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

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

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Untangling the ErbB signalling network

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

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

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The Conformational Plasticity of Protein Kinases

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

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

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

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

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Dissecting the molecular recognition of dual lapatinib derivatives for EGFR/HER2

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Anti-EGFR Binding Nanobody Delivery System to Improve the Diagnosis and Treatment of Solid Tumours

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A tale of the epidermal growth factor receptor: The quest for structural resolution on cells

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Constitutive asymmetric dimerization drives oncogenic activation of epidermal growth factor receptor carboxyl-terminal deletion mutants

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Yet another “active” pseudokinase, Erb3

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ERBB2 Overexpression Establishes ERBB3-Dependent Hypersensitivity of Breast Cancer Cells to Withaferin A

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TRAF4 binds to the juxtamembrane region of EGFR directly and promotes kinase activation

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Structural analysis of the EGFR TK domain and potential implications for EGFR targeted therapy

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Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography

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Allostery

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Autoinhibitory structure of preligand association state implicates a new strategy to attain effective DR5 receptor activation

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Conserved regulatory motifs in the juxtamembrane domain and kinase N-lobe revealed through deep mutational scanning of the MET receptor tyrosine kinase domain

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Tilting the Scales toward EGFR Mutant Selectivity: Expanding the Scope of Bivalent “Type V” Kinase Inhibitors

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Phosphatidylinositol 4,5-bisphosphate drives the formation of EGFR and EphA2 complexes

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Hydrogen Exchange Mass Spectrometry of Functional Membrane-Bound Chemotaxis Receptor Complexes

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Characterization of Growth Suppressive Functions of a Splice Variant of Cyclin D2

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A new Rac/PAK/GC/cGMP signaling pathway

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Predicting Efficacy and Toxicity in the Era of Targeted Therapy: Focus on Anti-EGFR and Anti-VEGF Molecules

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Characterizing Large-Scale Receptor Clustering on the Single Cell Level: A Comparative Plasmon Coupling and Fluorescence Superresolution Microscopy Study

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Expression, purification, and characterization of the native intracellular domain of human epidermal growth factor receptors 1 and 2 in Escherichia coli

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Expression, intracellular localization, and mutation of EGFR in conjunctival squamous cell carcinoma and the association with prognosis and treatment

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A small molecule inhibitor of HER3: a proof-of-concept study

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Discovery of Cyclic Peptidomimetic Ligands Targeting the Extracellular Domain of EGFR

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Hydrophobic Interaction between the SH2 Domain and the Kinase Domain Is Required for the Activation of Csk

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Probing the Heterogeneity of Protein Kinase Activation in Cells by Super-resolution Microscopy

Zhang, R., Fruhwirth, G. O., Coban, O., Barrett, J. J. E., Burgoyne, T., Lee, S. H., Simonson, P. D., Baday, M., Kholodenko, B. Ν., Futter, C. E., et al. (2016) · ACS Nano · doi:10.1021/acsnano.6b05356 · Cited by 16

Overcoming TKI resistance in fusion-driven NSCLC: new generation inhibitors and rationale for combination strategies

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A Structural Insight Into Two Important ErbB Receptors (EGFR and HER2) and Their Relevance to Non‐Small Cell Lung Cancer

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Sorting nexin-dependent therapeutic targeting of oncogenic epidermal growth factor receptor

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Targeted treatment of head and neck squamous-cell carcinoma: potential of lapatinib

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Targeted Cancer Therapy: Promise and Reality

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Anti-EGFR Agents: Current Status, Forecasts and Future Directions

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The EGF receptor inhibits the signaling of dopamine D 3 receptor through the phosphorylation of GRK2 on tyrosine residues

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Harnessing Integrative Omics to Facilitate Molecular Imaging of the Human Epidermal Growth Factor Receptor Family for Precision Medicine

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Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random

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EGFR transactivates RON to drive oncogenic crosstalk

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Pharmacokinetics, pharmacodynamics and clinical efficacy of pertuzumab in breast cancer therapy

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Co-Conserved Features Associated with cis Regulation of ErbB Tyrosine Kinases

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Inhibition of migration and invasion of colorectal cancer cells via deletion of Rac1 with RNA interference

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Identification of mutant alleles ofJAK3in pediatric patients with acute lymphoblastic leukemia

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Helicobacter pylori Induces Serine Phosphorylation of EGFR via Novel TAK1–p38 Activation Pathway in an HB‐EGF‐Independent Manner

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Two-Dimensional Trap for Ultrasensitive Quantification of Transient Protein Interactions

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Inhibition of tamoxifen's therapeutic effects by emodin in estrogen receptor-positive breast cancer cell lines

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Antiviral properties of placental growth factors: A novel therapeutic approach for COVID-19 treatment

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Multiomics Reveals Ectopic ATP Synthase Blockade Induces Cancer Cell Death via a lncRNA-mediated Phospho-signaling Network

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Effect of EGFR antagonists gefitinib (Iressa) and C225 (Cetuximab) on MnSOD-plasmid liposome transgene radiosensitization of a murine squamous cell carcinoma cell line.

