An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor

Activating Mutations in the Epidermal Growth Factor Receptor Underlying Responsiveness of Non–Small-Cell Lung Cancer to Gefitinib

Lynch, T. J., Bell, D. W., Sordella, R., Gurubhagavatula, S., Okimoto, R. A., Brannigan, B. W., Harris, P. L., Haserlat, S. M., Supko, J. G., Haluska, F. G., et al. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040938 · Cited by 11,486

EGFR Mutations in Lung Cancer: Correlation with Clinical Response to Gefitinib Therapy

Paez, J. G., Jänne, P. A., Lee, J. C., Tracy, S., Greulich, H., Gabriel, S., Herman, P., Kaye, F. J., Lindeman, N., Boggon, T. J., et al. (2004) · Science · doi:10.1126/science.1099314 · Cited by 9,368

Untangling the ErbB signalling network

Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974

EGF receptor gene mutations are common in lung cancers from “never smokers” and are associated with sensitivity of tumors to gefitinib and erlotinib

Pao, W., Miller, V., Zakowski, M., Doherty, J., Politi, K., Sarkaria, I., Singh, B., Heelan, R., Rusch, V., Fulton, L., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405220101 · Cited by 4,338

Clinical and biological features associated with epidermal growth factor receptor gene mutations in lung cancers

Shigematsu, H., Lin, L., Takahashi, T., Nomura, M., Suzuki, M., Wistuba, I. I., Fong, K. M., Lee, H., Toyooka, S., Shimizu, N., et al. (2005) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dji055 · Cited by 2,377

The Conformational Plasticity of Protein Kinases

Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760

Gefitinib-Sensitizing EGFR Mutations in Lung Cancer Activate Anti-Apoptotic Pathways

Sordella, R., Bell, D. W., Haber, D. A., & Settleman, J. E. (2004) · Science · doi:10.1126/science.1101637 · Cited by 1,605

Structure of the Epidermal Growth Factor Receptor Kinase Domain Alone and in Complex with a 4-Anilinoquinazoline Inhibitor

Stamos, J. L., Sliwkowski, M. X., & Eigenbrot, C. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207135200 · Cited by 1,594

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

Jeffrey, P. D., Russo, A. A., Polyák, K., Gibbs, E., Hurwitz, J., Massagué, J., & Pavletich, N. P. (1995) · Nature · doi:10.1038/376313a0 · Cited by 1,455

Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains

Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J.-H., Saito, K., Sakamoto, A., Inoue, M., Shirouzu, M., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00963-7 · Cited by 1,227

HER2 splice variants in breast cancer: investigating their impact on diagnosis and treatment outcomes

Hart, V., Gautrey, H., Kirby, J. A., & Tyson-Capper, A. J. (2020) · Oncotarget · doi:10.18632/oncotarget.27789 · Cited by 41

Mechanisms of Action of EGFR Tyrosine Kinase Receptor Incorporated in Extracellular Vesicles

Zanetti-Domingues, L. C., Bonner, S. E., Martin-Fernandez, M. L., & Huber, V. (2020) · Cells · doi:10.3390/cells9112505 · Cited by 41

Inverse correlation between T hr‐669 and constitutive tyrosine phosphorylation in the asymmetric epidermal growth factor receptor dimer conformation

Sato, K., Shin, M., Sakimura, A., Zhou, Y., Tanaka, T., Kawanishi, M., Kawasaki, Y., Yokoyama, S., Koizumi, K., Saiki, I., et al. (2013) · Cancer Science · doi:10.1111/cas.12225 · Cited by 38

Multiple post-translational modifications ensure EGFR functionality: Potential therapeutic targets to overcome its drug-resistance mutations

He, Q., Qu, M., Bao, H., Xu, Y., Shen, T., Tan, D., Barkat, M. Q., Xu, C., Zeng, L., & Wu, X. (2023) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2023.03.003 · Cited by 38

