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Therapeutic Inhibition of Myc in Cancer. Structural Bases and Computer-Aided Drug Discovery Approaches
Open accessAbstract
Myc (avian myelocytomatosis viral oncogene homolog) represents one of the most sought after drug targets in cancer. Myc transcription factor is an essential regulator of cell growth, but in most cancers it is overexpressed and associated with treatment-resistance and lethal outcomes. Over 40 years of research and drug development efforts did not yield a clinically useful Myc inhibitor. Drugging the “undruggable” is problematic, as Myc inactivation may negatively impact its physiological functions. Moreover, Myc is a disordered protein that lacks effective binding pockets on its surface. It is well established that the Myc function is dependent on dimerization with its obligate partner, Max (Myc associated factor X), which together form a functional DNA-binding domain to activate genomic targets. Herein, we provide an overview of the knowledge accumulated to date on Myc regulation and function, its critical role in cancer, and summarize various strategies that are employed to tackle Myc-driven malignant transformation. We focus on important structure-function relationships of Myc with its interactome, elaborating structural determinants of Myc-Max dimer formation and DNA recognition exploited for therapeutic inhibition. Chronological development of small-molecule Myc-Max prototype inhibitors and corresponding binding sites are comprehensively reviewed and particular emphasis is placed on modern computational drug design methods. On the outlook, technological advancements may soon provide the so long-awaited Myc-Max clinical candidate.
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“Two compounds, VPC-70067 (191) and VPC-70063 (192) (Table 3), were ultimately obtained.472”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [472]
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All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,429 · cited 1×
“Free and bound structures of the above-mentioned Myc peptides were modeled using the PREDITOR web server [152] based on dihedral constraints that were obtained from observed NMR chemical shifts, and further energy minimized using CHARMM27 parameters [153].”
MethodComparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Friesner, R. A., Banks, J. L., Murphy, R. B., Halgren, T. A., Klicic, J. J., Mainz, D. T., Repasky, M. P., Knoll, E. H., Shelley, M., Perry, J. K., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0306430 · Cited by 10,057
Halgren, T. A., Murphy, R. B., Friesner, R. A., Beard, H. S., Frye, L. L., Pollard, W. T., & Banks, J. L. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030644s · Cited by 5,340
ZINC − A Free Database of Commercially Available Compounds for Virtual Screening
Irwin, J. J., & Shoichet, B. K. (2005) · Journal of Chemical Information and Modeling · doi:10.1021/ci049714+ · Cited by 4,058
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390
ZINC 15 – Ligand Discovery for Everyone
Sterling, T., & Irwin, J. J. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00559 · Cited by 3,224
Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E., DeBolt, S., Ferguson, D. M., Seibel, G., & Kollman, P. A. (1995) · Computer Physics Communications · doi:10.1016/0010-4655(95)00041-d · Cited by 3,129 · cited 1×
“Five independent 100-nanosecond MD simulations in explicit solvent were then performed, using the Amber molecular dynamics package [129], for each of the following: Myc/PKUMDL-YC-1205, Myc/10074-A4, and Myc/AJ-292/41944612 (an inactive compound) docked complexes as initial structures.”
MethodZINC: A Free Tool to Discover Chemistry for Biology
Irwin, J. J., Sterling, T., Mysinger, M. M., Bolstad, E. S. D., & Coleman, R. G. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci3001277 · Cited by 2,611 · cited 1×
“7 million drug-like compounds from the ~6 million purchasable chemical space of the ZINC12 molecular database [145,146] reduced by physicochemical properties, including charge, number of rotatable bonds, and number of rings.”
BackgroundQuantifying the chemical beauty of drugs
Bickerton, G. R., Paolini, G. V., Besnard, J., Mureşan, S., & Hopkins, A. L. (2012) · Nature Chemistry · doi:10.1038/nchem.1243 · Cited by 2,397
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Items 101–175 of 175
Role of liquid–liquid phase separation in cancer: Mechanisms and therapeutic implications
Li, X., & Yu, Z. (2024) · Cancer Innovation · doi:10.1002/cai2.144 · Cited by 8
“However, IDRs such as MYC lack conventional “ protein pockets ” , rendering them devoid of drug targets [85].”
