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Tabuchi, Y., Yang, J., & Taki, M. (2021) · Chemical Communications · doi:10.1039/d0cc08109d · Cited by 28 · see citing works

Structure-based inhibitor design of mutant RAS proteins—a paradigm shift

Nyíri, K., Koppány, G., & Vértessy, B. G. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09914-6 · Cited by 27 · see citing works

The Influence of Oncogenic RAS on Chemotherapy and Radiotherapy Resistance Through DNA Repair Pathways

Cáceres-Gutiérrez, R. E., Alfaro‐Mora, Y., Andonegui, M. A., Díaz‐Chávez, J., & Herrera, L. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.751367 · Cited by 27 · see citing works

Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigen

Wright, K. M., DiNapoli, S. R., Miller, M. S., Azurmendi, P. A., Zhao, X., Yu, Z., Chakrabarti, M., Shi, W., Douglass, J., Hwang, M. S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40821-w · Cited by 27 · see citing works

Proof of concept for poor inhibitor binding and efficient formation of covalent adducts of KRAS G12C and ARS compounds

Khrenova, M. G., Kulakova, A. M., & Nemukhin, A. V. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00071j · Cited by 26 · see citing works

Covalent inhibitor targets KRasG12C: A new paradigm for drugging the undruggable and challenges ahead

Li, H., Qi, W.-L., Wang, Y., & Meng, L. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.011 · Cited by 25 · see citing works

Targeting KRAS Diversity: Covalent Modulation of G12X and Beyond in Cancer Therapy

Kirschner, T., Müller, M. P., & Rauh, D. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c02403 · Cited by 24 · see citing works

Unveiling the “invisible” druggable conformations of GDP-bound inactive Ras

Liu, D., Mao, Y., Gu, X., Zhou, Y., & Long, D. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024725118 · Cited by 24 · see citing works

Covalent inhibitors of the GTPase KRASG12C: a review of the patent literature

Kettle, J. G., & Cassar, D. J. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1709443 · Cited by 23 · see citing works

Discovery of covalent enzyme inhibitors using virtual docking of covalent fragments

Chowdhury, S. R., Kennedy, S., Zhu, K., Mishra, R. K., Chuong, P., Nguyen, A.-U., Kathman, S. G., & Statsyuk, A. V. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.019 · Cited by 23 · see citing works

Precedence and Promise of Covalent Inhibitors of EGFR and KRAS for Patients with Non-Small-Cell Lung Cancer

Cheng, H., & Planken, S. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00311 · Cited by 23 · see citing works

Technologies for Direct Detection of Covalent Protein–Drug Adducts

Mons, E., Kim, R. Q., & Mulder, M. P. C. (2023) · Pharmaceuticals · doi:10.3390/ph16040547 · Cited by 23 · see citing works

Covalent-Allosteric Inhibitors: Do We Get the Best of Both Worlds?

Tao, H., Yang, B., Farhangian, A., Xu, K., Li, T., Zhang, Z., & Li, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02760 · Cited by 21 · see citing works

Biophysical and structural analysis of KRAS switch-II pocket inhibitors reveals allele-specific binding constraints

Alexander, P., Chan, A. H., Rabara, D., Swain, M., Larsen, E. K., Dyba, M. D., Chertov, O., Ashraf, M., Champagne, A., Lin, K. Y., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110331 · Cited by 21 · see citing works

Oncogenic KRAS G12C: Kinetic and redox characterization of covalent inhibition

Huynh, M. V., Parsonage, D., Forshaw, T. E., Chirasani, V. R., Hobbs, G. A., Wu, H., Lee, J., Furdui, C. M., Poole, L. B., & Campbell, S. L. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102186 · Cited by 21 · see citing works

KRAS Ubiquitination at Lysine 104 Retains Exchange Factor Regulation by Dynamically Modulating the Conformation of the Interface

Yin, G., Zhang, J., Nair, V. V., Truong, V. H., Chaia, A. I., Petela, J., Harrison, J. S., Gorfe, A. A., & Campbell, S. L. (2020) · iScience · doi:10.1016/j.isci.2020.101448 · Cited by 21 · see citing works

Multiparameter Kinetic Analysis for Covalent Fragment Optimization by Using Quantitative Irreversible Tethering (qIT)

Craven, G. B., Affron, D. P., Kösel, T., Wong, T. L., Jukes, Z., Liu, C., Morgan, R. M. L., Armstrong, A., & Mann, D. J. (2020) · ChemBioChem · doi:10.1002/cbic.202000457 · Cited by 20 · see citing works

Inhibition of RAS: proven and potential vulnerabilities

Zuberi, M., Khan, I., & O’Bryan, J. P. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190023 · Cited by 20 · see citing works

Binding modes of GDP, GTP and GNP to NRAS deciphered by using Gaussian accelerated molecular dynamics simulations

Bao, H., Wang, W., Sun, H. B., & Chen, J. Z. (2023) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2023.2165542 · Cited by 19 · see citing works

Identification of the first structurally validated covalent ligands of the small GTPase RAB27A

