Structural basis of mutant-selectivity and drug-resistance related to CO-1686

Features and development of Coot

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<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

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<i>Phaser</i> crystallographic software

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Cancer Statistics, 2017.

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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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<i>EGFR</i> Mutations in Lung Cancer: Correlation with Clinical Response to Gefitinib Therapy

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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PRODRG: a tool for high-throughput crystallography of protein–ligand complexes

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Scaling and assessment of data quality

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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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Genotypic and Histological Evolution of Lung Cancers Acquiring Resistance to EGFR Inhibitors

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Epidermal growth factor receptor mutations in lung cancer

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Lung Cancer

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AZD9291, an Irreversible EGFR TKI, Overcomes T790M-Mediated Resistance to EGFR Inhibitors in Lung Cancer

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HKL -3000: the integration of data reduction and structure solution – from diffraction images to an initial model in minutes

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The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

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AZD9291 in EGFR Inhibitor–Resistant Non–Small-Cell Lung Cancer

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Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

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Novel mutant-selective EGFR kinase inhibitors against EGFR T790M

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Afatinib versus placebo for patients with advanced, metastatic non-small-cell lung cancer after failure of erlotinib, gefitinib, or both, and one or two lines of chemotherapy (LUX-Lung 1): a phase 2b/3 randomised trial

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Novel D761Y and Common Secondary T790M Mutations in Epidermal Growth Factor Receptor–Mutant Lung Adenocarcinomas with Acquired Resistance to Kinase Inhibitors

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Rociletinib in <i>EGFR</i>-Mutated Non–Small-Cell Lung Cancer

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Discovery of a Mutant-Selective Covalent Inhibitor of EGFR that Overcomes T790M-Mediated Resistance in NSCLC

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Analysis of Epidermal Growth Factor Receptor Gene Mutation in Patients with Non–Small Cell Lung Cancer and Acquired Resistance to Gefitinib

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The Allelic Context of the C797S Mutation Acquired upon Treatment with Third-Generation EGFR Inhibitors Impacts Sensitivity to Subsequent Treatment Strategies

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Neratinib, an Irreversible Pan-ErbB Receptor Tyrosine Kinase Inhibitor: Results of a Phase II Trial in Patients With Advanced Non–Small-Cell Lung Cancer

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EGFR Mutations and Resistance to Irreversible Pyrimidine-Based EGFR Inhibitors

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Activating Mutations in the Tyrosine Kinase Domain of the Epidermal Growth Factor Receptor Are Associated with Improved Survival in Gefitinib-Treated Chemorefractory Lung Adenocarcinomas

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EGFR mutation detection in NSCLC—assessment of diagnostic application and recommendations of the German Panel for Mutation Testing in NSCLC

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In Vitro and In Vivo Characterization of Irreversible Mutant-Selective EGFR Inhibitors That Are Wild-Type Sparing

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Routine EGFR Molecular Analysis in Non-Small-Cell Lung Cancer Patients is Feasible: Exons 18–21 Sequencing Results of 753 Patients and Subsequent Clinical Outcomes

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Screening for EGFR and KRAS mutations in non-small cell lung carcinomas using DNA extraction by hydrothermal pressure coupled with PCR-based direct sequencing.

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Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

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Emerging strategies to overcome resistance to third-generation EGFR inhibitors

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Structural Insight and Development of EGFR Tyrosine Kinase Inhibitors

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L718Q mutant EGFR escapes covalent inhibition by stabilizing a non-reactive conformation of the lung cancer drug osimertinib

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Crystal structure of EGFR T790M/C797S/V948R in complex with EAI045

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A sulfonyl fluoride derivative inhibits EGFRL858R/T790M/C797S by covalent modification of the catalytic lysine

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HOTAIR induces EGFR-TKIs resistance in non-small cell lung cancer through epithelial-mesenchymal transition

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Structural insights into drug development strategy targeting EGFR T790M/C797S

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Discovery of a Highly Potent and Broadly Effective Epidermal Growth Factor Receptor and HER2 Exon 20 Insertion Mutant Inhibitor