BackgroundXu, J., Xu, X., Yang, L., & Xu, X. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114407 · Cited by 7
Singh, A. K., Kumar, A., Kumar, P., Bhardwaj, T., Giri, R., & Garg, N. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0087 · Cited by 7
miRNome expression analysis in canine diffuse large B-cell lymphoma
Elshafie, N. O., Gribskov, M., Lichti, N. I., Sayedahmed, E. E., Childress, M. O., & dos Santos, A. P. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1238613 · Cited by 7
Biflorin inhibits the proliferation of gastric cancer cells by decreasing MYC expression
Barbosa-Jobim, G. S., Costa-Lira, É., Ralph, A. C. L., Souza, L. G. D. S., Lemos, T. L. G., Burbano, R. M. R., Calcagno, D. Q., Smith, M. D. A. C., Montenegro, R. C., & de Vasconcellos, M. C. (2019) · Toxicology in Vitro · doi:10.1016/j.tiv.2019.104735 · Cited by 7
Shirey, R. J., Hart, J. R., Sridharan, B., Novick, S. J., Turner, L. D., Zhou, B., Nielsen, A. L., Eubanks, L. M., Ueno, L. A., Hixon, M. S., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116246 · Cited by 6
Tissue-Based Diagnostic Biomarkers of Aggressive Variant Prostate Cancer: A Narrative Review
Kouroukli, O., Bravou, V., Giannitsas, K., & Tzelepi, V. (2024) · Cancers · doi:10.3390/cancers16040805 · Cited by 7
“Compounds that indirectly target MYCN by disrupting its heretodimerization with myc-associated factor X (MAX), for example, have been developed [112,113].”
BackgroundMechanism and application of nonessential amino acid deprivation associated with tumor therapy
Nong, S., Qian, Y., Zhang, T., Zhou, X., Wei, Y., Yin, X., & Ma, X. (2022) · MedComm – Future Medicine · doi:10.1002/mef2.12 · Cited by 6
Lind, J., Aksoy, O., Prchal‐Murphy, M., Fan, F., Fulciniti, M., Stoiber, D., Bakiri, L., Wagner, E. F., Zwickl-Traxler, E., Sattler, M., et al. (2024) · Blood Cancer Journal · doi:10.1038/s41408-024-01117-4 · Cited by 6
Zeng, L., Yuan, C., Shu, J. S., Qian, J., Wu, Q., Chen, Y., Wu, R., Ouyang, X., Li, Y., & Mei, W. (2022) · Molecules · doi:10.3390/molecules27061897 · Cited by 6
Nilotinib: Disrupting the MYC-MAX Heterocomplex
Shah, K., Ansari, M., Saeed, S., Wali, A., & Mushtaq, M. (2024) · Bioinformatics and Biology Insights · doi:10.1177/11779322241267056 · Cited by 5
Luminescence complementation technology for the identification of MYC:TRRAP inhibitors
Feris, E. J., Hinds, J. W., & Cole, M. D. (2021) · Oncotarget · doi:10.18632/oncotarget.28078 · Cited by 4
“Despite attempts at inhibiting MYC expression, its direct interaction with DNA and its obligate partner MAX, or any indirect MYC effectors, no clinically useful drug has emerged in nearly 20 years due to poor accessibility and specificity [9, 11, 12].”
InfluentialGolgi-localized Ring Finger Protein 121 is necessary for MYCN-driven neuroblastoma tumorigenesis
Cheung, B. B., Mittra, R., Murray, J. E., Wang, Q., Seneviratne, J. A., Raipuria, M., Wong, I. P. L., Restuccia, D. F., Gifford, A. J., Salib, A., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06899-8 · Cited by 4
Cellular experiments to study the inhibition of c-Myc/MAX heterodimerization
Singh, A. K., Sharma, S., Kumar, P., & Garg, N. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.07.009 · Cited by 4
Longoria-García, S., Sanchez-Dominguez, C. N., Sánchez‐Domínguez, M., Delgado-Balderas, J. R., Islas, J. F., Vidal-Gutiérrez, Ó., & Gallardo‐Blanco, H. L. (2023) · Nanomaterials · doi:10.3390/nano13202802 · Cited by 4
“Disruption of Myc:Max heterodimerization or their binding to the CME and non-CME is a current therapeutic strategy to treat cancer [10].”