Jamshidiha, M., Lanyon‐Hogg, T., Sutherell, C. L., Craven, G. B., Tersa, M., Vita, E. D., Brustur, D., Pérez‐Dorado, I., Hassan, S., Petracca, R., et al. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00225b · Cited by 18 · see citing works

Diffusion Limit and the Reactivity/Affinity Conundrum: Implications for Optimization and Hit Finding for Irreversible Modulators

Srinivasan, B. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02863 · Cited by 17 · see citing works

DIAPH3 promotes the tumorigenesis of lung adenocarcinoma

Guo, X., He, W., Gao, E., & Ma, H. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111662 · Cited by 17 · see citing works

Conformation-locking antibodies for the discovery and characterization of KRAS inhibitors

Davies, C. W., Oh, A. J., Mroue, R., Steffek, M., Bruning, J. M., Xiao, Y., Feng, S., Jayakar, S., Chan, E., Arumugam, V., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-021-01126-9 · Cited by 17 · see citing works

Current perspectives of KRAS in non-small cell lung cancer

Harris, E., & Thawani, R. (2024) · Current Problems in Cancer · doi:10.1016/j.currproblcancer.2024.101106 · Cited by 16 · see citing works

Repurposing drug molecule against SARS-Cov-2 (COVID-19) through molecular docking and dynamics: a quick approach to pick FDA-approved drugs

Farhat, N., & Khan, A. U. (2021) · Journal of Molecular Modeling · doi:10.1007/s00894-021-04923-w · Cited by 16 · see citing works

Allosteric Binding-Mediated Suppression on Activity of G12D KRAS Recognized via Markov State Model and Communication Pathway.

Chen, J.-Z., Wang, J., Wang, W., Zhao, L., Jin, H., & Hu, G.-D. (2026) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c07583 · Cited by 16 · see citing works

Advances and Challenges in RAS Signaling Targeted Therapy in Leukemia

Chen, Y., Yin, Z., Westover, K. D., Zhou, Z., & Shu, L. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-24-0504 · Cited by 15 · see citing works

Accelerating the Validation of Endogenous On-Target Engagement and In Cellulo Kinetic Assessment for Covalent Inhibitors of KRASG12C in Early Drug Discovery

Kantae, V., Polański, R., Lewis, H. J., Haider, A., Barratt, D. G., & Srinivasan, B. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00483 · Cited by 15 · see citing works

Therapeutic Targeting the Allosteric Cysteinome of RAS and Kinase Families

Li, L., Meyer, C., Zhou, Z.-W., Elmezayen, A., & Westover, K. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167626 · Cited by 14 · see citing works

Profiling Nascent Tumor Extracellular Vesicles via Metabolic Timestamping and Aptamer-Driven Specific Click Chemistry

Wu, Q., Zeng, Y., Wang, W., Liu, S., Huang, Y., Zhang, Y., Chen, X., You, Z., Zhang, C., Wang, T., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c01973 · Cited by 15 · see citing works

Targeting KRAS Oncogene for Patients With Colorectal Cancer: A New Step Toward Precision Medicine

Şahin, İ. H., Saridogan, T., Ayasun, R., Syed, M. P., Gorantla, V. C., Malhotra, M. K., Thomas, R. A., Rhee, J. C., Zhang, J. Y., Hsu, D. J., et al. (2024) · JCO Oncology Practice · doi:10.1200/op.23.00787 · Cited by 13 · 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

Discovery of Fulzerasib (GFH925) for the Treatment of KRAS G12C-Mutated Solid Tumors

Jiang, T., Lin, C., Le, S., Zhang, L., Liang, T., Cai, L., Lan, X., Ge, M., Liu, Z., He, W., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c03183 · Cited by 13 · see citing works

Development and Preclinical Evaluation of Radiolabeled Covalent G12C-Specific Inhibitors for Direct Imaging of the Oncogenic KRAS Mutant

Zhang, Z., Wang, X., Ye, J., Liu, H., Fang, J., Zhang, M., Li, Y., Huang, J., Zhang, D., Wang, J., et al. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00426 · Cited by 13 · see citing works

Mutant-Specific Targeting of Ras G12C Activity by Covalently Reacting Small Molecules

Goody, R. S., Müller, M. P., & Rauh, D. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.07.005 · Cited by 14 · see citing works

Identification of VVD-214/RO7589831, a Clinical-Stage, Covalent Allosteric Inhibitor of WRN Helicase for the Treatment of MSI-High Cancers

Kikuchi, S., Green, J. C., Rogness, D. C., Lam, B., Owyang, Z. A., Malmstrom, R. D., Tabatabaei, A., Snead, A. N., Hoffman, M. A., Bernard, S. M., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01805 · Cited by 14 · see citing works

Advanced technologies for screening and identifying covalent inhibitors

Guo, Y., Wen, S., Tong, A., & Wang, Y. (2024) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2024.117833 · Cited by 11 · see citing works

The structure of KRAS G12C bound to divarasib highlights features of potent switch-II pocket engagement