Targeting HER2 in solid tumors: Unveiling the structure and novel epitopes

Liu, X., Song, Y., Cheng, P., Liang, B., & Xing, D. (2024) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2024.102826 · Cited by 37

Regulation of the Ligand-dependent Activation of the Epidermal Growth Factor Receptor by Calmodulin

Li, H., Panina, S., Kaur, A., Ruano, M. J., Sánchez‐González, P., la Cour, J. M., Stephan, A., Olesen, U. H., Berchtold, M. W., & Villalobo, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.317529 · Cited by 37

Inhibiting EGFR Dimerization Using Triazolyl-Bridged Dimerization Arm Mimics

Hanold, L. E., Oruganty, K., Ton, N. T., Beedle, A. M., Kannan, N., & Kennedy, E. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118796 · Cited by 37

Destabilization of the Epidermal Growth Factor Receptor (EGFR) by a Peptide That Inhibits EGFR Binding to Heat Shock Protein 90 and Receptor Dimerization

Ahsan, A., Ray, D., Ramanand, S. G., Hegde, A., Whitehead, C. E., Rehemtulla, A., Morishima, Y., Pratt, W. B., Osawa, Y., Lawrence, T. S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492280 · Cited by 37

Structure-Functional Prediction and Analysis of Cancer Mutation Effects in Protein Kinases

Dixit, A., & Verkhivker, G. M. (2014) · Computational and Mathematical Methods in Medicine · doi:10.1155/2014/653487 · Cited by 37

Mechanistic Insights into R776H Mediated Activation of Epidermal Growth Factor Receptor Kinase

Ruan, Z., & Kannan, N. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00444 · Cited by 37

Hyaluronan/RHAMM Interactions in Mesenchymal Tumor Pathogenesis

Kouvidi, K., Nikitovic, D., Berdiaki, A., & Tzanakakis, G. N. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-800092-2.00012-5 · Cited by 37

EGFR mutants found in non-small cell lung cancer show different levels of sensitivity to suppression of Src: implications in targeting therapy

Fu, Y.-N., Yeh, C.-L., Cheng, H.-Y. H., Yang, C.-H., Tsai, S., Huang, S.-F., & Chen, Y.-R. (2008) · Oncogene · doi:10.1038/sj.onc.1210684 · Cited by 42

Insights into the suanzaoren mechanism—From constructing the 3D structure of GABA-A receptor to its binding interaction analysis

Chen, C. Y. (2008) · Journal of The Chinese Institute of Chemical Engineers · doi:10.1016/j.jcice.2008.03.013 · Cited by 37

Emerging importance of HER3 in tumorigenesis and cancer therapy

Garrett, J. T., Tendler, S., Feroz, W., Kilroy, M. K., & Yu, H. A. (2025) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-025-01008-y · Cited by 37

The role of pseudokinases in cancer

Zhang, H., Photiou, A., Grothey, A., Stebbing, J., & Giamas, G. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.017 · Cited by 40

FGFR3 Unliganded Dimer Stabilization by the Juxtamembrane Domain

Sarabipour, S., & Hristova, K. A. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.013 · Cited by 36

Regulation of Ack1 localization and activity by the amino-terminal SAM domain

Prieto-Echagüe, V., Gucwa, A. L., Brown, D. A., & Miller, W. T. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-42 · Cited by 35

Interaction of Rio1 Kinase with Toyocamycin Reveals a Conformational Switch That Controls Oligomeric State and Catalytic Activity

Kiburu, I., & LaRonde-LeBlanc, N. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037371 · Cited by 36

Rapid and accurate ranking of binding affinities of epidermal growth factor receptor sequences with selected lung cancer drugs

Wan, S., & Coveney, P. V. (2011) · Journal of The Royal Society Interface · doi:10.1098/rsif.2010.0609 · Cited by 36

Manipulating the lateral diffusion of surface-anchored EGF demonstrates that receptor clustering modulates phosphorylation levels