BackgroundRNA-binding proteins in bone pathophysiology
Maroni, P., Pesce, N. A., & Lombardi, G. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1412268 · Cited by 4
Gupta, P., Chaudagar, K. K., Saha, S. S., Bynoe, K. M., Maillat, L., Heiss, B. L., Stadler, W. M., & Patnaik, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.17.198598 · Cited by 4
“However despite multiple pharmaceutical efforts, c-myc has remained 85 “undruggable” (9-11).”
BackgroundMYC Point Mutations in Cancer: A Reboot and a Sequel
Luca, D. D., Munafò, C., Lorenzi, L., & Cucco, F. (2025) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-25-0940 · Cited by 3
Preclinical Studies of PROTACs in Hematological Malignancies
Fuchs, O., & Bokorová, R. (2021) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/1871529x21666210308111546 · Cited by 3
Li, S., Wang, Y., Yin, J., Li, K., Liu, L., & Gao, J. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e28411 · Cited by 3
“A plethora of strategies, both direct and indirect, have been employed to target c-Myc by exploiting its multiple regulatory mechanisms, encompassing c-Myc transcription and mRNA stability, c-Myc protein stability and degradation, as well as c-Myc binding to its interactome Max [19].”
BackgroundMyc 9aaTAD activation domain binds to mediator of transcription with superior high affinity
Knight, A., Houser, J., Otaševič, T., Juráň, V., Vybíhal, V., Smrčka, M., & Piskáček, M. (2024) · Molecular Medicine · doi:10.1186/s10020-024-00896-7 · Cited by 3
Therapeutic approaches targeting oncogenic proteins in myeloid leukemia: challenges and perspectives
Yan, X. Y., Kang, Y. Y., Zhang, Z. Y., Huang, P. C., Yang, C., & Naranmandura, H. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2443577 · Cited by 3
“Clinical studies have proved that AML patients with elevated levels of c-Myc exhibited more aggressive clinical manifestations, shorter median survival, and progression-free survival, in addition to a higher propensity for relapse following chemotherapy [88,91].”
Sengupta, P., & Chatterjee, S. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129649 · Cited by 3
Yao, K., Fan, H., Yang, T., Yang, C., Wang, G., Li, X., Ji, X., Wang, Q., Lv, S., & Guo, S. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1497919 · Cited by 2
Yang, Y., Jia, X., Yu, P., Lu, S.-H., Wang, C., Zhang, H., Wang, X., Zhou, Q., Sun, Y., & Wang, G. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217948 · Cited by 2
Chang, L., Oblinger, J. L., Wu, L. M. N., Miller, C. R., & Burns, S. S. (2025) · Cancer Research Communications · doi:10.1158/2767-9764.crc-25-0563 · Cited by 2
Structure-based drug design of small-molecule c-Myc G-quadruplex binders
Gao, J., Xu, C.-X., Hong, R., Cheng, G., & Jia, P. (2026) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-025-00760-8 · Cited by 3
Chen, H., Fu, R., & Wu, Z. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01877-8 · Cited by 3
“Selectivity represents a second major obstacle [31, 161].”
C9orf16 represents the aberrant genetic programs and drives the progression of PDAC
Chen, X., Zhang, H., & Xiao, B. (2022) · BMC Cancer · doi:10.1186/s12885-022-10202-5 · Cited by 2
An oncoprotein CREPT functions as a co-factor in MYC-driven transformation and tumor growth
Li, M., Li, J., He, C., Jiang, G., Ma, D., Guan, H., Lin, Y.-T., Li, M., Jia, J., Duan, X., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108030 · Cited by 2
“Notably, MYC regulation during the cell cycle is complex and involves multiple pathways and proteins that interact with it at various stages (5, 37).”
A novel role for Neurog2 in MYCN driven neuroendocrine plasticity of prostate cancer
Walke, P., Price, J. D. W., Vizeacoumar, F. S., Joseph, N., Maranda, V., Chowdhury, B., Patel, J., Zhang, Y., Dong, H., New, L., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03413-0 · Cited by 3
“Various strategies, including small molecules targeting the N-Myc-MAX interaction or direct modulation of N-Myc function, have shown promise in preclinical models [13].”
