The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Drugging the ‘undruggable’ cancer targets
Open accessAbstract
The term 'undruggable' was coined to describe proteins that could not be targeted pharmacologically. However, progress is being made to 'drug' many of these targets, and therefore more appropriate terms might be 'difficult to drug' or 'yet to be drugged'. Many desirable targets in cancer fall into this category, including the RAS and MYC oncogenes, and pharmacologically targeting these intractable proteins is now a key challenge in cancer research that requires innovation and the development of new technologies. In this Viewpoint article, we asked four scientists working in this field for their opinions on the most crucial advances, as well as the challenges and what the future holds for this important area of research.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Transcription factors have remained challenging drug targets due to the absence of druggable active sites (14).”
From Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN (2018) · cites this paper as [14]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Vogelstein, B., Papadopoulos, N., Velculescu, V. E., Zhou, S., Diaz, L. A., & Kinzler, K. W. (2013) · Science · doi:10.1126/science.1235122 · Cited by 7,863
The future of immune checkpoint therapy
Sharma, P., & Allison, J. P. (2015) · Science · doi:10.1126/science.aaa8172 · Cited by 4,878
Selective inhibition of BET bromodomains
Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390
Self-citationPeptide therapeutics: current status and future directions
Fosgerau, K., & Hoffmann, T. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.10.003 · Cited by 3,160
AR-V7 and Resistance to Enzalutamide and Abiraterone in Prostate Cancer
Antonarakis, E. S., Lu, C., Wang, H., Luber, B., Nakazawa, M., Roeser, J. C., Chen, Y., Mohammad, T. A., Chen, Y., Fedor, H. L., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1315815 · Cited by 2,710
K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557
Self-citationDrugging the undruggable RAS: Mission Possible?
Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997
Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells
Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683
Emerging mechanisms of resistance to androgen receptor inhibitors in prostate cancer
Watson, P. A., Arora, V. K., & Sawyers, C. L. (2015) · Nature Reviews Cancer · doi:10.1038/nrc4016 · Cited by 1,536
Cited by
Sorted by citations
Items 401–500 of 949
Divarasib in the Evolving Landscape of KRAS G12C Inhibitors for NSCLC
Brazel, D., & Nagasaka, M. (2024) · Targeted Oncology · doi:10.1007/s11523-024-01055-y · Cited by 21
Lee, Y.-T., Wu, S., Wu, C. ‐., Lin, Y.-H., Lin, C.-K., Chen, Z.-A., Sun, T.-C., Chen, Y., Chen, P., Mou, C., et al. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c16609 · Cited by 20
Calmodulin and IQGAP1 activation of PI3Kα and Akt in KRAS, HRAS and NRAS-driven cancers
Nussinov, R., Zhang, M., Tsai, C., & Jang, H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.10.032 · Cited by 21
Conformational editing of intrinsically disordered protein by α-methylation
Bauer, V., Schmidtgall, B., Gógl, G., Dolenc, J., Ősz, J., Nominé, Y., Kostmann, C., Cousido-Siah, A., Mitschler, A., Rochel, N., et al. (2020) · Chemical Science · doi:10.1039/d0sc04482b · Cited by 20
Targeting lipid metabolism in cancer: neuroblastoma
Agostini, M., Melino, G., Habeb, B. F., Calandria, J. M., & Bazan, N. G. (2022) · Cancer and Metastasis Reviews · doi:10.1007/s10555-022-10040-8 · Cited by 20
Martell, E., Kuzmychova, H., Kaul, E., Senthil, H., Chowdhury, S. R., Morrison, L. C., Fresnoza, A. L., Zagozewski, J. L., Venugopal, C., Anderson, C. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38049-9 · Cited by 20
Ding, J. H., Liu, L., Chiang, Y., Zhao, M., Liu, H., Yang, F., Shen, L., Lin, Y. L., Deng, H., Gao, J., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00787 · Cited by 19
Zhou, Y., Xu, S., López‐Carrobles, N., Ding, D., Liu, X., Menéndez‐Arias, L., & Zhan, P. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0019 · Cited by 20
Role of HOX genes in cancer progression and their therapeutical aspects.