Fernando, M. C., Craven, G. B., & Shokat, K. M. (2024) · Small GTPases · doi:10.1080/21541248.2025.2505441 · Cited by 11 · see citing works

Targeting a Novel KRAS Binding Site: Application of One-Component Stapling of Small (5–6-mer) Peptides

Fumagalli, G., Carbajo, R. J., Nissink, J. W. M., Tart, J., Dou, R., Thomas, A. P., & Spring, D. R. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01334 · Cited by 11 · see citing works

Covalent Ligand Electrophiles Are Differentially Activated by Proximity Effects Which Govern Latent Protein Reactivity

Frankovich, T. V., McCann, H. M., Hoffman, K. S., & Rullo, A. F. (2025) · ACS Central Science · doi:10.1021/acscentsci.5c00699 · Cited by 10 · see citing works

Kinase signalling adaptation supports dysfunctional mitochondria in disease

Skalka, G., Tsakovska, M., & Murphy, D. J. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1354682 · Cited by 12 · see citing works

Precision immune regulation in KRAS-mutated cancers: the final piece of the puzzle?

Fu, S., Ma, J., Cai, C., Tan, J., Deng, X., Shen, H., Zeng, S., Chen, Y., & Han, Y. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03444-1 · Cited by 11 · see citing works

Probing the KRas Switch II Groove by Fluorine NMR Spectroscopy

Peacock, D. M., Kelly, M. J. S., & Shokat, K. M. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00566 · Cited by 10 · see citing works

Covalent fragment mapping of KRasG12C revealed novel chemotypes with in vivo potency

Orgován, Z., Péczka, N., Petri, L., Ábrányi‐Balogh, P., Ranđelović, I., Tóth, S., Szakács, G., Nyíri, K., Vértessy, B. G., Pálfy, G., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115212 · Cited by 10 · see citing works

Exploitation of Proximity-Mediated Effects in Drug Discovery: An Update of Recent Research Highlights in Perturbing Pathogenic Proteins and Correlated Issues

Zhao, C., Wang, H., Zhan, W., Lv, X., & Ma, X. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00079 · Cited by 9 · see citing works

Contribution of Noncovalent Recognition and Reactivity to the Optimization of Covalent Inhibitors: A Case Study on KRasG12C

Péczka, N., Ranđelović, I., Orgován, Z., Csorba, N., Egyed, A., Petri, L., Ábrányi‐Balogh, P., Gadanecz, M., Perczel, A., Tóvári, J., et al. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00217 · Cited by 9 · see citing works

Size-Dependent Target Engagement of Covalent Probes

Petri, L., Gabizon, R., Ferenczy, G. G., Péczka, N., Egyed, A., Ábrányi‐Balogh, P., Takács, T., & Keserű, G. M. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00017 · Cited by 9 · see citing works

Let K-Ras activate its own inhibitor

Statsyuk, A. V. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0066-0 · Cited by 9 · see citing works

Binding modes of the KRAS(G12C) inhibitors GDC-6036 and LY3537982 revealed by all atom molecular dynamics simulations

Leini, R., Kapp, J. N., Kopra, K., & Pantsar, T. (2025) · Scientific Reports · doi:10.1038/s41598-025-07532-2 · Cited by 8 · see citing works

COOKIE-Pro: covalent inhibitor binding kinetics profiling on the proteome scale

Lin, H., Yang, B., Ding, L., Yang, Y., Holt, M. V., Jung, S. Y., Zhang, B., Wang, M. C., & Wang, J. (2025) · Nature Communications · doi:10.1038/s41467-025-63491-2 · Cited by 9 · see citing works

Abstract 686: Drugging an undruggable pocket: The biochemical mechanism of covalent KRASG12C inhibitors

Hansen, R., Peters, U., Babbar, A., Chen, Y., Feng, J., Janes, M. R., Li, L., Ren, P., Liu, Y., & Zarrinkar, P. P. (2018) · Cancer Research · doi:10.1158/1538-7445.am2018-686

Proof of concept for poor inhibitor binding and efficient formation of covalent adducts of KRAS G12C and ARS compounds

Khrenova, M. G., Kulakova, A. M., & Nemukhin, A. V. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00071j · Cited by 26 · see citing works

Covalently targeting KRAS G12C

Janes, M. R., Li, L., Hansen, R., Peters, U., Ren, P., & Liu, Y. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00008-5 · Cited by 1 · see citing works

Oncogenic KRAS G12C: Kinetic and redox characterization of covalent inhibition

Huynh, M. V., Parsonage, D., Forshaw, T. E., Chirasani, V. R., Hobbs, G. A., Wu, H., Lee, J., Furdui, C. M., Poole, L. B., & Campbell, S. L. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102186 · Cited by 21 · see citing works

Abstract 929: Discovery of novel covalent KRASG12C inhibitors that display high potency and selectivity in vitro and in vivo

Li, L., Janes, M. R., Zhang, J., Hansen, R., Peters, U., Guo, X., Chen, Y., Babbar, A., Firdaus, S. J., Feng, J., et al. (2018) · Cancer Research · doi:10.1158/1538-7445.am2018-929