Discovery of N-((3 R,4 R)-4-Fluoro-1-(6-((3-methoxy-1-methyl-1 H-pyrazol-4-yl)amino)-9-methyl-9 H-purin-2-yl)pyrrolidine-3-yl)acrylamide (PF-06747775) through Structure-Based Drug Design: A High Affinity Irreversible Inhibitor Targeting Oncogenic EGFR Mutants with Selectivity over Wild-Type EGFR

Understanding organofluorine chemistry. An introduction to the C–F bond

O’Hagan, D. (2007) · Chemical Society Reviews · doi:10.1039/b711844a · Cited by 4,049 · see citing works

Epidermal growth factor receptor mutations in lung cancer

Sharma, S. V., Bell, D. W., Settleman, J., & Haber, D. A. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2088 · Cited by 3,170 · see citing works

The resurgence of covalent drugs

Singh, J., Petter, R. C., Baillie, T. A., & Whitty, A. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3410 · Cited by 1,873 · see citing works

A Medicinal Chemist’s Guide to Molecular Interactions

Bissantz, C., Kuhn, B., & Ståhl, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100112j · Cited by 1,741 · see citing works

Novel mutant-selective EGFR kinase inhibitors against EGFR T790M

Zhou, W., Ercan, D., Chen, L., Yun, C.-H., Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., et al. (2009) · Nature · doi:10.1038/nature08622 · Cited by 1,013 · see citing works

PF00299804, an Irreversible Pan-ERBB Inhibitor, Is Effective in Lung Cancer Models with <i>EGFR</i> and <i>ERBB2</i> Mutations that Are Resistant to Gefitinib

Engelman, J. A., Zejnullahu, K., Gale, C.-M., Lifshits, E., Gonzales, A. J., Shimamura, T., Zhao, F., Vincent, P. W., Naumov, G. N., Bradner, J. E., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1885 · Cited by 730 · see citing works

Understanding resistance to EGFR inhibitors—impact on future treatment strategies

Wheeler, D. L., Dunn, E. F., & Harari, P. M. (2010) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.97 · Cited by 683 · see citing works

Discovery of a Potent and Selective EGFR Inhibitor (AZD9291) of Both Sensitizing and T790M Resistance Mutations That Spares the Wild Type Form of the Receptor

Finlay, M. R. V., Anderton, M., Ashton, S., Ballard, P., Bethel, P. A., Box, M. R., Bradbury, R. H., Brown, S. J., Butterworth, S., Campbell, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500973a · Cited by 636 · see citing works

Concise review of the glutathione S-transferases and their significance to toxicology

Eaton, D. L. (1999) · Toxicological Sciences · doi:10.1093/toxsci/49.2.156 · Cited by 627 · 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

Discovery of (10 R )-7-Amino-12-fluoro-2,10,16-trimethyl-15-oxo-10,15,16,17-tetrahydro- 2H -8,4-(metheno)pyrazolo[4,3- h ][2,5,11]-benzoxadiazacyclotetradecine-3-carbonitrile (PF-06463922), a Macrocyclic Inhibitor of Anaplastic Lymphoma Kinase (ALK) and c-ros Oncogene 1 (ROS1) with Preclinical Brain Exposure and Broad-Spectrum Potency against ALK-Resistant Mutations

Johnson, T. W., Richardson, P., Bailey, S., Brooun, A., Burke, B. J., Collins, M. R., Cui, J. J., Deal, J. G., Deng, Y., Dinh, D. M., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500261q · Cited by 616 · see citing works

Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitor–Resistant Disease

Ohashi, K., Maruvka, Y. E., Michor, F., & Pao, W. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.43.3912 · Cited by 467 · see citing works

The C–F bond as a conformational tool in organic and biological chemistry

Hunter, L. (2010) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.6.38 · Cited by 396 · see citing works

A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors

Lanning, B. R., Whitby, L. R., Dix, M. M., Douhan, J., Gilbert, A. M., Hett, E. C., Johnson, T., Joslyn, C. M., Kath, J. C., Niessen, S., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1582 · Cited by 361 · see citing works

Irreversible Protein Kinase Inhibitors: Balancing the Benefits and Risks

Barf, T., & Kaptein, A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003203 · Cited by 331 · see citing works

Development of a new permeability assay using low‐efflux MDCKII cells

Di, L., Whitney‐Pickett, C., Umland, J. P., Zhang, H., Zhang, X., Gebhard, D. F., Lai, Y., Federico, J. J., Davidson, R. E., Smith, R., et al. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22674 · Cited by 328 · see citing works

Rapid assessment of a novel series of selective CB2 agonists using parallel synthesis protocols: A Lipophilic Efficiency (LipE) analysis

Ryckmans, T., Edwards, M. P., Horne, V. A., Correia, A. M., Owen, D. R., Thompson, L. R., Tran, I., Tutt, M. F., & Young, T. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.062 · Cited by 282 · see citing works

Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance

Schwartz, P. A., Kuzmic, P., Solowiej, J., Bergqvist, S., Bolanos, B., Almaden, C., Nagata, A., Ryan, K., Feng, J., Dalvie, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313733111 · Cited by 281 · see citing works

Fluorine Bonding — How Does It Work In Protein−Ligand Interactions?