Taillandier, D. (2021) · Biologie Aujourd hui · doi:10.1051/jbio/2021006 · Cited by 2
Pragati, & Sarkar, S. (2021) · BioFactors · doi:10.1002/biof.1721 · Cited by 2
Welsh, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136939 · Cited by 1
Therapeutic peptidomimetics: targeting the undruggable space
Mabonga, L., Masamba, P., & Kappo, A. P. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-820141-1.00026-1 · Cited by 1
Designing metabolic target-specific inhibitors for cancer therapy
Singh, T., Kharat, A. S., Rathi, B., & Kumar, D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99879-6.00011-0 · Cited by 1
Bamrah, G. K., Kumari, N., & Srivastava, S. (2024) · Proceedings of the Indian National Science Academy · doi:10.1007/s43538-024-00244-7 · Cited by 1
Fotinopoulos, P., Fortis, S. P., Mahaira, L., Salagianni, M. L., Pergialiotis, V., Daskalakis, G., Papantoniou, N. E., Antsaklis, A. J., & Pappa, K. I. (2024) · Hellenic Journal of Obstetrics and Gynecology · doi:10.33574/hjog.0548 · Cited by 1
MYC: Master Regulator of Cell Death and Tumor Progression
Capasso, L., Mele, D., Fayyaz, F., Altucci, L., & Nebbioso, A. (2025) · Biochemistry · doi:10.5772/intechopen.1008763 · Cited by 2
Fu, Y., Jiang, L., Xie, G., Peng, Y., Fu, Y., Zhu, Q., Liu, Y., Zhao, G., Liu, X., Peng, Y., et al. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01744-3 · Cited by 2
“Similarly, NSC13728 and KI-MS2-008 stabilize Max-Max protein homodimers, disrupting Myc-Max heterodimer formation and its subsequent signaling 27,28 .”
Wang, X., Sun, H., Xiao, W., Zhang, Y., Lu, X., Gong, Z., Li, D., Liu, S., Xia, X., Wang, H., et al. (2025) · Non-coding RNA Research · doi:10.1016/j.ncrna.2025.12.001 · Cited by 1
“Myelocytomatosis Viral Oncogene Homolog (MYC), a transcription factor, binds to E-box sequences in DNA to regulate cell proliferation and metabolism [62,63].”
Breaking the bonds: targeting protein dimerization for prostate cancer therapy
Singh, N., & Heemers, H. V. (2026) · Endocrinology · doi:10.1210/endocr/bqag056 · Cited by 1
USP25 Promotes Glycolysis of Acute Myeloid Leukemia Cells and Enhances Tumor Immunity
Wang, N., Yang, C., Zhang, R., Ren, W., & Shen, B. (2026) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.2478/aite-2026-0020 · Cited by 1
“Thus, targeting of c-Myc has been revealed as thera-peutical strategies for AML treatment (Brondfield et al. 2015; Carabet et al. 2018).”
Shehzadi, S. A., Naveed, S., Khan, D., Arif, K., Islam, A., Hassan, M., Kloczkowski, A., Hassan, E. S., & Abdelhameed, A. S. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110318 · Cited by 1
Tool and Techniques on Computer-Aided Drug Design for Targeted Cancer Therapy
Niveditha, V. G., Sindhu, V., Kizhakedathil, M. P. J., Sundari, I. S., & Balasubramaniyan, M. (2023) · Biological and medical physics, biomedical engineering · doi:10.1007/978-981-19-9786-0_23 · Cited by 1
In Silico Study of the Anti-MYC Potential of Lanostane-Type Triterpenes
de Oliveira, J. A. C., Negreiro, J. M., Nunes, F. M., Barbosa, F. G., Mafezoli, J., de Mattos, M. C., Fernandes, M. E. G. C., Pessoa, C., Furtado, C. L. M., Zanatta, G., et al. (2024) · ACS Omega · doi:10.1021/acsomega.4c10201 · Cited by 1
Identifying and Validating MYC:Protein Interactors in Pursuit of Novel Anti-MYC Therapies
Resetca, D., MacDonald, A. S., Kenney, T. M. G., Wei, Y., Arrowsmith, C. H., Raught, B., & Penn, L. Z. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1476-1_4 · Cited by 1
Cell-Based Methods for the Identification of Myc-Inhibitory Small Molecules
Burkhart, C. A., Haber, M., Norris, M. D., Gudkov, A. V., & Nikiforov, M. A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1476-1_19 · Cited by 1
Kakegawa, S., Matsumoto, I., Tamura, M., Takata, M., Yoshida, S., Saito, D., Tanaka, Y., Takemura, H., & Ooi, A. (2020) · PubMed Central
Inchworm stepping of Myc-Max heterodimer protein diffusion along DNAPreprint
Dai, L.-Q., & Yu, J. (2020) · bioRxiv · doi:10.1101/2020.06.17.156398 · Cited by 11
“Computational studies have been conducted mostly toward Myc-Max inhibition for drug discovery approaches [41-43].”