Yadav, C., Yadav, R., Nanda, S., Ranga, S., Ahuja, P., & Tanwar, M. (2024) · Gene · doi:10.1016/j.gene.2024.148501 · Cited by 17
A patent review of RAF kinase inhibitors (2010–2018)
Man, R., Zhang, Y., Jiang, A.-Q., & Zhu, H. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1651842 · Cited by 19
The Road Not Taken with Pyrrole-Imidazole Polyamides: Off-Target Effects and Genomic Binding
Lin, J. C., & Nagase, H. (2020) · Biomolecules · doi:10.3390/biom10040544 · Cited by 19
Peptide/Lipid-Associated Nucleic Acids (PLANAs) as a Multicomponent siRNA Delivery System
Hall, R., Alasmari, A., Mozaffari, S., Mahdipoor, P., Parang, K., & Aliabadi, H. M. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00969 · Cited by 20
Dutta, K., Kanjilal, P., Das, R., & Thayumanavan, S. (2020) · Angewandte Chemie · doi:10.1002/ange.202010412 · Cited by 18
Bhat, S. M., Palepu, K., Hong, L., Mao, J., Ye, T., Iyer, R., Zhao, L., Chen, T., Vincoff, S., Watson, R., et al. (2024) · bioRxiv · doi:10.1101/2023.06.26.546591 · Cited by 90
Allostery in Disease: Anticancer Drugs, Pockets, and the Tumor Heterogeneity Challenge
Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169050 · Cited by 19
Diehl, J. N., Hibshman, P. S., Ozkan‐Dagliyan, I., Goodwin, C. M., Howard, S. V., Cox, A. D., & Der, C. J. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.008 · Cited by 18
Váradi, M., Nagy, N. T., Reis, H., Hadaschik, B. A., Niedworok, C., Módos, O., Szendrői, A., Ablat, J., Black, P. C., Keresztes, D., et al. (2023) · Cancer Medicine · doi:10.1002/cam4.5639 · Cited by 18
Chemical Proteomics–Guided Discovery of Covalent Ligands for Cancer Proteins
Zhang, X., & Cravatt, B. F. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-061421-041946 · Cited by 19
Augmentation of Myc-Dependent Mitotic Gene Expression by the Pygopus2 Chromatin Effector
Andrews, P., Popadiuk, C., Belbin, T. J., & Kao, K. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.020 · Cited by 18
Nubbemeyer, B., Pepanian, A., George, A. A. P., & Imhof, D. (2021) · ChemMedChem · doi:10.1002/cmdc.202100039 · Cited by 18
Salem, A. H., Tao, Z., Bueno, O. F., Chen, J., Chen, S., Edalji, R. P., Elmore, S. W., Fournier, K. M., Harper, K. C., Hong, R. S., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0077 · Cited by 18
Single-molecule analysis of interaction between p53TAD and MDM2 using aerolysin nanopores
Oh, S., Lee, M., & Chi, S. (2021) · Chemical Science · doi:10.1039/d1sc00386k · Cited by 19
Harumoto, T., Iwai, H., Tanigawa, M., Kubo, T., Atsumi, T., Tsutsumi, K., Takashima, M., Destito, G., Soloff, R. S., Tomizuka, K., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00652 · Cited by 18
Hale, J. J. (2022) · Wiley eBooks · doi:10.1002/9781119627784.ch1 · Cited by 18
Niessen, J., Arendt, N., Sjöblom, M., Dubbelboer, I. R., Borchardt, T. B., Koziolek, M., Hedeland, M., Lennernäs, H., Indulkar, A. S., & Dahlgren, D. (2025) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2025.114719 · Cited by 18
Srinivasan, B. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02863 · Cited by 19
Niitsu, Y., Sato, Y., Takanashi, K., Hayashi, T., Kubo-Birukawa, N., Shimizu, F., Fujitani, N., Shimoyama, R., Kukitsu, T., Kurata, W., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000361117 · Cited by 16
PLZF and its fusion proteins are pomalidomide-dependent CRBN neosubstrates
Shimizu, N., Asatsuma‐Okumura, T., Yamamoto, J., Yamaguchi, Y., Handa, H., & Ito, T. (2021) · Communications Biology · doi:10.1038/s42003-021-02801-y · Cited by 17