Zhou, P., Zou, J., Tian, F., & Shang, Z. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci9002393 · Cited by 266 · see citing works

Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer

Eck, M. J., & Yun, C.-H. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.010 · Cited by 225 · see citing works

An evaluation of hERG current assay performance: Translating preclinical safety studies to clinical QT prolongation

Gintant, G. A. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.008 · Cited by 221 · see citing works

Insights into the Aberrant Activity of Mutant EGFR Kinase Domain and Drug Recognition

Gajiwala, K. S., Feng, J., Ferre, R. A., Ryan, K., Brodsky, O., Weinrich, S. L., Kath, J. C., & Stewart, A. (2012) · Structure · doi:10.1016/j.str.2012.11.014 · Cited by 204 · see citing works

Drug discovery considerations in the development of covalent inhibitors

Mah, R., Thomas, J. R., & Shafer, C. M. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.10.003 · Cited by 197 · see citing works

The EGFR T790M Mutation in Acquired Resistance to an Irreversible Second-Generation EGFR Inhibitor

Kim, Y.-W., Ko, J., Cui, Z.-Y., Abolhoda, A., Ahn, J. S., Ou, S.-H., Ahn, M., & Park, K. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0750 · Cited by 179 · see citing works

Targeted covalent drugs of the kinase family

Singh, J., Petter, R. C., & Kluge, A. F. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.06.168 · Cited by 177 · see citing works

Structure-Based Approach for the Discovery of Pyrrolo[3,2-d]pyrimidine-Based EGFR T790M/L858R Mutant Inhibitors

Sogabe, S., Kawakita, Y., Igaki, S., Iwata, H., Miki, H., Cary, D. R., Takagi, T., Takagi, S., Ohta, Y., & Ishikawa, T. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300327z · Cited by 175 · see citing works

pH-Dependent Solubility and Permeability Criteria for Provisional Biopharmaceutics Classification (BCS and BDDCS) in Early Drug Discovery

Varma, M. V. S., Gardner, I. B., Steyn, S. J., Nkansah, P., Rotter, C. J., Whitney‐Pickett, C., Zhang, H., Di, L., Cram, M., Fenner, K. S., et al. (2012) · Molecular Pharmaceutics · doi:10.1021/mp2004912 · Cited by 162 · see citing works

Role of Physicochemical Properties and Ligand Lipophilicity Efficiency in Addressing Drug Safety Risks

Edwards, M. P., & Price, D. A. (2010) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(10)45023-x · Cited by 147 · see citing works

Discovery of Highly Potent, Selective, and Brain-Penetrant Aminopyrazole Leucine-Rich Repeat Kinase 2 (LRRK2) Small Molecule Inhibitors

Estrada, A. A., Chan, B. K., Baker‐Glenn, C. A. G., Beresford, A. P., Burdick, D. J., Chambers, M. G., Chen, H., Domínguez, S. L., Dotson, J., Drummond, J., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401654j · Cited by 137 · see citing works

The Role of Erlotinib (Tarceva, OSI 774) in the Treatment of Non-Small Cell Lung Cancer

Perez-Soler, R. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-040017 · Cited by 110 · see citing works

Second-Generation Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors in Lung Cancers

Yu, H. A., & Riely, G. J. (2013) · Journal of the National Comprehensive Cancer Network · doi:10.6004/jnccn.2013.0024 · Cited by 98 · see citing works

Discovery of 1-{(3R,4R)-3-[({5-Chloro-2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-pyrrolo[2,3-d]pyrimidin-4-yl}oxy)methyl]-4-methoxypyrrolidin-1-yl}prop-2-en-1-one (PF-06459988), a Potent, WT Sparing, Irreversible Inhibitor of T790M-Containing EGFR Mutants

Cheng, H., Nair, S. K., Murray, B. W., Almaden, C., Bailey, S., Baxi, S. M., Behenna, D. C., Cho-Schultz, S., Dalvie, D., Dinh, D. M., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01633 · Cited by 96 · see citing works

Discovery of (<i>R</i>,<i>E</i>)-<i>N</i>-(7-Chloro-1-(1-[4-(dimethylamino)but-2-enoyl]azepan-3-yl)-1<i>H</i>-benzo[<i>d</i>]imidazol-2-yl)-2-methylisonicotinamide (EGF816), a Novel, Potent, and WT Sparing Covalent Inhibitor of Oncogenic (L858R, ex19del) and Resistant (T790M) EGFR Mutants for the Treatment of EGFR Mutant Non-Small-Cell Lung Cancers

Lelais, G., Epple, R., Marsilje, T. H., Long, Y. O., McNeill, M., Chen, B., Lu, W., Anumolu, J., Badiger, S., Bursulaya, B., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01985 · Cited by 95 · see citing works

Is hyperconjugation responsible for the “gauche effect” in 1-fluoropropane and other 2-substituted-1-fluoroethanes? †

Rablen, P. R., Hoffmann, R. W., Hrovat, D. A., & Borden, W. T. (1999) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/a901974j · Cited by 91 · see citing works

Transition States and Energetics of Nucleophilic Additions of Thiols to Substituted α,β-Unsaturated Ketones: Substituent Effects Involve Enone Stabilization, Product Branching, and Solvation

Krenske, E. H., Petter, R. C., Zhu, Z., & Houk, K. N. (2011) · The Journal of Organic Chemistry · doi:10.1021/jo200761w · Cited by 86 · see citing works

Design, Synthesis, and Biological Evaluation of Novel Conformationally Constrained Inhibitors Targeting Epidermal Growth Factor Receptor Threonine790 → Methionine790 Mutant

Chang, S., Zhang, L., Xu, S., Luo, J., Lu, X., Zhang, Z., Xu, T., Liu, Y., Tu, Z., Xu, Y., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201591k · Cited by 85 · see citing works

Discovery of selective irreversible inhibitors for EGFR-T790M

Zhou, W., Ercan, D., Janne, P. A., & Gray, N. S. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.12.036 · Cited by 67 · see citing works