Stabley, D. R., Retterer, S. T., Marshall, S., & Salaita, K. S. (2013) · Integrative Biology · doi:10.1039/c3ib20239a · Cited by 36

Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy

Wang, Y., & Barth, P. (2015) · Nature Communications · doi:10.1038/ncomms8196 · Cited by 36

Surfactant protein D inhibits activation of non-small cell lung cancer-associated mutant EGFR and affects clinical outcomes of patients

Umeda, Y., Hasegawa, Y., Otsuka, M., Ariki, S., Takamiya, R., Saito, A., Uehara, Y., Saijo, H., Kuronuma, K., Chiba, H., et al. (2017) · Oncogene · doi:10.1038/onc.2017.253 · Cited by 36

Overexpression-mediated activation of MET in the Golgi promotes HER3/ERBB3 phosphorylation

Frazier, N. M., Brand, T. M., Gordan, J. D., Grandis, J. R., & Jura, N. (2018) · Oncogene · doi:10.1038/s41388-018-0537-0 · Cited by 37

Drug resistance in targeted cancer therapies with RAF inhibitors

Degirmenci, U., Yap, J., Sim, Y. R. M., Qin, S., & Hu, J. (2021) · Cancer Drug Resistance · doi:10.20517/cdr.2021.36 · Cited by 36

It Takes More than Two to Tango: Complex, Hierarchal, and Membrane-Modulated Interactions in the Regulation of Receptor Tyrosine Kinases

Kovács, T., Zákány, F., & Nagy, P. (2022) · Cancers · doi:10.3390/cancers14040944 · Cited by 37

Luciferase Fragment Complementation Imaging of Conformational Changes in the Epidermal Growth Factor Receptor

Yang, K. S., Ilagan, M. X. G., Piwnica-Worms, D. R., & PIKE, L. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808041200 · Cited by 36

Targeting the Dimerization of Epidermal Growth Factor Receptors with Small‐Molecule Inhibitors

Yang, R., Yang, K. S., PIKE, L. J., & Marshall, G. R. (2010) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2010.00986.x · Cited by 36

Conformational regulation of the EGFR kinase core by the juxtamembrane and C‐terminal tail: A molecular dynamics study

Mustafa, M., Mirza, A., & Kannan, N. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22862 · Cited by 36

Efficacy of an EGFR-Specific Peptide against EGFR-Dependent Cancer Cell Lines and Tumor Xenografts

Ahsan, A., Ramanand, S. G., Bergin, I. L., Zhao, L., Whitehead, C. E., Rehemtulla, A., Ray, D., Pratt, W. B., Lawrence, T. S., & Nyati, M. K. (2014) · Neoplasia · doi:10.1593/neo.14182 · Cited by 36

Contribution of EGFR and ErbB-3 Heterodimerization to the EGFR Mutation-Induced Gefitinib- and Erlotinib-Resistance in Non-Small-Cell Lung Carcinoma Treatments

Wang, D. D., Ma, L., Wong, M. P., Lee, V. H.-F., & Yan, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128360 · Cited by 35

Malfunctions within the Cbl interactome uncouple receptor tyrosine kinases from destructive transport

Đikić, I., & Schmidt, M. H. H. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.04.005 · Cited by 38

Src Mediates Cigarette Smoke–Induced Resistance to Tyrosine Kinase Inhibitors in NSCLC Cells

Filosto, S., Baston, D. S., Chung, S., Becker, C. R., & Goldkorn, T. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-1029 · Cited by 37

Rule-Based Modeling of Signal Transduction: A Primer

Sekar, J. A. P., & Faeder, J. R. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-833-7_9 · Cited by 35

Structural and functional characterization of KEOPS dimerization by Pcc1 and its role in t6A biosynthesis