Jang, J., Son, J., Park, E., Kosaka, T., Saxon, J. A., Clercq, D. J. H. D., Choi, H. G., Tanizaki, J., Eck, M. J., Janne, P. A., et al. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201805187 · Cited by 31 · see citing works

Design and Synthesis of Proteolysis Targeting Chimeras (Protacs) as an Egfr Degrader Based on Co-1686

Li, Q., Guo, Q., Wang, S., Wan, S., Li, Z., Zhang, J., & Wu, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114455 · Cited by 30 · see citing works

Synthesis and Fundamental Evaluation of Radioiodinated Rociletinib (CO-1686) as a Probe to Lung Cancer with L858R/T790M Mutations of Epidermal Growth Factor Receptor (EGFR)

Fawwaz, M., Mishiro, K., Nishii, R., Sawazaki, I., Shiba, K., Kinuya, S., & Ogawa, K. (2020) · Molecules · doi:10.3390/molecules25122914 · Cited by 28 · see citing works

Leak Proof PDBBind: A Reorganized Data Set of Protein–Ligand Complexes for More Generalizable Binding Affinity Prediction

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Leak Proof PDBBind: A Reorganized Dataset of Protein-Ligand Complexes for More Generalizable Binding Affinity PredictionPreprint

Li, J., Guan, X., Zhang, O., Sun, K., Wang, Y., Bagni, D., & Head-Gordon, T. L. (2023) · PubMed · doi:10.48550/arxiv.2308.09639 · Cited by 22 · see citing works

Recent advances in the design of small molecular drugs with acrylamides covalent warheads

Liang, L., Zhang, Z., You, Q., & Guo, X. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117902 · Cited by 19 · see citing works

Molecular dynamics, MM/PBSA and in vitro validation of a novel quinazoline-based EGFR tyrosine kinase inhibitor identified using structure-based in silico screening

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Deuterated Curcuminoids: Synthesis, Structures, Computational/Docking and Comparative Cell Viability Assays against Colorectal Cancer

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How Different Substitution Positions of F, Cl Atoms in Benzene Ring of 5-Methylpyrimidine Pyridine Derivatives Affect the Inhibition Ability of EGFRL858R/T790M/C797S Inhibitors: A Molecular Dynamics Simulation Study

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A Radiobrominated Tyrosine Kinase Inhibitor for EGFR with L858R/T790M Mutations in Lung Carcinoma

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Design, synthesis, and molecular docking study of novel quinoline‐based bis‐chalcones as potential antitumor agents

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Advances in HER2-Targeted Therapies: From monoclonal antibodies to dual inhibitors developments in cancer treatment

Bhagyalalitha, M., Akshatha, H. S., Kumar, S. A., Singh, M., Pujar, K. G., Bidye, D. P., & Pujar, G. V. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107695 · Cited by 14 · see citing works

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 · see citing works

To Investigate Growth Factor Receptor Targets and Generate Cancer Targeting Inhibitors

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Synthesis and evaluation of a rociletinib analog as prospective imaging double mutation L858R/T790M in non-small cell lung cancer

Fawwaz, M., Mishiro, K., Purwono, B., Nishii, R., & Ogawa, K. (2023) · Journal of Pharmacy & Pharmacognosy Research · doi:10.56499/jppres23.1743_12.2.231 · Cited by 12 · see citing works

Resistor: An algorithm for predicting resistance mutations via Pareto optimization over multistate protein design and mutational signatures

Guerin, N., Feichtner, A., Stefan, E., Kaserer, T., & Donald, B. R. (2022) · Cell Systems · doi:10.1016/j.cels.2022.09.003 · Cited by 9 · see citing works

Structural elements that enable specificity for mutant EGFR kinase domains with next-generation small-molecule inhibitors

Damghani, T., Wittlinger, F., Beyett, T. S., Eck, M. J., Laufer, S., & Heppner, D. E. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.03.013 · Cited by 9 · see citing works

Synthesis and initial in vitro evaluation of olmutinib derivatives as prospective imaging probe for non-small cell lung cancer