Tyrosine Kinase Inhibitors. 20. Optimization of Substituted Quinazoline and Pyrido[3,4-<i>d</i>]pyrimidine Derivatives as Orally Active, Irreversible Inhibitors of the Epidermal Growth Factor Receptor Family

Smaill, J. B., Gonzales, A. J., Spicer, J. A., Lee, H., Reed, J. E., Sexton, K., Althaus, I. W., Zhu, T., Black, S. L., Blaser, A., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00883 · Cited by 63 · see citing works

Structural Optimization and Structure–Activity Relationships of N2-(4-(4-Methylpiperazin-1-yl)phenyl)-N8-phenyl-9H-purine-2,8-diamine Derivatives, a New Class of Reversible Kinase Inhibitors Targeting both EGFR-Activating and Resistance Mutations

Yang, J., Wang, L., Liu, J., Zhong, L., Zheng, R., Xu, Y., Ji, P., Zhang, C., Wang, W., Lin, X., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301365e · Cited by 59 · see citing works

Should the Incorporation of Structural Alerts be Restricted in Drug Design? An Analysis of Structure-Toxicity Trends with Aniline-Based Drugs

Kalgutkar, A. S. S. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141112122118 · Cited by 43 · see citing works

Rapid Discovery of Pyrido[3,4- d ]pyrimidine Inhibitors of Monopolar Spindle Kinase 1 (MPS1) Using a Structure-Based Hybridization Approach

Innocenti, P., Woodward, H. L., Solanki, S., Naud, S., Westwood, I. M., Cronin, N., Hayes, A., Roberts, J., Henley, A. T., Baker, R., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01811 · Cited by 36 · see citing works

Mechanisms of Acquired Resistance to Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors and New Therapeutic Perspectives in Non Small Cell Lung Cancer

Bonanno, L., Jirillo, A., & Favaretto, A. G. (2011) · Current Drug Targets · doi:10.2174/138945011795528958 · Cited by 27 · see citing works

Potent, selective and orally bioavailable leucine-rich repeat kinase 2 (LRRK2) inhibitors

Greshock, T. J., Sanders, J. M., Drolet, R. E., Rajapakse, H. A., Chang, R. K., Kim, B. Y., Rada, V. L., Tiscia, H. E., Su, H., Lai, M., et al. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.04.021 · Cited by 23 · see citing works

The Role of Epidermal Growth Factor Receptor Mutations and Epidermal Growth Factor Receptor-Tyrosine Kinase Inhibitors in the Treatment of Lung Cancer

Chang, S., Chang, C., & Shih, J. (2011) · Cancers · doi:10.3390/cancers3022667 · Cited by 6 · see citing works

Management of acquired resistance to EGFR TKI–targeted therapy in advanced non-small cell lung cancer

Wu, S., & Shih, J. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0777-1 · Cited by 789 · see citing works

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

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works

Lipophilic Efficiency as an Important Metric in Drug Design

Johnson, T. W., Gallego, R. A., & Edwards, M. P. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00077 · Cited by 385 · see citing works

A review on progression of epidermal growth factor receptor (EGFR) inhibitors as an efficient approach in cancer targeted therapy

Ayati, A., Moghimi, S., Salarinejad, S., Safavi, M., Pouramiri, B., & Foroumadi, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.103811 · Cited by 385 · see citing works

Third generation EGFR TKIs: current data and future directions

Tan, C., Kumarakulasinghe, N. B., Huang, Y., Ang, Y. L. E., Choo, J. R.-E., Goh, B.-C., & Soo, R. A. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0778-0 · Cited by 317 · see citing works

Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T.-A., Svensson, R. U., Olucha, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.051 · Cited by 262 · see citing works

Optimizing the sequencing of tyrosine kinase inhibitors (TKIs) in epidermal growth factor receptor (EGFR) mutation-positive non-small cell lung cancer (NSCLC)

Gelatti, A., Drilon, A. E. D. C., & Santini, F. C. (2019) · Lung Cancer · doi:10.1016/j.lungcan.2019.09.017 · Cited by 220 · see citing works

Beyond Osimertinib: The Development of Third-Generation EGFR Tyrosine Kinase Inhibitors For Advanced EGFR+ NSCLC

Nagasaka, M., Zhu, V. W., Lim, S. M., Greco, M., Wu, F., & Ou, S.-H. I. (2021) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2020.11.028 · Cited by 219 · see citing works

Recent advances in activity-based probes (ABPs) and affinity-based probes (A f BPs) for profiling of enzymes

Fang, H., Peng, B., Ong, S. Y., Wu, Q., Li, L., & Yao, S. Q. (2021) · Chemical Science · doi:10.1039/d1sc01359a · Cited by 210 · see citing works

Progress with covalent small-molecule kinase inhibitors

Zhao, Z., & Bourne, P. E. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.01.035 · Cited by 200 · see citing works

Where Do Recent Small Molecule Clinical Development Candidates Come From?