Wan, L. C. K., Pillon, M. C., Thevakumaran, N., Sun, Y., Chakrabartty, A., Guarné, A., Kurinov, I. V., Durocher, D., & Sicheri, F. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw542 · Cited by 34

Structural insight into the binding mechanism of ATP to EGFR and L858R, and T790M and L858R/T790 mutants

Saldaña-Rivera, L., Bello, M., & Méndez-Luna, D. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1558112 · Cited by 34

Resolving the EGF-EGFR interaction characteristics through a multiple-temperature, multiple-inhibitor, real-time interaction analysis approach

Björkelund, H., Gedda, L., Malmqvist, M., & Andersson, K. (2012) · Molecular and Clinical Oncology · doi:10.3892/mco.2012.37 · Cited by 35

Carboxyl Group Footprinting Mass Spectrometry and Molecular Dynamics Identify Key Interactions in the HER2-HER3 Receptor Tyrosine Kinase Interface

Collier, T. S., Diraviyam, K., Monsey, J. D., Shen, W., Sept, D., & Bose, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474882 · Cited by 35

ErbB polymorphisms: insights and implications for response to targeted cancer therapeutics

Alaoui‐Jamali, M. A., Morand, G. B., & da Silva, S. D. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00017 · Cited by 34

Ligand-induced transmembrane conformational coupling in monomeric EGFR

Srinivasan, S., Regmi, R., Lin, X., Dreyer, C. A., Chen, X., Quinn, S. D., He, W., Coleman, M. A., Carraway, K. L., Zhang, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31299-z · Cited by 34

Similar but different: ligand-induced activation of the insulin and epidermal growth factor receptor families

Ward, C. W., & Lawrence, M. C. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.03.014 · Cited by 34

Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading

Kadry, Y. A., Huet-Calderwood, C., Simon, B., & Calderwood, D. (2018) · Journal of Cell Science · doi:10.1242/jcs.221184 · Cited by 34

Identification and antitumor activity of a novel inhibitor of the NIMA-related kinase NEK6

Donato, M. D., Righino, B., Filippetti, F., Battaglia, A., Petrillo, M., Pirolli, D., Scambia, G., Rosa, M. C. D., & Gallo, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-34471-y · Cited by 34

Structure–Activity Relationships of Hexahydrocyclopenta[c]quinoline Derivatives as Allosteric Inhibitors of CDK2 and EGFR

Carlino, L., Christodoulou, M. S., Restelli, V., Caporuscio, F., Foschi, F., Semrau, M. S., Costanzi, E., Tinivella, A., Pinzi, L., Presti, L. L., et al. (2018) · ChemMedChem · doi:10.1002/cmdc.201800687 · Cited by 36

BCAP31 drives TNBC development by modulating ligand-independent EGFR trafficking and spontaneous EGFR phosphorylation

Fu, W., Sun, H., Zhao, Y., Chen, M., Yang, X., Liu, Y., & Jin, W. (2019) · Theranostics · doi:10.7150/thno.35383 · Cited by 36

Role of EGF Receptor Regulatory Networks in the Host Response to Viral Infections

Carlin, C. R. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.820355 · Cited by 36

Structure and function of epigen, the last EGFR ligand

Schneider, M. R., & Yarden, Y. (2013) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.011 · Cited by 34

Molecular dynamics simulation reveals structural and thermodynamic features of kinase activation by cancer mutations within the epidermal growth factor receptor

Wan, S., & Coveney, P. V. (2011) · Journal of Computational Chemistry · doi:10.1002/jcc.21866 · Cited by 34

Behaviours of Medicago truncatula–Sinorhizobium meliloti Symbioses Under Osmotic Stress in Relation with the Symbiotic Partner Input: Effects on Nodule Functioning and Protection

Mhadhbi, H., Fotopoulos, V., Djébali, N., Polidoros, A. N., & Aouani, M. E. (2009) · Journal of Agronomy and Crop Science · doi:10.1111/j.1439-037x.2009.00361.x · Cited by 34