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Palmitoylation of the EGF Receptor Impairs Signal Transduction and Abolishes High-Affinity Ligand Binding

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Updates on Inflammatory Molecular Pathways Mediated by ADAM17 in Autoimmunity

Sisto, M., & Lisi, S. (2024) · Cells · doi:10.3390/cells13242092 · Cited by 14

Structural insights into the non-inhibitory mechanism of the anti-EGFR EgB4 nanobody

Zeronian, M. R., Doulkeridou, S., Henegouwen, P. M. P. V. B. E., & Janssen, B. J. C. (2022) · BMC Molecular and Cell Biology · doi:10.1186/s12860-022-00412-x · Cited by 16

Structural Analysis of the Macrocyclic Inhibitor BI‐4020 Binding to EGFR Kinase

Beyett, T. S., Rana, J. K., Schaeffner, I. K., Heppner, D. E., & Eck, M. J. (2024) · ChemMedChem · doi:10.1002/cmdc.202300343 · Cited by 14

In silico exploration of anticancer plant phytochemicals for EGFR-targeted lung cancer therapy

Dipa, C. D., Hossain, S., Chy, M. M. K., Rahman, M. S. F., Kayes, T., Easha, A. M., Moin, A. T., Vakare, S. N., Patil, R. B., & Sarkar, B. K. (2025) · Scientific Reports · doi:10.1038/s41598-025-10412-4 · Cited by 15

Shedding light on complexity of protein–protein interactions in cancer

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Rational Computational Design of Fourth-Generation EGFR Inhibitors to Combat Drug-Resistant Non-Small Cell Lung Cancer

Park, H., Jung, H.-Y., Kim, K., Kim, M., & Hong, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239323 · Cited by 14

Building protein networks in synthetic systems from the bottom-up

Shim, J., Zhou, C., Gong, T., Iserlis, D. A., Linjawi, H. A., Wong, M. S., Pan, T., & Tan, C. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107753 · Cited by 14

Threonine phosphorylation regulates the molecular assembly and signaling of EGFR in cooperation with membrane lipids

Maeda, R., Tamagaki-Asahina, H., Sato, T., Yanagawa, M., & Sako, Y. (2022) · Journal of Cell Science · doi:10.1242/jcs.260355 · Cited by 15

In silico screening of chalcone derivatives as promising EGFR-TK inhibitors for the clinical treatment of cancer

Mathpal, S., Joshi, T., Sharma, P., Maiti, P., Nand, M., Pande, V., & Chandra, S. (2023) · 3 Biotech · doi:10.1007/s13205-023-03858-8 · Cited by 14

EGFR/HER-2 inhibitors: synthesis, biological evaluation and 3D-QSAR analysis of dihydropyridine-containing thiazolinone derivatives

Ren, Y.-J., Wang, Z., Zhang, X., Qiu, H., Wang, P., Gong, H., Jiang, A.-Q., & Zhu, H. (2015) · RSC Advances · doi:10.1039/c4ra10606g · Cited by 14

Molecular modeling of ErbB4/HER4 kinase in the context of the HER4 signaling network helps rationalize the effects of clinically identified HER4 somatic mutations on the cell phenotype

Telesco, S., Vadigepalli, R., & Radhakrishnan, R. (2013) · Biotechnology Journal · doi:10.1002/biot.201300022 · Cited by 14

Conversion of MIG6 peptide from the nonbinder to binder of lung cancer-related EGFR by phosphorylation and cyclization

Li, N., & Wei, M. (2016) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2016.1200058 · Cited by 14

Resistance to Therapy

Rivera, G. A., & Wakelee, H. A. (2016) · Cancer treatment and research · doi:10.1007/978-3-319-40389-2_9 · Cited by 14

Molecular dynamics simulation analysis of the effect of T790M mutation on epidermal growth factor receptor protein architecture in non-small cell lung carcinoma

Peng, X., Wang, J., & Zhang, W. (2017) · Oncology Letters · doi:10.3892/ol.2017.6387 · Cited by 14

Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23

Liu, L., Thaker, T. M., Freed, D. M., Frazier, N. M., Malhotra, K., Lemmon, M. A., & Jura, N. (2018) · Structure · doi:10.1016/j.str.2017.12.012 · Cited by 14

Reduced Expression of Epidermal Growth Factor Receptors in Rat Liver During Aging

Kamat, A., Ghosh, P., Glover, R., Zhu, B., Yeh, C., Choudhury, G. G., & Katz, M. S. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.7.683 · Cited by 14