Brown, D. G., & Boström, J. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00675 · Cited by 179 · see citing works

Targeting EGFR ^L858R/T790M and EGFR ^{L858R/T790M/C797S} resistance mutations in NSCLC: Current developments in medicinal chemistry

Lu, X., Yu, L., Zhang, Z., Ren, X., Smaill, J. B., & Ding, K. (2018) · Medicinal Research Reviews · doi:10.1002/med.21488 · Cited by 173 · see citing works

Recent Progress of Small-Molecule Epidermal Growth Factor Receptor (EGFR) Inhibitors against C797S Resistance in Non-Small-Cell Lung Cancer

Chen, L., Fu, W., Zheng, L., Liu, Z., & Liang, G. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01310 · Cited by 167 · see citing works

Assessing Lysine and Cysteine Reactivities for Designing Targeted Covalent Kinase Inhibitors

Liu, R., Yue, Z., Tsai, C.-C., & Shen, J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13248 · Cited by 137 · see citing works

Targeting non-small cell lung cancer with small-molecule EGFR tyrosine kinase inhibitors

Singh, M., & Jadhav, H. R. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.10.004 · Cited by 130 · see citing works

Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations

Young, R. J., & Leeson, P. D. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00180 · Cited by 112 · see citing works

The Importance of the Pyrazole Scaffold in the Design of Protein Kinases Inhibitors as Targeted Anticancer Therapies

Nițulescu, G. M., Stancov, G., Șeremet, O. C., Nițulescu, G., Mihai, D. P., Duta-Bratu, C.-G., Bărbuceanu, Ș., & Olaru, O. T. (2023) · Molecules · doi:10.3390/molecules28145359 · Cited by 108 · see citing works

Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors

Niessen, S., Dix, M. M., Barbas, S., Potter, Z. E., Lu, S., Brodsky, O., Planken, S., Behenna, D. C., Almaden, C., Gajiwala, K. S., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.017 · Cited by 99 · see citing works

Third-generation epidermal growth factor receptor tyrosine kinase inhibitors for the treatment of non-small cell lung cancer

Wright, N. A., & Goss, G. D. (2019) · Translational Lung Cancer Research · doi:10.21037/tlcr.2019.06.01 · Cited by 93 · see citing works

RamPlot : a webserver to draw 2D, 3D and assorted Ramachandran (φ, ψ) maps

Kumar, M., & Rathore, R. S. (2025) · Journal of Applied Crystallography · doi:10.1107/s1600576725001669 · Cited by 73 · see citing works

Advances in pyrazolo[1,5- a ]pyrimidines: synthesis and their role as protein kinase inhibitors in cancer treatment

Iorkula, T. H., Osayawe, O. J.-K., Odogwu, D. A., Ganiyu, L. O., Faderin, E., Awoyemi, R. F., Akodu, B. O., Ifijen, I. H., Aworinde, O. R., Agyemang, P., et al. (2025) · RSC Advances · doi:10.1039/d4ra07556k · Cited by 68 · see citing works

Covalent Proximity Scanning of a Distal Cysteine to Target PI3Kα

Borsari, C., Keleş, E., McPhail, J. A., Schäfer, A., Sriramaratnam, R., Goch, W., Schaefer, T., Pascale, M. D., Bal, W., Gstaiger, M., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c13568 · Cited by 64 · see citing works

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

Li, J., Guan, X., Zhang, O., Sun, K., Wang, Y., Bagni, D., & Head-Gordon, T. L. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c08598 · Cited by 57 · see citing works

Complex Crystal Structures of EGFR with Third-Generation Kinase Inhibitors and Simultaneously Bound Allosteric Ligands

Niggenaber, J., Heyden, L., Grabe, T., Müller, M. P., Lategahn, J., & Rauh, D. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00472 · Cited by 56 · see citing works

Discovery of 2,4,6-trisubstitued pyrido[3,4-d]pyrimidine derivatives as new EGFR-TKIs

Zhang, H., Wang, J., Shen, Y. H., Wang, H., Duan, W.-M., Zhao, H., Hei, Y., Xin, M., Cao, Y., & Zhang, S. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.051 · Cited by 54 · see citing works

Design, synthesis, and biological evaluation of benzo[d]imidazole-2-carboxamides as new anti-TB agents

Dhameliya, T. M., Patel, K. I., Tiwari, R., Vagolu, S. K., Panda, D., Sriram, D., & Chakraborti, A. K. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104538 · Cited by 47 · see citing works

The role of quantum chemistry in covalent inhibitor design

Mihalovits, L. M., Ferenczy, G. G., & Keserű, G. M. (2021) · International Journal of Quantum Chemistry · doi:10.1002/qua.26768 · Cited by 45 · see citing works

p38α MAP kinase inhibitors to overcome EGFR tertiary C797S point mutation associated with osimertinib in non-small cell lung cancer (NSCLC): emergence of fourth-generation EGFR inhibitor

Ahmad, I., Shaikh, M., Surana, S. J., Ghosh, A., & Patel, H. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1844801 · Cited by 44 · see citing works

Synthesis, characterization, anticancer, pharmacokinetics and molecular docking investigation of N (3)-alkyl incorporated-3-acetyl-4-hydroxycoumarin thiosemicarbazones and their copper(II) complexes

Shrestha, R. M., Mahiya, K., Shrestha, A., Mohanty, S. R., Yadav, S. K., & Yadav, P. N. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.136945 · Cited by 43 · see citing works

Synthesis, characterization, and anticancer potency of coumarin-derived thiosemicarbazones and their Copper(II) complexes

Shrestha, R. M., Mahiya, K., Shrestha, A., Mohanty, S. R., Yadav, S. K., & Yadav, P. N. (2024) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2024.112142 · Cited by 39 · see citing works

Covalent binding design strategy: A prospective method for discovery of potent targeted anticancer agents

Wang, L., Zhao, J., Yao, Y., Wang, C., Zhang, J., Shu, X. H., Sun, X., Li, Y., Liu, K., Yuan, H., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.09.024 · Cited by 39 · see citing works

Selective Covalent Targeting of Mutated EGFR(T790M) with Chlorofluoroacetamide-Pyrimidines