Quantitation of the Effect of ErbB2 on Epidermal Growth Factor Receptor Binding and Dimerization

Yu, L., Macdonald-Obermann, J. L., Westfall, C. S., Piwnica-Worms, D. R., & PIKE, L. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.373647 · Cited by 34

A Network of Hydrophobic Residues Impeding Helix αC Rotation Maintains Latency of Kinase Gcn2, Which Phosphorylates the α Subunit of Translation Initiation Factor 2

Gárriz, A., Qiu, H., Dey, M., Seo, E.-J., Dever, T. E., & Hinnebusch, A. G. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01446-08 · Cited by 34

HER3 as a Therapeutic Target in Cancer

Karachaliou, N., Lazzari, C., Verlicchi, A., Sosa, A. E., & Rosell, R. (2016) · BioDrugs · doi:10.1007/s40259-016-0205-2 · Cited by 34

Tyrosine Phosphorylation of ErbB4 is Enhanced by PSD95 and Repressed by Protein Tyrosine Phosphatase Receptor Type Z

Fujikawa, A., Chow, J. P. H., Shimizu, H., Fukada, M., Suzuki, R., & Noda, M. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm140 · Cited by 34

Hotspot Mutations in KIT Receptor Differentially Modulate Its Allosterically Coupled Conformational Dynamics: Impact on Activation and Drug Sensitivity

de Beauchêne, I. C., Allain, A., Panel, N., Laine, É., Trouvé, A., Dubreuil, P. C., & Tchertanov, L. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003749 · Cited by 36

Assessing the Accuracy of Two Enhanced Sampling Methods Using EGFR Kinase Transition Pathways: The Influence of Collective Variable Choice

Pan, A. C., Weinreich, T. M., Shan, Y., Scarpazza, D. P., & Shaw, D. E. (2014) · Journal of Chemical Theory and Computation · doi:10.1021/ct500223p · Cited by 33

Computational Approaches to Prioritize Cancer Driver Missense Mutations

Zhao, F., Zheng, L., Goncearenco, A., Panchenko, A. R., & Li, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072113 · Cited by 33

Temporal Modulation of HER2 Membrane Availability Increases Pertuzumab Uptake and Pretargeted Molecular Imaging of Gastric Tumors

Pereira, P. M. R., Mandleywala, K., Ragupathi, A., Carter, L. M., Goos, J. A. C. M., Janjigian, Y. Y., & Lewis, J. S. (2019) · Journal of Nuclear Medicine · doi:10.2967/jnumed.119.225813 · Cited by 33

Discoidin domain receptors: Micro insights into macro assemblies

Agarwal, G., Smith, A. W., & Jones, B. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.06.010 · Cited by 33

A conformational sensor based on genetic code expansion reveals an autocatalytic component in EGFR activation

Baumdick, M. E., Gelléri, M., Uttamapinant, C., Beránek, V., Chin, J. W., & Bastiaens, P. I. H. (2018) · Nature Communications · doi:10.1038/s41467-018-06299-7 · Cited by 33

Epidermal growth factor receptor (EGFR) tyrosine kinase inhibitors for the treatment of non-small cell lung cancer: a patent review (2014-present)

Sun, X., Xu, S., Yang, Z., Zheng, P., & Zhu, W. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2021.1860210 · Cited by 34

Discovery and optimization of 4-anilinoquinazoline derivatives spanning ATP binding site and allosteric site as effective EGFR-C797S inhibitors

Dou, D., Wang, J., Qiao, Y., Wumaier, G., Sha, W., Li, W., Mei, W., Yang, T., Zhang, C., He, H., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114856 · Cited by 33

Immunotherapeutic progress and application of bispecific antibody in cancer

Kang, J., Sun, T., & Zhang, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1020003 · Cited by 37

The Strength and Cooperativity of KIT Ectodomain Contacts Determine Normal Ligand-Dependent Stimulation or Oncogenic Activation in Cancer