BET inhibition is an effective approach against KRAS-driven PDAC and NSCLC
Jauset, T., Massó-Vallés, D., Martínez-Martín, S., Beaulieu, M.-È., Foradada, L., Fiorentino, F. P., Yokota, J., Haendler, B., Siegel, S., Whitfield, J. R., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24648 · Cited by 19
Self-citationComputational models of melanoma
Albrecht, M., Lucarelli, P., Kulms, D., & Sauter, T. (2020) · Theoretical Biology and Medical Modelling · doi:10.1186/s12976-020-00126-7 · Cited by 17
A guide for bioinformaticians: ‘omics-based drug discovery for precision oncology
Mun, J., Choi, G., & Lim, B. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.08.004 · Cited by 18
Corso, A. D., Catalano, M., Schmid, A. S., Scheuermann, J., & Neri, D. (2018) · Angewandte Chemie · doi:10.1002/ange.201811650 · Cited by 19
Kafle, P., Kharel, P., Nilson, D., Herndon, D., Yasuda, S., & Sharma, I. (2025) · Chem · doi:10.1016/j.chempr.2025.102753 · Cited by 18
Comparative reactivity profiling of cysteine-specific probes by chemoproteomics
Yang, F., Chen, N., Wang, F., Jia, G., & Wang, C. (2022) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2022.100024 · Cited by 16
Kumar, A., Khani, A. T., Duault, C., Aramburo, S., Ortiz, A. S., Lee, S. J., Chan, A., McDonald, T., Huang, M., Lacayo, N. J., et al. (2023) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-006649 · Cited by 16
Yang, B., Zhou, J., Cai, K., Wang, Y., Feng, Y., Li, W., Jiang, Y., Kuo, S. H., Roy, J., Anorma, C., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302342120 · Cited by 16
E3MPH16: An efficient endosomolytic peptide for intracellular protein delivery
Kawaguchi, Y., Kawamura, Y., Hirose, H., Kiyokawa, M., Hirate, M., Hirata, T., Higuchi, Y., & Futaki, S. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.01.067 · Cited by 16
Amjadi‐Moheb, F., Paniri, A., & Akhavan‐Niaki, H. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3613 · Cited by 16
Rationale for MYC imaging and targeting in pancreatic cancer
Schneider, G., Wirth, M., Keller, U. B., & Saur, D. (2021) · EJNMMI Research · doi:10.1186/s13550-021-00843-1 · Cited by 15
D154Q Mutation does not Alter KRAS Dimerization
Grozavu, I., Stuart, S. E., Lyakisheva, A., Yao, Z., Pathmanathan, S., Ohh, M., & Štagljar, I. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167392 · Cited by 16
Activation of Rho Family GTPases by Small Molecules
Palsuledesai, C. C., Surviladze, Z., Waller, A., Miscioscia, T. F., Guo, Y., Wu, Y., Strouse, J., Romero, E., Salas, V. M., Curpan, R. F., et al. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00038 · Cited by 18
Condurat, A.-L., Aminzadeh-Gohari, S., Malnar, M., Schider, N., Opitz, L., Thomas, R., Menon, V., Kofler, B., & Pruszak, J. (2023) · Scientific Reports · doi:10.1038/s41598-023-29796-2 · Cited by 14
Yegambaram, M., Sun, X., Lü, Q., Flores, A. G., Zemskova, M., Soto, J. E., Rauckhorst, A. J., Maltepe, E., Wang, T., Fineman, J. R., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103765 · Cited by 17
Druglike Molecular Degraders of the Oncogenic RNA-Binding Protein HuR
Kassabri, L., & Benhamou, R. I. (2025) · JACS Au · doi:10.1021/jacsau.5c00551 · Cited by 16
Dual Targeting Oncoproteins MYC and HIF1α Regresses Tumor Growth of Lung Cancer and Lymphoma
Huang, X., Liu, Y., Wang, Y., Bailey, C., Zheng, P., & Liu, Y. (2021) · Cancers · doi:10.3390/cancers13040694 · Cited by 17
Ras superfamily GTPase activating proteins in cancer: Potential therapeutic targets?
