Stabilization of the Max Homodimer with a Small Molecule Attenuates Myc-Driven Transcription
Open accessAbstract
The transcription factor Max is a basic-helix-loop-helix leucine zipper (bHLHLZ) protein that forms homodimers or interacts with other bHLHLZ proteins, including Myc and Mxd proteins. Among this dynamic network of interactions, the Myc/Max heterodimer has crucial roles in regulating normal cellular processes, but its transcriptional activity is deregulated in a majority of human cancers. Despite this significance, the arsenal of high-quality chemical probes to interrogate these proteins remains limited. We used small molecule microarrays to identify compounds that bind Max in a mechanistically unbiased manner. We discovered the asymmetric polycyclic lactam, KI-MS2-008, which stabilizes the Max homodimer while reducing Myc protein and Myc-regulated transcript levels. KI-MS2-008 also decreases viable cancer cell growth in a Myc-dependent manner and suppresses tumor growth in vivo. This approach demonstrates the feasibility of modulating Max with small molecules and supports altering Max dimerization as an alternative approach to targeting Myc.
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In 2019, Struntz et al. utilized SMM screening to identify KI-MS2-001 (IC50 = 1.98 μM), a molecule with a unique asymmetric polycyclic lactam compound.
“In 2019, Struntz et al. utilized SMM (small molecule microarray) screening to identify KI-MS2-001 (168) (IC50 = 1.98 μM), a molecule with a unique asymmetric polycyclic lactam compound.422”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
Experimental data indicate that KI-MS2-008 is effective in reducing tumor size at a low dose (0.06 mg·kg−1, iv) in mouse T-cell acute lymphoblastic leukemia (T-ALL) transplant tumor models.
“Experimental data indicate that KI-MS2-008 is effective in reducing tumor size at a low dose (0.06 mg·kg−1, iv) in mouse T-cell acute lymphoblastic leukemia (T-ALL) transplant tumor models.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
Stabilizing the Max-Max homodimer can prevent Myc-Max transactivation of target genes.
“Thus, stabilizing the Max-Max homodimer can prevent Myc-Max transactivation of target genes.422”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
Formation of Max-Max homodimer provides an alternative mechanism for blocking Myc/Max interactions and preventing Myc/Max heterodimers from binding to DNA, resulting in reduced transcriptional activity.
“On the other hand, formation of Max-Max homodimer provides an alternative mechanism for blocking Myc/Max interactions and preventing Myc/Max heterodimers from binding to DNA, resulting in reduced transcriptional activity.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
Further structural optimization led to the development of KI-MS2-008 (IC50 = 1.28 μM), which exhibits significantly increased binding affinity for Max-Max homodimers, reduces Myc protein levels, perturbs Myc-driven transcriptional programs, induces Myc-dependent cellular differentiation, and affects viable cell growth of both engineered and non-engineered cell lines.
“Further structural optimization led to the development of KI-MS2-008 (IC50 = 1.28 μM), which exhibits significantly increased binding affinity for Max-Max homodimers, reduces Myc protein levels, perturbs Myc-driven transcriptional programs, induces Myc-dependent cellular differentiation, and affects viable cell growth of both engineered and non-engineered cell lines.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
KI-MS2-008 stabilizes Max homodimers and renders Max less capable of binding Myc.
“KI-MS2-008 (Fig. 6), an optimized analog of one of the drug hits, stabilizes Max homodimers and thus renders Max less capable of binding Myc.107”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [107]
Cites
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860 · see citing works
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482 · see citing works
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638 · see citing works
The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041 · see citing works
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625 · see citing works
Self-citationUltrafast and memory-efficient alignment of short DNA sequences to the human genome.
Langmead, B., Trapnell, C., Pop, M., & Salzberg, S. L. (2009) · Genome Biology · doi:10.1186/gb-2009-10-3-r25 · Cited by 21,849 · see citing works
Self-citationModel-based Analysis of ChIP-Seq (MACS)
Zhang, Y., Liu, T., Meyer, C. A., Eeckhoute, J., Johnson, D. S., Bernstein, B. E., Nusbaum, C., Myers, R. M., Brown, M., Li, W., et al. (2008) · Genome Biology · doi:10.1186/gb-2008-9-9-r137 · Cited by 18,386 · see citing works
Differential expression analysis for sequence count data
Anders, S., & Huber, W. (2010) · Genome Biology · doi:10.1186/gb-2010-11-10-r106 · Cited by 15,581 · see citing works
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807 · see citing works
Dang, C. V. (2012) · Cell · doi:10.1016/j.cell.2012.03.003 · Cited by 3,390 · see citing works
Detection of Influential Observation in Linear Regression
Cook, R. D. (1977) · Technometrics · doi:10.1080/00401706.1977.10489493 · Cited by 2,284 · see citing works
Detection of Influential Observation in Linear Regression
Cook, R. D. (2000) · Technometrics · doi:10.2307/1271434 · Cited by 2,277 · see citing works
Kay, L., Keifer, P. A., & Saarinen, T. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00052a088 · Cited by 2,268 · see citing works
Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay
Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261 · see citing works
The cellular thermal shift assay for evaluating drug target interactions in cells
Jafari, R., Almqvist, H., Axelsson, H., Ignatushchenko, M., Lundbäck, T., Nordlund, P., & Molina, D. M. (2014) · Nature Protocols · doi:10.1038/nprot.2014.138 · Cited by 1,521 · see citing works
Transcriptional Amplification in Tumor Cells with Elevated c-Myc
Lin, C. Y., Lovén, J., Rahl, P. B., Paranal, R. M., Burge, C. B., Bradner, J. E., Lee, T. I., & Young, R. A. (2012) · Cell · doi:10.1016/j.cell.2012.08.026 · Cited by 1,498 · see citing works
Self-citationTranscription factors as targets for cancer therapy
Darnell, J. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc906 · Cited by 1,194 · see citing works
Palmer, A. G. I., Cavanagh, J., Wright, P. E., & Rance, M. (1991) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(91)90036-s · Cited by 948 · see citing works
Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression
Laherty, C. D., Yang, W., Sun, J.-M., Davie, J., Seto, E., & Eisenman, R. N. (1997) · Cell · doi:10.1016/s0092-8674(00)80215-9 · Cited by 933 · see citing works
Reversible tumorigenesis by MYC in hematopoietic lineages.