Sato, M., Fuchida, H., Shindo, N., Kuwata, K., Tokunaga, K., Xiao-Lin, G., Inamori, R., Hosokawa, K., Watari, K., Shibata, T., et al. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00574 · Cited by 38 · see citing works

Design, synthesis and antitumor activity of novel thiophene-pyrimidine derivatives as EGFR inhibitors overcoming T790M and L858R/T790M mutations

Xiao, Z., Zhou, Z., Chu, C., Zhang, Q., Zhou, L., Yang, Z., Li, X., Yu, L., Zheng, P., Xu, S., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112511 · Cited by 36 · see citing works

Prediction of kinase inhibitors binding modes with machine learning and reduced descriptor sets

Abdelbaky, I., Tayara, H., & Chong, K. T. (2021) · Scientific Reports · doi:10.1038/s41598-020-80758-4 · Cited by 35 · see citing works

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Das, D., Wang, J., & Hong, J. (2021) · ChemMedChem · doi:10.1002/cmdc.202100166 · Cited by 34 · see citing works

Enantioselective Fluorocyclizations Mediated by Amino‐Acid‐Derived Phthalazine

Wang, H.-T., Wang, Y., Liu, S., Mai, Y., Zong, X., Gao, H., Hu, R., Jiang, X., & Yeung, Y. (2019) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201900814 · Cited by 32 · see citing works

Identification of optimal dosing schedules of dacomitinib and osimertinib for a phase I/II trial in advanced EGFR-mutant non-small cell lung cancer

Poels, K. E., Schoenfeld, A. J., Makhnin, A., Tobi, Y. Y., Wang, Y., Cabanos, H. F., Chakrabarti, S., Shi, M., Napoli, C., McDonald, T. O., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23912-4 · Cited by 32 · see citing works

Allenamide as a bioisostere of acrylamide in the design and synthesis of targeted covalent inhibitors

Chen, D., Guo, D., Yan, Z., & Zhao, Y. (2017) · MedChemComm · doi:10.1039/c7md00571g · Cited by 32 · see citing works

A clinical review on third and fourth generation EGFR tyrosine kinase inhibitors for the treatment of non-small cell lung cancer

Gawli, C., Patil, C. R., & Patel, H. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118146 · Cited by 27 · see citing works

Discovery of thiapyran-pyrimidine derivatives as potential EGFR inhibitors

Xiao, Z., Chu, C., Zhou, L., Zhou, Z., Zhang, Q., Yang, F., Yang, Z., Zheng, P., Xu, S., & Zhu, W. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115669 · Cited by 27 · see citing works

Discovery of Novel EGFR Inhibitor Targeting Wild-Type and Mutant Forms of EGFR: In Silico and In Vitro Study

Todsaporn, D., Zubenko, A. A., Kartsev, V. G., Aiebchun, T., Mahalapbutr, P., Petrou, A., Geronikaki, A. A., Диваева, Л. Н., Chekrisheva, V., Yıldız, İ., et al. (2023) · Molecules · doi:10.3390/molecules28073014 · Cited by 27 · see citing works

Pyrimidine-fused Dinitrogenous Penta-heterocycles as a Privileged Scaffold for Anti-Cancer Drug Discovery

Li, W., Zhang, J., Wang, M., Dong, R., Zhou, X., Zheng, X. X., & Sun, L. (2022) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026622666220111143949 · Cited by 25 · see citing works

The prospect of combination therapies with the third-generation EGFR-TKIs to overcome the resistance in NSCLC

Li, S., Zhu, S., Wei, H., Zhu, P., Jiao, Y., Yi, M., Gong, J., Zheng, K., & Zhang, L. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113959 · Cited by 24 · see citing works

Structure-based design and synthesis of 2,4-diaminopyrimidines as EGFR L858R/T790M selective inhibitors for NSCLC

Chen, L., Fu, W., Feng, C., Qu, R., Tong, L., Zheng, L., Fang, B., Qiu, Y., Hu, J., Cai, Y., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.061 · Cited by 24 · see citing works

Discovery of new thieno[3,2-d]pyrimidine derivatives targeting EGFRL858R/T790M NSCLCs by the conformation constrained strategy

Chen, Y., Yang, L., Qiao, H., Cheng, Z., Xie, J., Zhou, W., Huang, X., Jiang, Y., Yu, B., & Zhao, W. H. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112388 · Cited by 24 · see citing works

Discovery of 3-pyrazolyl-substituted pyrazolo[1,5-a]pyrimidine derivatives as potent TRK inhibitors to overcome clinically acquired resistance

Gong, Y., Wu, F., Wang, M., Xu, H.-C., Zhuo, L., Yang, G., & Huang, W. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114654 · Cited by 22 · see citing works

Synthesis and biological evaluation of irreversible EGFR tyrosine kinase inhibitors containing pyrido[3,4-d]pyrimidine scaffold

Zhang, H., Wang, J., Zhao, H., Yang, X., Lei, H., Xin, M., Cao, Y., & Zhang, S. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.05.039 · Cited by 22 · see citing works

Novel Aurora A and Protein Kinase C (α, β1, β2, and θ) Multitarget Inhibitors: Impact of Selenium Atoms on the Potency and Selectivity

Bijian, K., Wernic, D., Nivedha, A. K., Su, J., Lim, F. P. L., Miron, C. E., Amzil, H., Moitessier, N., & Alaoui‐Jamali, M. A. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01031 · Cited by 21 · see citing works