BackgroundPreventing cancer by long-term partial Myc suppressionPreprint
Sodir, N. M., Pellegrinet, L., Kortlever, R. M., Kwon, Y.-W., Kim, S., Garcia, D. A., Perfetto, A., Anastasiou, P., Swigart, L. B., Littlewood, T. D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.30.422650
Hall, F. L., & Gordon, E. M. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.97057
myc Gene and Cancer Variant Analysis and Network Interaction: An In-Silico Analysis
Kabrah, S. M., Qadah, T., & Flemban, A. F. (2021) · Indian Journal of Forensic Medicine & Toxicology · doi:10.37506/ijfmt.v16i1.17791
Structural characterization and selective drug targeting of higher-order DNA G-quadruplex systems.
Monsen, R. C. (2020) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/3553
Machine-Learning Based Drug and Supplement Design Platform for Chronic Disease Control
Qi, P. (2022) · International Conference on Biomedical Engineering and Applications (ICBEA) · doi:10.1145/3543081.3543092
“Myc inhibition, however, has been shown to have a strong negative impact on the physiological functions of normal somatic cells [17].”
BackgroundXie, Y., Zhang, W., Guo, L., Kril, L. M., Begley, K. L., Sviripa, V. M., Chen, X., Liu, X., Lee, E. Y., He, D., et al. (2023) · doi:10.1158/1535-7163.c.6542721.v1
Xie, Y., Zhang, W., Guo, L., Kril, L. M., Begley, K. L., Sviripa, V. M., Chen, X., Liu, X., Lee, E. Y., He, D., et al. (2023) · doi:10.1158/1535-7163.c.6542721
Sriratanasak, N., Chanvorachote, P., & Luanpitpong, S. (2019) · doi:10.58837/chula.the.2019.428
Undruggable oncoproteins cMyc and NMyc bind to mediator of transcription with superior high affinityPreprint
Knight, A., Houser, J., Otaševič, T., Juráň, V., Vybíhal, V., Smrčka, M., & Piskáček, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.15.585150
“The c-Myc protein harbors conserved regions MB0 ( 10-32 10-32 ), MBI (44-63 Despite four decades of research and drug development, c-Myc has been recognized as highly undruggable oncotarget [21,22].”
BackgroundZhang, E., Chen, Z., Liu, W., Lin, L., Wu, L., Guan, J., Wang, J., Kong, C., Bi, J., & Zhang, M. (2024) · Figshare · doi:10.6084/m9.figshare.24934414
A novel role for Neurog2 in MYCN driven neuroendocrine plasticity of prostate cancerPreprint
Vizeacoumar, F. J., Walke, P., Price, J. D. W., Vizeacoumar, F. S., Joseph, N., Maranda, V., Chowdhury, B., Patel, J., Zhang, Y., Dong, H., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-5313977/v1
Cloud Computation Methods to Accelerate Breast Cancer Drug Discovery through Molecular Modeling
Kobi, J., & Nchaw, A. N. (2025) · doi:10.38124/ijisrt/25may2204
Llombart, V., O’Connor, D., Demeulemeester, J., Bhamra, A., Šurinová, S., Turňa, A., Fung, K. T. M., Wang, L., Li, Y., Rapoz-D’Silva, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.16.659507
Experimental Treatment in Prostate Cancer: Gene Profiling and Genetic
van der Poel, H. G. (2025) · Springer eBooks · doi:10.1007/978-3-031-55405-6_8
PA2G4 Functions as a Cofactor for MYC Family Oncoproteins in MYC-Driven Malignancies
Krishan, S., Koach, J., Lim, T., Yeo, K. K. L., Cheong, F., Luo, J.-S., Massudi, H., Gao, X., Heangsarath, S., Kueh, A. J., et al. (2025) · Cells · doi:10.3390/cells14181422
Sen, A., Bhowmik, A. D., Mandal, S., Mondal, P., Chattopadhyay, A., & Rath, J. (2025) · Natural Product Research · doi:10.1080/14786419.2025.2571860
Zhang, E., Chen, Z., Liu, W., Lin, L., Wu, L., Guan, J., Wang, J., Kong, C., Bi, J., & Zhang, M. (2024) · Figshare · doi:10.6084/m9.figshare.24934723
SHP2 promotes osteosarcoma via regulating STAT3/TET3/HOXB2 signaling
Yang, H., & Ji, J. (2026) · Scientific Reports · doi:10.1038/s41598-026-35493-7
“Up to 70% of human tumors, especially those that are very aggressive and resistant to therapy, have aberrant overexpression of c-Myc, which is extensively expressed in a variety of tissues and organs 41 .”