Xiao, H., Wang, G., Zhao, M., Wen, S., Ouyang, L., & Sun, Q. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115104 · Cited by 18
Yu, H. T., Shi, T., Yao, L., Xu, D., Ding, Y., Xia, Q., Liu, W., & Wang, X. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01048-3 · Cited by 15
Cameron, D. P., Grosser, J., Ladigan, S., Kuzin, V., Iliopoulou, E., Wiegard, A., Benredjem, H., Jackson, K., Liffers, S. T., Lueong, S., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg5109 · Cited by 16
Nucleic acid therapeutics as differentiation agents for myeloid leukemias
Kovecses, O., Mercier, F., & McKeague, M. (2024) · Leukemia · doi:10.1038/s41375-024-02191-0 · Cited by 18
Ge, Y., Janson, V., & Liu, H. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136820 · Cited by 17
DCTPP1: A promising target in cancer therapy and prognosis through nucleotide metabolism
Liu, S., Li, F., & Wang, Z. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104348 · Cited by 18
Non-coding RNAs, metabolic stress and adaptive mechanisms in cancer
Liu, X., Feng, S., Zhang, X. D., Li, J., Zhang, K., Wu, M., & Thorne, R. F. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.06.024 · Cited by 15
Oronsky, B. T., Cabrales, P., Caroen, S. Z., Guo, X., Scribner, C. L., Oronsky, A. L., & Reid, T. R. (2021) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2021.1876025 · Cited by 15
Cytosolic Delivery of Small Protein Scaffolds Enables Efficient Inhibition of Ras and Myc
Chan, A., Wang, H. H., Haley, R. M., Song, C., Gonzalez-Martinez, D., Bugaj, L. J., Mitchell, M. J., & Tsourkas, A. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00798 · Cited by 15
Li, J., Li, R., Ma, L.-R., Wang, P., Xu, D., Huang, J., Li, L.-Q., Tang, L. L., Xie, Y., Leung, E. L., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.875330 · Cited by 17
Liu, L., Geng, X., Zhang, J., Li, S., & Gao, J. (2022) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14064 · Cited by 15
Kumar, S. U., Balasundaram, A., Hephzibah Cathryn, R., Varghese, R. P., Ramamoorthy, S., Ramanathan, G., Younes, S. N., Zayed, H., & Doss, C. G. P. (2022) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2022.105701 · Cited by 15
Fu, L., Huang, Y. L., Hou, J., Sun, M., Wang, L., Wang, X., & Chen, L. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01696f · Cited by 16
Zhang, H., Liu, C., Zhu, D., Zhang, Q., & Li, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01016 · Cited by 15
Aptamers and apple pies: a mini-review of PSMA aptamers and lessons from Donald S. Coffey.
Lupold, S. E. (2018) · Europe PMC (PubMed Central) · Cited by 15
Bhandari, N., Acharya, D., Chatterjee, A., Mandve, L., Kumar, P., Pratap, S., Malakar, P., & Shukla, S. K. (2023) · Cell Cycle · doi:10.1080/15384101.2023.2265676 · Cited by 14
Obesity under the moonlight of c-MYC
Nevzorova, Y. A., & Cubero, F. J. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1293218 · Cited by 16
Sharma, S., Risen, S. J., Gilberto, V. S., Boland, S. W., Chatterjee, A., Moreno, J. A., & Nagpal, P. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00024 · Cited by 13
Caron, G., Jiménez, D. G., Vallaro, M., Vitagliano, L., Lopez, L. L., Apprato, G., & Ermondi, G. (2024) · ADMET & DMPK · doi:10.5599/admet.2334 · Cited by 15
Reciprocal Induction of MDM2 and MYCN in Neural and Neuroendocrine Cancers
Tran, H. N., Singh, H. P., Guo, W., Cambier, L., Riggan, L., Shackleford, G. M., Thornton, M. E., Grubbs, B. H., Erdreich‐Epstein, A., Qi, D.-L., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.563156 · Cited by 14
A Long Overdue Targeted Treatment for KRAS Mutations in NSCLC: Spotlight on Adagrasib
Brazel, D., Arter, Z., & Nagasaka, M. (2022) · Lung Cancer Targets and Therapy · doi:10.2147/lctt.s383662 · Cited by 16
Chen, J., Zhang, S., Huang, X., Wang, Q., Xu, W., Huang, J., Su, Y., Sun, Q., Du, X., Xing, B., et al. (2025) · Neoplasia · doi:10.1016/j.neo.2025.101140 · Cited by 15