Reshetnyak, A. V., Opatowsky, Y., Boggon, T. J., Folta‐Stogniew, E. J., Tomé, F., Lax, I., & Schlessinger, J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.021 · Cited by 33

The SH2 Domain Regulates c-Abl Kinase Activation by a Cyclin-Like Mechanism and Remodulation of the Hinge Motion

Dölker, N., Górna, M. W., Sutto, L., Torralba, A. S., Superti‐Furga, G., & Gervasio, F. L. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003863 · Cited by 33

Microtubules Accelerate the Kinase Activity of Aurora-B by a Reduction in Dimensionality

Noujaim, M. G., Bechstedt, S., Wieczorek, M., & Brouhard, G. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086786 · Cited by 32

Structural Analysis of ARC-Type Inhibitor (ARC-1034) Binding to Protein Kinase A Catalytic Subunit and Rational Design of Bisubstrate Analogue Inhibitors of Basophilic Protein Kinases

Lavõgina, D., Lust, M., Viil, I., König, N., Raidaru, G., Rogozina, J., Enkvist, E., Uri, A., & Bossemeyer, D. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800797n · Cited by 33

Molecular mechanisms of asymmetric RAF dimer activation

Jambrina, P. G., Bohuszewicz, O., Buchete, N., Kölch, W., & Rosta, E. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140025 · Cited by 33

Ack1: Activation and Regulation by Allostery

Gajiwala, K. S., Maegley, K. A., Ferre, R. A., He, Y.-A., & Yu, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053994 · Cited by 31

Profiling of protein–protein interactions via single-molecule techniques predicts the dependence of cancers on growth-factor receptors

Lee, H.-W., Choi, B., Kang, H. N., Kim, H., Min, A., Cha, M., Ryu, J. Y., Park, S., Sohn, J., Shin, K., et al. (2018) · Nature Biomedical Engineering · doi:10.1038/s41551-018-0212-3 · Cited by 32

Multisite EGFR phosphorylation is regulated by adaptor protein abundances and dimer lifetimes

Salazar-Cavazos, E., Nitta, C. F., Mitra, E. D., Wilson, B. S., Lidke, K. A., Hlavacek, W. S., & Lidke, D. S. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-09-0548 · Cited by 32

Investigating the Impact of Different Acrylamide (Electrophilic Warhead) on Osimertinib’s Pharmacological Spectrum by Molecular Mechanic and Quantum Mechanic Approach

Patel, H., Ahmad, I., Jadhav, H., Pawara, R. H., Lokwani, D. K., & Surana, S. J. (2020) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207323666201204125524 · Cited by 32

Regulation of Signaling from the Epidermal Growth Factor Family

Burgess, A. W. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04156 · Cited by 33

Oligo-Metastatic Cancers: Putative Biomarkers, Emerging Challenges and New Perspectives

Ottaiano, A., Santorsola, M., Circelli, L., Trotta, A. M., Izzo, F., Perri, F., Cascella, M., Sabbatino, F., Granata, V., Correra, M., et al. (2023) · Cancers · doi:10.3390/cancers15061827 · Cited by 32

Synthesis of novel mono- and bis-pyrazolylthiazole derivatives as anti-liver cancer agents through EGFR/HER2 target inhibition

Salem, M. E., Mahrous, E. M., Ragab, E. A., Nafie, M. S., & Dawood, K. M. (2023) · BMC Chemistry · doi:10.1186/s13065-023-00921-6 · Cited by 32

Molecular dynamics analysis of conserved hydrophobic and hydrophilic bond-interaction networks in ErbB family kinases

Shih, A., Telesco, S., Choi, S.-H., Lemmon, M. A., & Radhakrishnan, R. (2011) · Biochemical Journal · doi:10.1042/bj20101791 · Cited by 31