Pradhan, S., Kasana, S., Kurmi, B. D., & Patel, P. (2026) · Archiv der Pharmazie · doi:10.1002/ardp.70196
Nanobody‐Mediated c‐MYC Degradation Inhibits Tumor Cell Progression
Xue, Y., Jiang, H., Zong, Z., Tian, X., Miao, Z., Li, T., Wei, Y., & Deng, H. (2026) · MedComm · doi:10.1002/mco2.70701
“Unlike other oncogenic proteins, c-MYC lacks well-defined pockets or grooves for small-molecule binding, rendering it “undruggable” by conventional methods [ 22–24 ].”
HNRNPU mutations redirect cell cycle control to E2F in MYC-driven lymphomas
Qureshi, Q., Coyle, K. M., Brown, C., Thomas, N., Collinge, B. J., Dreval, K., Steidl, C., Scott, D. W., Audas, T. E., & Morin, R. D. (2026) · Blood Advances · doi:10.1182/bloodadvances.2025019135
Chemical intervention strategies targeting MYC for cancer therapy
Wu, D., Zhu, Y., Ye, M., Guo, X., Jiang, Z., & Zhang, X. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104726
Pinoresinol as a Potential c-Myc Complex Modulator: An In Silico Study
Villanueva-Castillo, A., Mancilla-Simbro, C., Villa-Díaz, F., Ramírez-Mata, A., Pastelín, C. F., Moreno-Mejía, R. S., Lucio‐Castillo, H., Castro-Bautista, B. L., Castillo-Sosa, C. G., Matamoros-González, F., et al. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48080833
BindingDB Entry 50021153: MYC the oncogene from hell: Novel opportunities for cancer therapy.
BindingDB (2025) · UC San Diego · doi:10.7270/q2qz2gkz
BindingDB Entry 50018504: Targeting MYC: From understanding its biology to drug discovery.
BindingDB (2024) · UC San Diego · doi:10.7270/q2qz2g61
Metadata
- Authors
- Carabet, L. A., Rennie, P. S., & Cherkasov, A.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Cherkasov, Artem
- ORCID
- Cherkasov, Artem
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2018-12-29
- Volume
- 20
- Issue
- 1
- Pages
- 120
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6337544
- OpenAlex
- W2907541282
- Cited by
- 172
- References
- 213
- Citations by year
- 2026: 11 · 2025: 23 · 2024: 29 · 2023: 17 · 2022: 23 · 2021: 29 · 2020: 26 · 2019: 14
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- cIRcle (University of British Columbia) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Open Collections
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
- Keywords
- c-Myc, MYC inhibitors, undruggable targets, intrinsically disordered proteins, small molecule inhibitors, structure-function relationship, protein-protein interaction, DNA-binding domain, cancer therapy resistance, computer-aided drug design
- MeSH terms
- Animals, Antineoplastic Agents, Humans, Protein Binding, Proto-Oncogene Proteins c-myc, Quantitative Structure-Activity Relationship, Small Molecule Libraries, Drug Discovery, Molecular Docking Simulation
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