Fawwaz, M., Mishiro, K., Arwansyah, A., Nishii, R., & Ogawa, K. (2023) · Bioimpacts · doi:10.34172/bi.2023.27774 · Cited by 6 · see citing works

Design, preparation and biological evaluation of new Rociletinib-inspired analogs as irreversible EGFR inhibitors to treat non-small-cell-lung cancer

Konsue, A., Lamtha, T., Gleeson, D., Jones, D. J. L., Britton, R. G., Pickering, J., Choowongkomon, K., & Gleeson, M. P. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117906 · Cited by 5 · see citing works

Discovery of a Highly Potent and Broadly Effective Epidermal Growth Factor Receptor and HER2 Exon 20 Insertion Mutant Inhibitor

Jang, J., Son, J., Park, E., Kosaka, T., Saxon, J. A., Clercq, D. J. H. D., Choi, H. G., Tanizaki, J., Eck, M. J., Janne, P. A., et al. (2018) · Angewandte Chemie · doi:10.1002/ange.201805187 · Cited by 5 · see citing works

Molecular dynamics simulation and free energy analysis of EGFR resistance mutations: implications for the design of novel inhibitors

Wu, H., Chen, H., Xia, X., Liu, Y., Zhang, M., & Dong, J. (2025) · New Journal of Chemistry · doi:10.1039/d5nj01567g · Cited by 4 · see citing works

Covalent Epidermal Growth Factor Receptor (EGFR) Inhibitors in Targeted Therapy of Drug-Resistant Non-Small Cell Lung Cancer (A Review)

Shvetsov, A. B., & Semenov, A. (2024) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162024060347 · Cited by 3 · see citing works

Probing the Effect of Protein and Inhibitor Conformational Flexibility on the Reaction of Rocelitinib-Like Covalent Inhibitors of Epidermal Growth Factor Receptor. A Quantum Mechanics/Molecular Mechanics Study

Kaewkham, O., Gleeson, D., Fukasem, P., Santatiwongchai, J., Jones, D. J. L., Britton, R. G., & Gleeson, M. P. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01985 · Cited by 3 · see citing works

A Paradigm Shift in Experimental Biochemistry: A Priori Estimation of Physical Parameters of Biomolecules

Kulikov, K. G., Koshlan, T., & Golovitsky, A. P. (2023) · Biophysical Reviews and Letters · doi:10.1142/s1793048023500017 · Cited by 2 · see citing works

A Grid Map Based Approach to Identify Nonobvious Ligand Design Opportunities in 3D Protein Structure Ensembles

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Computationally guided design of N4-(2-methyl-2H-indazol-6-yl)-N2-phenylpyrimidine-2,4-diamine inhibitors of EGFR kinase targeting Cys797

Konsue, A., Gleeson, D., Choowongkomon, K., Jones, D. J. L., Hannanta‐anan, P., Britton, R. G., & Gleeson, M. P. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118544 · Cited by 1 · see citing works

Synthesis, radiolabeling, and evaluation of a 68Ga-labeled tyrosine kinase inhibitor for detecting EGFRT790M mutations in vivo

Xie, J., Xu, W., Deng, H., Wu, X., & Zhu, J. (2026) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2026.1741512 · Cited by 1 · see citing works

Resistor: an algorithm for predicting resistance mutations using Pareto optimization over multistate protein design and mutational signaturesPreprint

Guerin, N., Feichtner, A., Stefan, E., Kaserer, T., & Donald, B. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.18.476733 · Cited by 1 · see citing works

Analysis to determine the effect of mutations on binding to small chemical molecules

Koshlan, T. V., & Kulikov, K. G. (2022) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720022400030

Design and Synthesis of Proteolysis Targeting Chimeras (Protacs) as an Egfr Degrader Based on Co-1686Preprint

Wu, X.-Y., Li, Q., Guo, Q., Wang, S., Wan, S., Li, Z., & Zhang, J. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4051300

A Protein-Ligand Interaction-focused 3D Molecular Generative Framework for Generalizable Structure-based Drug DesignPreprint