Urine test for EGFR analysis in patients with non-small cell lung cancer

Franovic, A., Raymond, V. M., Erlander, M. G., & Reckamp, K. L. (2017) · Journal of Thoracic Disease · doi:10.21037/jtd.2017.06.144 · Cited by 19 · see citing works

Preparation of Rhodium(III) complexes with 2(1H)-quinolinone derivatives and evaluation of their in vitro and in vivo antitumor activity

Lü, X., Wu, Y., Yang, J., Ma, F.-E., Li, L., Chen, S., Zhang, Y., Ni, Q., Pan, Y., Hong, X., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.074 · Cited by 19 · see citing works

Tanshinone IIA promotes apoptosis by downregulating BCL2 and upregulating TP53 in triple-negative breast cancer

Liu, J., Zhang, C., Liu, S., Wang, X., Wu, X.-Z., & Hao, J. (2022) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-022-02316-1 · Cited by 16 · see citing works

Discovery of novel 4-arylamino-quinazoline derivatives as EGFRL858R/T790M inhibitors with the potential to inhibit the non-small cell lung cancers

Gan, W., Wang, C., Pan, Q., Li, Y., Guo, Y., Fan, D., Peng, Y., Rao, Z., Xu, S., Zheng, P., et al. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105994 · Cited by 15 · see citing works

Highly diastereoselective synthesis of enantioenriched anti -α-allyl-β-fluoroamines

Chevis, P. J., Wangngae, S., Thaima, T., Carroll, A. W., Willis, A. C., Pattarawarapan, M., & Pyne, S. G. (2019) · Chemical Communications · doi:10.1039/c9cc02765c · Cited by 15 · see citing works

Third generation EGFR TKI landscape for metastatic EGFR mutant non-small cell lung cancer (NSCLC)

Tan, A. C., Teh, Y. L., Lai, G. G. Y., & Tan, D. S.-W. (2019) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2019.1604228 · Cited by 15 · see citing works

Design of a Lead-Like Cysteine-Targeting Covalent Library and the Identification of Hits to Cys55 of Bfl-1

Lucas, S. C. C., Milbradt, A. G., Blackwell, J. H., Bonomo, S., Brierley, A., Cassar, D. J., Freeman, J., Hadfield, T. E., Morrill, L. A., Riemens, R., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00781 · Cited by 14 · see citing works

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 · see citing works

Identification of novel allosteric binding sites and multi-targeted allosteric inhibitors of receptor and non-receptor tyrosine kinases using a computational approach

Kakarala, K. K., & Jamil, K. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1891140 · Cited by 13 · see citing works

Targeting the EGFR/RAS/RAF signaling pathway in anticancer research: a recent update on inhibitor design and clinical trials (2020–2023)

Hajjo, R., Sabbah, D. A., Bardaweel, S. K., & Zhong, H. A. (2024) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2024.2327307 · Cited by 12 · see citing works

Repurposing the Kinase Inhibitor Mavelertinib for Giardiasis Therapy

Michaels, S. A., Hulverson, M. A., Whitman, G. R., Tran, L. T. N., Choi, R., Fan, E., McNamara, C. W., Love, M. S., & Ojo, K. K. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00017-22 · Cited by 11 · see citing works

Discovery of a Novel, Selective and Irreversible Inhibitor (Abivertinib) of Mutated EGFR and T790M-induced Resistance for the Treatment of NSCLC

Mao, L., Tang, W., Zhang, X., Liu, J., Chen, Y., Hua, Y., Weng, B., Mo, X., Bao, Y., Li, T., et al. (2020) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2020.100035 · Cited by 11 · see citing works

A phase 1b/2 study of PF-06747775 as monotherapy or in combination with Palbociclib in patients with epidermal growth factor receptor mutant advanced non-small cell lung cancer

Cho, B. C., Goldberg, S. B., Kim, D., Socinski, M. A., Burns, T. F., Lwin, Z., Pathan, N., Wei, D., Masters, J. C., Cossons, N., et al. (2022) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2022.2075341 · Cited by 10 · see citing works

Enantiospecific Synthesis of (3R,4R)-1-Benzyl-4-fluoropyrrolidin-3-amine Utilizing a Burgess-Type Transformation

Widlicka, D. W., Gontcharov, A. V., Mehta, R., Pedro, D. J., & North, R. (2019) · Organic Process Research & Development · doi:10.1021/acs.oprd.9b00245 · Cited by 10 · see citing works

Coumarin–furo[2,3- d ]pyrimidone hybrid molecules targeting human liver cancer cells: synthesis, anticancer effect, EGFR inhibition and molecular docking studies

Wang, T., Gao, Y., Wu, F., Luo, L., Ma, J., & Hu, Y. (2024) · RSC Medicinal Chemistry · doi:10.1039/d3md00668a · Cited by 9 · see citing works

Origami with small molecules: exploiting the C–F bond as a conformational tool

Ryan, P., Iftikhar, R., & Hunter, L. (2025) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.21.54 · Cited by 9 · see citing works

Prospect of reprogramming replication licensing for cancer drug development

Kyei-Barffour, I., & Acheampong, D. O. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.111190 · Cited by 9 · see citing works

Lead generation of 1,2-dithiolanes as exon 19 and exon 21 mutant EGFR tyrosine kinase inhibitors

Mansour, T. S., Potluri, V. K., Pallepati, R., Basetti, V., Keesara, M., Moghudula, A. G., & Maiti, P. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.04.029 · Cited by 8 · see citing works

Hypoglycemic Activity of Rice Resistant-Starch Metabolites: A Mechanistic Network Pharmacology and In Vitro Approach