Profiling Epidermal Growth Factor Receptor and Heregulin Receptor 3 Heteromerization Using Receptor Tyrosine Kinase Heteromer Investigation Technology

Ayoub, M. A., See, H. B., Seeber, R. M., Armstrong, S. P., & Pfleger, K. D. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064672 · Cited by 14

Profiling and Optimizing Targeted Covalent Inhibitors through EGFR-Guided Studies

Damghani, T., Chitnis, S. P., Abidakun, O. A., Patel, K. B., Lin, K. S., Ouellette, E. A., Lantry, A. M., & Heppner, D. E. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01661 · Cited by 13

Multi‐Target Rational Design and Synthesis of Some 2‐Quinolinone Antitumor Candidates Downregulating the Expression of EGFR, VEGFR‐2, and Telomerase With Apoptotic Potential

El‐Helw, E. A. E., Mousa, M. H. A., Ghareeb, E. A., Mahmoud, N. F. H., Sharaky, M. M., El‐Bordany, E. A. A., Khatib, A. O. A., Soliman, E.-S. A., Alnajjar, R. A., & Al-Karmalawy, A. A. (2025) · Drug Development Research · doi:10.1002/ddr.70176 · Cited by 13

The immunoglobulin‐like domain of neuregulins potentiates ErbB3/HER3 activation and cellular proliferation

Centa, A., Barrueco, R. R., Montero, J. C., & Pandiella, A. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12310 · Cited by 13

NH125 Sensitizes Staphylococcus aureus to Cell Wall-Targeting Antibiotics through the Inhibition of the VraS Sensor Histidine Kinase

Bhattarai, S., Marsh, L., Knight, K., Ali, L., Gomez, A., Sunderhaus, A., & Aziz, M. H. A. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.04861-22 · Cited by 13

Better safe than sorry: dual targeting antibodies for cancer immunotherapy

Schoenfeld, K., Harwardt, J., & Kolmar, H. (2024) · Biological Chemistry · doi:10.1515/hsz-2023-0329 · Cited by 13

Extracellular domain mutations of the EGF receptor differentially modulate high-affinity and low-affinity responses to EGF receptor ligands

Macdonald-Obermann, J. L., & PIKE, L. J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105763 · Cited by 13

Targeting mutant EGFR in non-small cell lung cancer in the context of cell adaptation and resistance

Roberts, S. K., Galgadas, I., Clarke, D. T., Zanetti-Domingues, L. C., Gervasio, F. L., & Martin-Fernandez, M. L. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104407 · Cited by 14

Ab Initio Modeling and Experimental Assessment of Janus Kinase 2 (JAK2) Kinase-Pseudokinase Complex Structure

Wan, X., Ma, Y., McClendon, C. L., Huang, L. J.-S., & Huang, N. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003022 · Cited by 13

A pickup in pseudokinase activity

Dar, A. C. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130110 · Cited by 13

Structural Characterization of the Self-Association of the Death Domain of p75NTR

Qu, Q., Chen, J., Wang, Y., Gui, W., Wang, L., Fan, Z., & Jiang, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057839 · Cited by 13

Truncation, modification, and optimization of MIG6segment 2 peptide to target lung cancer-related EGFR

Yu, X., Yang, R., & Leng, C.-J. (2016) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2016.02.015 · Cited by 13

A Catalytically Disabled Double Mutant of Src Tyrosine Kinase Can Be Stabilized into an Active-Like Conformation

Meng, Y., Ahuja, L. G., Kornev, A. P., Taylor, S. S., & Roux, B. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.01.019 · Cited by 13

Crystal Structures of Human CaMKIα Reveal Insights into the Regulation Mechanism of CaMKI

Zha, M., Zhong, C., Ou, Y., Han, L., Wang, J., & Ding, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044828 · Cited by 13

Pseudokinase drug intervention: a potentially poisoned chalice

Claus, J., Cameron, A. J. M., & Parker, P. J. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130078 · Cited by 13

Chemotherapy Drug Response to the L858R‐induced Conformational Change of EGFR Activation Loop in Lung Cancer

Ding, X., Liu, X., Song, X., & Yao, J. (2016) · Molecular Informatics · doi:10.1002/minf.201600088 · Cited by 13

Epidermal growth factor receptors containing a single tyrosine in their C-terminal tail bind different effector molecules and are signaling-competent

Gill, K., Macdonald-Obermann, J. L., & PIKE, L. J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.802553 · Cited by 13

Pan-HER-targeted approach for cancer therapy: Mechanisms, recent advances and clinical prospect

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Mutation and drug-specific intracellular accumulation of EGFR predict clinical responses to tyrosine kinase inhibitors

de Wit, M., Gao, Y., Mercieca, D., de Heer, I. J., Valkenburg, B., van Royen, M. E., Aerts, J. G. J. V., Smitt, P. A. E. S., & French, P. J. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102796 · Cited by 13

