga, J. M., Pedersen, K., & Parra-Palau, J. L. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3795 · Cited by 236 · see citing works

Research Highlights

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Studies of the Allosteric Activation of the Epidermal Growth Factor Receptor

Engel, K. A. (2013) · eScholarship (California Digital Library)

Emerging Allosteric Mechanism of EGFR Activation in Physiological and Pathological Contexts

Tsai, C., & Nussinov, R. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.05.021 · Cited by 44 · see citing works

EGF Receptor Activation: Push Comes to Shove

Hubbard, S. R. (2006) · Cell · doi:10.1016/j.cell.2006.05.028 · Cited by 28 · see citing works

Activation Mechanism of Solubilized Epidermal Growth Factor Receptor Tyrosine Kinase

Ge, G., Wu, J., Wang, Y., & Lin, Q. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6285 · Cited by 12 · see citing works