Ren, J., Dai, J., Chen, Y., Wang, Z., Sha, R., Mao, J., & Mao, Y. (2024) · Metabolites · doi:10.3390/metabo14040224 · Cited by 7 · see citing works

Polyphenol-based therapeutics for glioblastoma: validation from In-vitro cell viability assay and integrated onco-omics computational analysis

Yogesh, H. S., Shaik, S. F., Sangi, S., Swaroop, K., Sreeharsha, N., Anitha, K. N., Mishra, V. K., Kurmi, S. P. C., Nath, S., & Thapa, S. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04690-y · Cited by 6 · see citing works

Network Pharmacology Based Elucidation of Molecular Mechanisms of Laoke Formula for Treatment of Advanced Non-Small Cell Lung Cancer

Feng, Y.-Y., Liu, J.-F., Xue, Y., Liu, D., & Wu, X.-Z. (2024) · Chinese Journal of Integrative Medicine · doi:10.1007/s11655-024-3717-5 · Cited by 6 · see citing works

Determination of the solubility of 6-Chloro-7-azapurine in twelve single solvents and four binary mixed solvent systems at t = (278.15–323.15) K

Hu, G., Xu, H., Yang, W., Hao, A., Sun, W., Shen, W., & Hu, Y. (2021) · The Journal of Chemical Thermodynamics · doi:10.1016/j.jct.2021.106493 · 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

PatentNetML: A Novel Framework for Predicting Key Compounds in Patents Using Network Science and Machine Learning

Zhu, T.-F., Qian, R., Wei, X., Lü, A., & Cao, D. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01893 · Cited by 5 · see citing works

A Mechanistic Study of a Potent and Selective Epidermal Growth Factor Receptor Inhibitor against the L858R/T790M Resistance Mutation

Akher, F. B., Farrokhzadeh, A., Ravenscroft, N., & Kuttel, M. M. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00710 · Cited by 5 · see citing works

In Silicon Approach for Discovery of Chemopreventive Agents

Wang, J., Li, W., Wang, B., Hu, B., Jiang, H., Lai, B., Li, N., & Cheng, M. (2017) · Current Pharmacology Reports · doi:10.1007/s40495-017-0094-1 · 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

Targeting EGFR by Newer 1-(3,5-Bis((E)-4‑hydroxy-3-methoxystyryl)-1H-pyrazol-1-yl)-2-((substituted phenyl)amino)ethan-1-one Analogues for the Treatment of Cancer: Synthesis, In-vitro and In-silico Studies

Mohamed, M. A., Ali, A., Ali, A., Afzal, O., Ahsan, M. F., Alamri, M. A., Alossaimi, M. A., Altamimi, A. S. A., Salahuddin, S., & Ahsan, M. J. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.138826 · Cited by 3 · see citing works

Discovery of a potent, selective, and orally available EGFR C797S mutant inhibitor (DS06652923) with in vivo antitumor activity

Kageji, H., Momose, T., Ebisawa, M., Nakazawa, Y., OKADA, H. M., Togashi, N., Nagamoto, Y., Obuchi, W., Yasumatsu, I., Kihara, K., et al. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117862 · Cited by 2 · see citing works

Thermal Stability and Utility of Dienes as Protecting Groups for Acrylamides

Hooper, A. R., & Burns, A. S. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00075 · Cited by 2 · see citing works

Neurotropic activity and safety of methylene-cycloalkylacetate (MCA) derivative 3-(3-allyl-2-methylenecyclohexyl) propanoic acid

Lahiani, A., Haham, D., Lankri, D., Cornell-Kennon, S., Schaefer, E., Tsvelikhovsky, D., & Lazarovici, P. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00255 · Cited by 2 · see citing works

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

Schmalhorst, P. S., & Bergner, A. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00051 · Cited by 2 · see citing works

Receptor Tyrosine Kinases

Karl, K., Light, T. P., & Hristova, K. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00135-3 · Cited by 2 · see citing works

Structure‐Based Drug Design

Ferreira, L. L. G., & Andricopulo, A. D. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc141.pub2 · Cited by 2 · see citing works

Identification of novel lead molecules against the EGFR kinase domain using structure-based virtual screening, molecular docking, and molecular dynamics simulations

Jannu, M., Vankadoth, U. N., Umamaheswari, A., & Jinka, R. (2025) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2025.2590462 · Cited by 1 · see citing works

Computational exploration of novel indanone-pyrazole fused schiff base scaffolds as potential EGFR inhibitors for anticancer therapy

Karati, D., Sen, D., Mahanti, B., Roy, S., & Mukherjee, S. (2026) · Discover Chemistry. · doi:10.1007/s44371-026-00503-0 · Cited by 1 · see citing works

Deciphering the Structural Basis of Allosteric Inhibition of Mutant Epidermal Growth Factor Receptor and Identification of Novel Inhibitors

Pal, S., & Mohanty, D. (2026) · Computational and Structural Biotechnology Journal · doi:10.34133/csbj.0118 · Cited by 1 · see citing works

Covalent epidermal growth factor receptor (EGFR) inhibitors in targeted therapy of drug-resistant non-small cell lung cancer

Shvetsov, A. B., & Semenov, A. V. (2024) · Биоорганическая химия · doi:10.31857/s0132342324060037

Identification of oncology pharmacokinetic drivers through in vitro experiments and computational modeling

Boras, B. W., Greenwald, E. C., Wang, Y., Shi, M., Pascual, B., Cianfrogna, J. A., Bartlett, D. W., & Spilker, M. E. (2025) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-025-09986-3