Synergistic Activation of p21-activated Kinase 1 by Phosphatidylinositol 4,5-Bisphosphate and Rho GTPases

Malecka, K. A., Szentpétery, Z., & Peterson, J. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.428904 · Cited by 14

Molecular Oncology of Breast Cancer

Ioan, A.-M., Klobocista, M. M., Shirazi, S., & Press, M. F. (2009) · Elsevier eBooks · doi:10.1016/b978-1-4160-5221-0.00028-0 · Cited by 13

SCHOOL Model and New Targeting Strategies

Sigalov, A. B. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-09789-3_20 · Cited by 15

Metabolic Phenotypes, Dependencies, and Adaptation in Lung CancerPreprint

DeNicola, G. M., & Shackelford, D. B. (2021) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a037838 · Cited by 13

The clathrin adaptor complex-1 and Rab12 regulate post-golgi trafficking of WT epidermal growth factor receptor (EGFR)

Wang, J., Lau, P. K., Li, C. W., & Guo, Y. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.102979 · Cited by 14

Trans-activating mutations of the pseudokinase ERBB3

Koivu, M. K. A., Chakroborty, D., Airenne, T. T., Johnson, M. S., Kurppa, K. J., & Elenius, K. (2024) · Oncogene · doi:10.1038/s41388-024-03070-9 · Cited by 12

Bilateral regulation of EGFR activity and local PI(4,5)P2 dynamics in mammalian cells observed with superresolution microscopy

Abe, M., Yanagawa, M., Hiroshima, M., Kobayashi, T., & Sako, Y. (2024) · eLife · doi:10.7554/elife.101652 · Cited by 12

EGFR lung cancer mutants get specialized

Littlefield, P., & Jura, N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314719110 · Cited by 12

Homo- and Heteroassociations Drive Activation of ErbB3

Váradi, T., Schneider, M. C., Sevcsik, E., Kiesenhofer, D., Baumgart, F., Batta, G., Kovács, T., Platzer, R., Huppa, J. B., Szöllõsi, J., et al. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.10.001 · Cited by 12

Click Conjugation of Boron Dipyrromethene (BODIPY) Fluorophores to EGFR-Targeting Linear and Cyclic Peptides

Williams, T. M., Kaufman, N. E. M., Zhou, Z., Singh, S. S., Jois, S. D. S., & Vicente, M. G. H. (2021) · Molecules · doi:10.3390/molecules26030593 · Cited by 12

Dimerization and autophosphorylation of the MST family of kinases are controlled by the same set of residues

Weingartner, K. A., Tran, T. T., Tripp, K. W., & Kavran, J. M. (2023) · Biochemical Journal · doi:10.1042/bcj20230067 · Cited by 12

To Investigate Growth Factor Receptor Targets and Generate Cancer Targeting Inhibitors

Basu, D., Pal, R., Sarkar, M., Barma, S., Halder, S., Roy, H., Nandi, S., & Samadder, A. (2023) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266261150231110053650 · Cited by 12

Liposome‐Mediated Assembly of Receptor Signaling Complexes

Montefusco, D. J., Asinas, A. E., & Weis, R. M. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)23012-5 · Cited by 12

Regulation of JAK2 Activation by Janus Homology 2: Evidence from Molecular Dynamics Simulations

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Insight into the recognition patterns of the ErbB receptor family transmembrane domains: heterodimerization models through molecular dynamics search

Soumana, O. S., Garnier, N., & Genest, M. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0293-0 · Cited by 12

PhotoGate microscopy to track single molecules in crowded environments

Belyy, V., Shih, S.-M., Bandaria, J. N., Huang, Y., Lawrence, R. E., Zoncu, R., & Yıldız, A. (2017) · Nature Communications · doi:10.1038/ncomms13978 · Cited by 12

Computational analysis of receptor tyrosine kinase inhibitors and cancer metabolism: implications for treatment and discovery of potential therapeutic signatures

Li, J., Halfter, K., Zhang, M., Saad, C., Xu, K. L., Bauer, B., Huang, Y., Shi, L., & Mansmann, U. (2019) · BMC Cancer · doi:10.1186/s12885-019-5804-0 · Cited by 12

Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment

Viegas, A., Yin, D. M., Borggräfe, J., Viennet, T., Falke, M., Schmitz, A., Famulok, M., & Etzkorn, M. (2019) · Structure · doi:10.1016/j.str.2019.11.001 · Cited by 12

Increasing kinase domain proximity promotes MST2 autophosphorylation during Hippo signaling

Tran, T. T., Mitra, J., Ha, T., & Kavran, J. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015723 · Cited by 13

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 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