Programmable PROTAC delivery for precise and spatiotemporal protein degradation
Sheng, J., Ma, T., Wu, Y., & Wang, M. (2026) · Chemical Communications · doi:10.1039/d5cc05651a · Cited by 13
Dai, M., Sridhar, R., Li, R., Tan, R., Yan, K., Fan, G., & Liu, M. (2022) · Technology in Cancer Research & Treatment · doi:10.1177/15330338221095950 · Cited by 14
Thng, D. K. H., Toh, T. B., Pigini, P., Hooi, L., Dan, Y. Y., Chow, P. K. H., Bonney, G. K., Rashid, M. B. M. A., Guccione, E., Wee, D. K. B., et al. (2022) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10363 · Cited by 13
Khalid, K. M., Ratnayake, W. S., Apostolatos, C., & Acevedo-Duncan, M. E. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2023.1213715 · Cited by 12
Yang, L., Du, Y.-E., Liao, F., Huang, T., Liu, Y., Liu, J., Wang, C., Zhan, Z., Cao, Y., Wang, Z., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116486 · Cited by 13
Breaking barriers: Innovative approaches for skin delivery of RNA therapeutics
Subramanian, G., Kalidasan, K., Quah, S., Qi Chou, G. H., Chan, J., Wacker, M. G., & Sampath, P. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.124435 · Cited by 13
Zhao, C., Zhao, F., Yang, L., Wang, Y., Wang, H., Fang, F., Zuo, H., Li, Z., He, G., Zhan, W., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00272 · Cited by 13
Utilizing aptamers in targeted protein degradation strategies for disease therapy
Li, L., Xie, S., Zhou, J., & Ran, J. (2025) · The Journal of Pathology · doi:10.1002/path.6422 · Cited by 13
TGFβ promotes YAP‐dependent AXL induction in mesenchymal‐type lung cancer cells
Choi, J., Lee, H., Kwon, E., Kong, H., Kwon, O., & Cha, H. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12857 · Cited by 13
Ppp6c deficiency accelerates K‐rasG12D‐induced tongue carcinogenesis
Kishimoto, K., Kanazawa, K., Nomura, M., Tanaka, T., Shigemoto-Kuroda, T., Fukui, K., Miura, K., Kurosawa, K., Kawai, M., Kato, H., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.3962 · Cited by 13
Targeting Gαi/s Proteins with Peptidyl Nucleotide Exchange Modulators
Nubbemeyer, B., George, A. A. P., Kühl, T., Pepanian, A., Beck, M. S., Maghraby, R., Boushehri, M. A. S., Muehlhaupt, M., Pfeil, E. M., Annala, S., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00929 · Cited by 13
Applications and Limitations of Oxime‐Linked “Split PROTACs”
Gui, W., & Kodadek, T. J. (2022) · ChemBioChem · doi:10.1002/cbic.202200275 · Cited by 14
Gu, J., Peng, R.-K., Guo, C., Zhang, M., Yang, J., Yan, X. H., Zhou, Q., Li, H., Wang, N., Zhu, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34598-7 · Cited by 15
Rosenkranz, A. A., & Slastnikova, T. A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030987 · Cited by 14
Song, Y., Chua, H. E., Bhowmick, S. S., Choi, B. K. K., & Zhou, S. (2018) · ACM SIGMOD International Conference on Management of Data (SIGMOD) · doi:10.1145/3183713.3196902 · Cited by 13
Drug Design of “Undruggable” Targets
Wang, J., Li, S., & Li, H. (2019) · Chinese Journal of Chemistry · doi:10.1002/cjoc.201800552 · Cited by 13
Targeting STAT3 anti-apoptosis pathways with organic and hybrid organic–inorganic inhibitors
Minus, M. B., Wang, H., Munoz, J. O., Stevens, A. M., Mangubat-Medina, A. E., Krueger, M., Liu, W., Kasembeli, M. M., Cooper, J. C., Kolosov, M. I., et al. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob02682g · Cited by 13
The Discovery of Cryptic Pockets Increases the Druggability of “Undruggable” Proteins
Mou, M., Yang, W., Huang, G., Yang, X., Zhang, X. L., Kandegama, W., Ashby, C. R., Hao, G., & Gao, Y. (2025) · Medicinal Research Reviews · doi:10.1002/med.70001 · Cited by 14
Single-round evolution of RNA aptamers with GRAPE-LM
Zhang, J., Ju, Z., Tang, S., Liu, C., Cai, Y., Zeng, H., Meng, X., Liu, B., Zhang, Y., & Wang, Y. (2026) · Nature Biotechnology · doi:10.1038/s41587-026-03007-5 · Cited by 12