Anti-Proliferative Effect of Cytohesin Inhibition in Gefitinib-Resistant Lung Cancer Cells

Bill, A., Schmitz, A., König, K., Heukamp, L. C., Hannam, J. S., & Famulok, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041179 · Cited by 32

Regulation of EGFR trafficking and cell signaling by Sprouty2 and MIG6 in lung cancer cells

Walsh, A. M., & Lazzara, M. J. (2013) · Journal of Cell Science · doi:10.1242/jcs.123208 · Cited by 31

Carboxyl-Group Footprinting Maps the Dimerization Interface and Phosphorylation-induced Conformational Changes of a Membrane-associated Tyrosine Kinase

Zhang, H., Shen, W., Rempel, D. L., Monsey, J. D., Vidavsky, I., Gross, M. L., & Bose, R. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.005678 · Cited by 32

New trend in ligand-induced EGFR trafficking: A dual-mode clathrin-mediated endocytosis model

Zhou, Y., & Sakurai, H. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104503 · Cited by 31

Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors

Cai, K., Zhang, X., & Bai, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01035 · Cited by 31

Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer

Brown, B. P., Zhang, Y., Kim, S., Finneran, P., Yan, Y., Du, Z., Kim, J., Hartzler, A. L., Lenoue-Newton, M. L., Smith, A. W., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2206588119 · Cited by 31

EGF receptor modulates HEV entry in human hepatocytes

Schrader, J. A., Burkard, T. L., Brüggemann, Y., Gömer, A., Meister, T. L., Fu, R., Mehnert, A.-K., Thi, V. L. D., Behrendt, P., Durantel, D., et al. (2023) · Hepatology · doi:10.1097/hep.0000000000000308 · Cited by 31

EGFR as therapeutic target to develop new generation tyrosine kinase inhibitors against breast cancer: A critical review

Raju, R. M., Jeffin Joy, A., Raghavendra, N. M., Justin, A., & Kumar, B. R. P. (2024) · Results in Chemistry · doi:10.1016/j.rechem.2024.101490 · Cited by 33

Structural Model for p75NTR–TrkA Intracellular Domain Interaction: A Combined FRET and Bioinformatics Study

Iacaruso, M. F., Galli, S., Marti, M. A., Villalta, J. I., Estrin, D. A., Jares-Erijman, E. A., & Pietrasanta, L. I. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.022 · Cited by 31

β3 Integrin–EGF receptor cross-talk activates p190RhoGAP in mouse mammary gland epithelial cells

Balanis, N. G., Yoshigi, M., Wendt, M. K., Schiemann, W. P., & Carlin, C. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0700 · Cited by 30

Asymmetric kinase dimer formation is crucial for the activation of oncogenic EGFRvIII but not for ERBB3 phosphorylation

Kancha, R. K., von Bubnoff, N. C. C., & Duyster, J. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-39 · Cited by 31

Structural Basis of TPR-Mediated Oligomerization and Activation of Oncogenic Fusion Kinases

Pal, K., Bandyopadhyay, A., Zhou, X. E., Xu, Q., Marciano, D. P., Brunzelle, J. S., Yerrum, S., Griffin, P. R., Woude, G. V., Melcher, K., et al. (2017) · Structure · doi:10.1016/j.str.2017.04.015 · Cited by 35

Single-Molecule Rotation for EGFR Conformational Dynamics in Live Cells

Park, Y., Shin, S., Jin, H., Park, J., Hong, Y., Choi, J., Jung, B., Song, H., & Seo, D. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09037 · Cited by 31

Congenital myasthenic syndrome due to mutations in MUSK suggests that the level of MuSK phosphorylation is crucial for governing synaptic structure

Cruz, P. M. R., Cossins, J., Cheung, J., Maxwell, S., Jayawant, S., Herbst, R., Waithe, D., Kornev, A. P., Palace, J. A., & Beeson, D. (2019) · Human Mutation · doi:10.1002/humu.23949 · Cited by 31