Zhung, W., Kim, H., & Kim, W. Y. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-jsjwx

Computational Screening of Indole Metabolites Targeting EGFR Wild‐Type and Mutant Proteins Using Molecular Docking and Molecular Dynamics Simulations

Shukla, R., Pal, M., Maurya, A., Siddiqui, Z., Dubey, A., Singh, S., Prasad, O., & Sinha, L. (2026) · ChemistrySelect · doi:10.1002/slct.202506601

Anticancer effects of bisabolol oxide A-Loaded Micellar/Liposomal nanoparticles on DU-145 cells with deregulation of miR-34a and miR-181a: in silico and in vitro studies

Kohan, S. F., Khorrami, Z. A., Fatideh, F. B., Chegini, S. N., Kararoudi, A. N., Zahmatkesh, H., Rasti, B., Nikpassand, M., Shahriarinour, M., Ranji, N., et al. (2026) · BMC Biotechnology · doi:10.1186/s12896-026-01168-4

BindingDB Entry 50014256: A sulfonyl fluoride derivative inhibits EGFR

BindingDB (2022) · UC San Diego · doi:10.7270/q2sq946r

BindingDB Entry 50022952: Recent advances in the design of small molecular drugs with acrylamides covalent warheads.

BindingDB (2026) · UC San Diego · doi:10.7270/q2rv0tkm

BindingDB Entry 50022956: Design, preparation and biological evaluation of new Rociletinib-inspired analogs as irreversible EGFR inhibitors to treat non-small-cell-lung cancer.

BindingDB (2026) · UC San Diego · doi:10.7270/q2cj8kb3

BindingDB Entry 50016077: Design and synthesis of proteolysis targeting chimeras (PROTACs) as an EGFR degrader based on CO-1686.

BindingDB (2023) · UC San Diego · doi:10.7270/q2gm8c8b

RESEARCH ARTICLE OF1 | CANCER DISCOVERYDECEMBER 2013 www.aacrjournals.org Discovery of a Mutant-Selective Covalent Inhibitor of EGFR that Overcomes T790M- Mediated Resistance in NSCLC

Walter, A. O., Sjin, R. T. T., Sjin, T., Haringsma, H. J., Ohashi, K., Sun, J., Lee, K., Dubrovskiy, R., Labenski, M., Zhu, Z., et al. (2016)

Abstract 1791: CO-1686, a novel mutant-selective EGFR inhibitor, overcomes T790M mediated resistance in Non-Small Cell Lung Cancer (NSCLC)

Walter, A. O., Sjin, R. T. T., Haringsma, H. J., Lin, K., Dubrovskiy, A., Lee, K., Martin, T. S., Karp, R., Zhu, Z., Nu, D., et al. (2012) · Cancer Research · doi:10.1158/1538-7445.am2012-1791 · Cited by 4 · see citing works

Discovery of a Mutant-Selective Covalent Inhibitor of EGFR that Overcomes T790M-Mediated Resistance in NSCLC

Walter, A. O., Sjin, R. T. T., Haringsma, H. J., Ohashi, K., Sun, J., Lee, K., Dubrovskiy, A., Labenski, M., Zhu, Z., Wang, Z., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0314 · Cited by 620 · see citing works

Abstract B120: Preclinical assessment of a mutant-selective covalent inhibitor of EGFR that overcomes T790M-mediated resistance in NSCLC.

Simmons, A. D., Haringsma, H. J., Walter, A. O., Sjin, R. T. T., Ohler, Z. W., Allen, A. R., & Harding, T. C. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-13-b120 · Cited by 1 · see citing works

Abstract C189: CO-1686, an orally available, mutant-selective inhibitor of the epidermal growth factor receptor (EGFR), causes tumor shrinkage in non-small cell lung cancer (NSCLC) with T790M mutations.

Walter, A. O., Sjin, R. T. T., Haringsma, H. J., Lin, K., Dubrovskiy, A., Lee, K., Martin, T. S., Karp, R., Zhu, Z., Niu, D., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-11-c189 · Cited by 12 · see citing works