Liao, Y., Chan, S. C., Welsh, E. A., Fang, B., Sun, L., Schönbrunn, E., Koomen, J. M., Duckett, D. R., Haura, E. B., Monastyrskyi, A., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00587 · Cited by 12
Lipid Metabolic Reprogramming in Embryonal Neoplasms with MYCN Amplification
Talapatra, J., & Reddy, M. M. (2023) · Cancers · doi:10.3390/cancers15072144 · Cited by 12
Liu, H., Zhou, Y., Fredimoses, M., Niu, P., Ge, Y., Wu, R. J., Liu, T., Li, P., Shi, Y., Shi, Y., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.131966 · Cited by 12
Untangling the Role of MYC in Sarcomas and Its Potential as a Promising Therapeutic Target
Sias, F., Zoroddu, S., Migheli, R., & Bagella, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26051973 · Cited by 14
The Druggable Transcriptome Project: From Chemical Probes to Precision Medicines
Disney, M. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00006 · Cited by 11
Advancing target validation with PROTAC technology
Spitz, M. L., Kashkush, A., & Benhamou, R. I. (2025) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2025.2490248 · Cited by 12
Wang, Z., Abudurexiti, M., Zhu, W., Li, T., Xu, H., Wan, F., & Ye, D. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-00904-x · Cited by 15
Benhamou, R. I., Abe, M., Choudhary, S., Meyer, S. M., Angelbello, A. J., & Disney, M. D. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00558 · Cited by 12
Control of Intracellular Molecular Networks Using Algebraic Methods
Vieira, L. S., Laubenbacher, R., & Murrugarra, D. (2019) · Bulletin of Mathematical Biology · doi:10.1007/s11538-019-00679-w · Cited by 11
Brachyury: Strategies for Drugging an Intractable Cancer Therapeutic Target
Robinson, H., McFarlane, R. J., & Wakeman, J. A. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.01.014 · Cited by 12
Loss of MYSM1 inhibits the oncogenic activity of cMYC in B cell lymphoma
Lin, Y. H., Wang, H., Fiore, A., Förster, M., Tung, L. T., Belle, J. I., Robert, F., Pelletier, J., Langlais, D., & Nijnik, A. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16554 · Cited by 12
Rosen, H. T., Li, K., Stieger, C. E., Li, E. L., Currier, B., Brittain, S. M., Garcia, F. J., Beard, D. C., Jones, M. D., Haenni‐Holzinger, S., et al. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202508518 · Cited by 15
Approach in Improving Potency and Selectivity of Kinase Inhibitors: Allosteric Kinase Inhibitors
Wei, S., Zhao, T., Wang, J., & Zhai, X. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557521666201222144355 · Cited by 12
Ren, Y., Zhu, X., Fu, K., Zhang, H., Zhao, W., Yang, L., Fang, Q., Wang, J., Chen, Y., & Guo, D. M. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115355 · Cited by 11
Metadata
- Authors
- Dang, C. V., Reddy, E. P., Shokat, K. M., & Soucek, L.
- Affiliations
- The Wistar Institute (US)
- Icahn School of Medicine at Mount Sinai (US)
- Howard Hughes Medical Institute (US)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Corresponding author
- Dang, Chi V.
- Reddy, E. Premkumar
- Shokat, Kevan M.
- Soucek, Laura
- Venue
- Nature Reviews Cancer
- Published
- 2017-06-23
- Volume
- 17
- Issue
- 8
- Pages
- 502-508
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC5945194
- OpenAlex
- W2692768525
- Cited by
- 927
- References
- 57
- Citations by year
- 2026: 93 · 2025: 113 · 2024: 125 · 2023: 110 · 2022: 121 · 2021: 121 · 2020: 113 · 2019: 63 · 2018: 58 · 2017: 10
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (R01CA057341, R01CA158209, R01CA051497)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
- Keywords
- oncogenic Ras, MYC oncogene, oncogene targeting, anticancer drug development
- MeSH terms
- Antineoplastic Agents, Humans, Neoplasms, Receptors, Androgen, Oncogene Proteins, Fusion, Proto-Oncogene Proteins c-myc, NF-kappa B, ras Proteins, Proto-Oncogene Proteins c-myb, Drug Discovery, Molecular Targeted Therapy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review