Genetic trajectory and immune microenvironment of lung-specific oligometastatic colorectal cancer

Ottaiano, A., Circelli, L., Lombardi, A., Scala, S., Martucci, N., Galon, J., Buonanno, M., Scognamiglio, G., Botti, G., Hermitte, F., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2480-6 · Cited by 32

SpyPhage: A Cell-Free TXTL Platform for Rapid Engineering of Targeted Phage Therapies

Liyanagedera, S. B. W., Williams, J., Wheatley, J. P., Biketova, A. Y., Hasan, M., Sagona, A. P., Purdy, K. J., Puxty, R. J., Fehér, T., & Kulkarni, V. V. (2022) · ACS Synthetic Biology · doi:10.1021/acssynbio.2c00244 · Cited by 31

Evidence for extended YFP-EGFR dimers in the absence of ligand on the surface of living cells

Kozer, N., Henderson, C. A., Jackson, J. T., Nice, E. C., Burgess, A. W., & Clayton, A. H. A. (2011) · Physical Biology · doi:10.1088/1478-3975/8/6/066002 · Cited by 31

Conformational dynamics of the EGFR kinase domain reveals structural features involved in activation

Papakyriakou, A., Vourloumis, D., Tzortzatou-Stathopoulou, F. F., & Karpusas, M. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22353 · Cited by 31

Inhibition of Receptor Dimerization as a Novel Negative Feedback Mechanism of EGFR Signaling

Kluba, M., Engelborghs, Y., Hofkens, J., & Mizuno, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139971 · Cited by 31

Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation

Karabadzhak, A. G., Petti, L. M., Barrera, F. N., Edwards, A. P. B., Moya-Rodríguez, A., Polikanov, Y. S., Freites, J. A., Tobias, D. J., Engelman, D. M., & DiMaio, D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705622114 · Cited by 31

Distinct ErbB-2–Coupled Signaling Pathways Promote Mammary Tumors with Unique Pathologic and Transcriptional Profiles

Schade, B., Lam, S. H. L., Cernea, D. D., Sanguin‐Gendreau, V., Cardiff, R. D., Jung, B. L., Hallett, M. T., & Muller, W. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4724 · Cited by 30

Molecular determinants of drug-specific sensitivity for epidermal growth factor receptor (EGFR) exon 19 and 20 mutants in non-small cell lung cancer

Tsigelny, I. F., Wheler, J. J., Greenberg, J. P., Kouznetsova, V. L., Stewart, D. J., Bazhenova, L., & Kurzrock, R. (2015) · Oncotarget · doi:10.18632/oncotarget.3472 · Cited by 30

Making NSCLC Crystal Clear: How Kinase Structures Revolutionized Lung Cancer Treatment

Vilachã, J. F., Mitchel, S. C., Akele, M. Z., Evans, S., & Groves, M. R. (2020) · Crystals · doi:10.3390/cryst10090725 · Cited by 29

Integrative annotation and knowledge discovery of kinase post-translational modifications and cancer-associated mutations through federated protein ontologies and resources

Huang, L., ROSS, K. E., Baffi, T. R., Drabkin, H., Kochut, K., Ruan, Z., D’Eustachio, P., McSkimming, D. I., Arighi, C. N., Chen, C., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-24457-1 · Cited by 30

A Brief History of Single-Particle Tracking of the Epidermal Growth Factor Receptor

Clarke, D. T., & Martin-Fernandez, M. L. (2019) · Methods and Protocols · doi:10.3390/mps2010012 · Cited by 30

More than the sum of the parts: Toward full‐length receptor tyrosine kinase structures

Diwanji, D. C., Thaker, T. M., & Jura, N. (2019) · IUBMB Life · doi:10.1002/iub.2060 · Cited by 30

Research Highlights

(2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb0706-575

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 48

EGF Receptor Activation: Push Comes to Shove

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

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