Targeting EGFR by newer 4,6-Bis(( E )-4-hydroxy-3-methoxystyryl)-1-(aryl)pyrimidin-2(1 H )-one analogues as antiproliferative agents: eco-friendly chemical modification, in-vitr o and in-silico studies

Ahsan, M. F., Ahsan, M. J., Yusuf, M., Syed, T., Asiri, Y. I., Ali, A., & Salahuddin, S. (2025) · Journal of Taibah University for Science · doi:10.1080/16583655.2025.2544430

Design of Allosteric Inhibitors for Mutant EGFR by Combined use of Machine Learning and Molecular Dynamics SimulationsPreprint

Pal, S., & Mohanty, D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.01.691623

Identification of Potential Drug Leads from Dendrobium stuartii Through Integrated In Silico, Phytochemical, and Pharmacological Methods

Setiawan, D., Hadi, S., Mahdi, N. I., Mardiati, N., Sutomo, Rizki, M. I., Normaidah, N., Buih, P. H. J., Nugraha, A. T., Apriliany, F., et al. (2026) · Journal of Applied Pharmaceutical Science · doi:10.1177/22313354261461005

Daidzein derivatives as potential inhibitors of mutant EGFR in non-small cell lung cancer: A computational study supported by molecular docking, DFT, molecular dynamics simulations, and MM/PBSA techniques

Munir, F., Hussain, K., Zhao, G., & Zhang, J. (2026) · Computer Methods and Programs in Biomedicine · doi:10.1016/j.cmpb.2026.109679

Small-molecule kinase-targeted covalent inhibitors till 2025: A comprehensive review of discovery, binding modes, clinical indications, and synthetic approaches

Dahab, M. A., Ashoub, A. F., Ali, R. A., Sallam, A. S., & Mayhoub, A. S. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.119449

BindingDB Entry 50013322: Discovery of new thieno[3,2-d]pyrimidine derivatives targeting EGFR

BindingDB (2022) · UC San Diego · doi:10.7270/q24x5cjs

BindingDB Entry 50023448: Discovery of a potent, selective, and orally available EGFR C797S mutant inhibitor (DS06652923) with in vivo antitumor activity.

BindingDB (2026) · UC San Diego · doi:10.7270/q2b85f2n

BindingDB Entry 50003230: Covalent binding design strategy: A prospective method for discovery of potent targeted anticancer agents.

BindingDB (2020) · UC San Diego · doi:10.7270/q2n87dg5

BindingDB Entry 50002351: Mapping the Efficiency and Physicochemical Trajectories of Successful Optimizations.

BindingDB (2020) · UC San Diego · doi:10.7270/q2dj5j62

BindingDB Entry 50012885: Discovery of thiapyran-pyrimidine derivatives as potential EGFR inhibitors.

BindingDB (2022) · UC San Diego · doi:10.7270/q2736vnz

BindingDB Entry 50020975: Design of a Lead-Like Cysteine-Targeting Covalent Library and the Identification of Hits to Cys55 of Bfl-1.

BindingDB (2025) · UC San Diego · doi:10.7270/q2v98dn0

BindingDB Entry 50001188: Lipophilic Efficiency as an Important Metric in Drug Design.

BindingDB (2020) · UC San Diego · doi:10.7270/q2wm1gwq

BindingDB Entry 50021545: Coumarin-furo[2,3-d]pyrimidone hybrid molecules targeting human liver cancer cells: synthesis, anticancer effect, EGFR inhibition and molecular docking studies.

BindingDB (2025) · UC San Diego · doi:10.7270/q2jw8kjs

Discovery of 1-{(3R,4R)-3-[({5-Chloro-2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-pyrrolo[2,3-d]pyrimidin-4-yl}oxy)methyl]-4-methoxypyrrolidin-1-yl}prop-2-en-1-one (PF-06459988), a Potent, WT Sparing, Irreversible Inhibitor of T790M-Containing EGFR Mutants

Cheng, H., Nair, S. K., Murray, B. W., Almaden, C., Bailey, S., Baxi, S. M., Behenna, D. C., Cho-Schultz, S., Dalvie, D., Dinh, D. M., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01633 · Cited by 96 · see citing works

Abstract 1735: Discovery of novel and selective reversible inhibitors of EGFR containing the T790M drug resistance mutation with activity in vitro and in vivo

Schaefer, G., Hanan, E. J., Chan, E., Shao, L., Chen, Y., Knight, J. D., Yauch, R. L., Schmidt, S., Sideris, S., Malek, S., et al. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-1735

Pyrimido[4,5‐d]pyrimidin‐4(1H)‐one Derivatives as Selective Inhibitors of EGFR Threonine790 to Methionine790 (T790M) Mutants

Xu, T., Zhang, L., Xu, S., Yang, C., Luo, J., Ding, F., Lu, X., Liu, Y., Tu, Z., Li, S., et al. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201302313 · Cited by 37 · see citing works

Oxopyrido[2,3-d]pyrimidines as Covalent L858R/T790M Mutant Selective Epidermal Growth Factor Receptor (EGFR) Inhibitors

Wurz, R. P., Pettus, L. H., Ashton, K., Brown, J., Chen, J. J., Herberich, B., Hong, F., Harrington, E. H., Nguyen, T. T., Jean, D. J. S., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00193 · Cited by 22 · see citing works

Structure-based design and synthesis of 2,4-diaminopyrimidines as EGFR L858R/T790M selective inhibitors for NSCLC

Chen, L., Fu, W., Feng, C., Qu, R., Tong, L., Zheng, L., Fang, B., Qiu, Y., Hu, J., Cai, Y., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.061 · Cited by 24 · see citing works