Felsher, D., & Bishop, J. (1999) · Molecules and Cells · doi:10.1016/s1097-2765(00)80367-6 · Cited by 917 · see citing works
Self-citationGrzesiek, S., & Bax, A. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00079a052 · Cited by 892 · see citing works
MYC inactivation uncovers pluripotent differentiation and tumour dormancy in hepatocellular cancer
Shachaf, C. M., Kopelman, A. M., Arvanitis, C., Karlsson, Å., Beer, S., Mandl, S., Bachmann, M. H., Borowsky, A. D., Ruebner, B., Cardiff, R. D., et al. (2004) · Nature · doi:10.1038/nature03043 · Cited by 874 · see citing works
Self-citationSequence-Specific DNA Binding by the c-Myc Protein
Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., & Weintraub, H. M. (1990) · Science · doi:10.1126/science.2251503 · Cited by 863 · see citing works
Conditional mouse lung cancer models using adenoviral or lentiviral delivery of Cre recombinase
DuPage, M. J. P., Dooley, A. L., & Jacks, T. (2009) · Nature Protocols · doi:10.1038/nprot.2009.95 · Cited by 862 · see citing works
Modelling Myc inhibition as a cancer therapy
Soucek, L., Whitfield, J. R., Martins, C. P., Finch, A. J., Murphy, D. J., Sodir, N. M., Karnezis, A. N., Swigart, L. B., Nasi, S., & Evan, G. I. (2008) · Nature · doi:10.1038/nature07260 · Cited by 822 · see citing works
MYC Activation Is a Hallmark of Cancer Initiation and MaintenancePreprint
Gabay, M., Li, Y., & Felsher, D. W. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014241 · Cited by 808 · see citing works
Self-citationA general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients
Schleucher, J., Schwendinger, M. G., Sattler, M., Schmidt, P. M., Schedletzky, O., Glaser, S. J., S�rensen, O., & Griesinger, C. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175254 · Cited by 808 · see citing works
Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
Ayer, D. E., Kretzner, L., & Eisenman, R. N. (1993) · Cell · doi:10.1016/0092-8674(93)90661-9 · Cited by 697 · see citing works
Sustained Loss of a Neoplastic Phenotype by Brief Inactivation of MYC
Jain, M., Arvanitis, C., Chu, K., Dewey, W. C., Leonhardt, E. A., Trinh, M., Sundberg, C. D., Bishop, J. M., & Felsher, D. W. (2002) · Science · doi:10.1126/science.1071489 · Cited by 647 · see citing works
Self-citationpwr: Basic Functions for Power Analysis
Champely, S. (2006) · doi:10.32614/cran.package.pwr · Cited by 603 · see citing works
X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA
Nair, S. K., & Burley, S. K. (2003) · Cell · doi:10.1016/s0092-8674(02)01284-9 · Cited by 551 · see citing works
MYC: Connecting selective transcriptional control to global RNA production
Kress, T. R., Sabò, A., & Amati, B. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3984 · Cited by 521 · see citing works
Zeller, K. I., Jegga, A. G., Aronow, B. J., O’Donnell, K. A., & Dang, C. V. (2003) · Genome biology · doi:10.1186/gb-2003-4-10-r69 · Cited by 483 · see citing works
Farrell, A. S., & Sears, R. C. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014365 · Cited by 468 · see citing works
Riss, T., Moravec, R. A., Niles, A. L., Duellman, S. J., Benink, H. A., Worzella, T. J., & Minor, L. K. (2016) · Europe PMC (PubMed Central) · Cited by 465 · see citing works
Low molecular weight inhibitors of Myc–Max interaction and function
Yin, X., Giap, C., Lazo, J. S., & Prochownik, E. V. (2003) · Oncogene · doi:10.1038/sj.onc.1206641 · Cited by 426 · see citing works
An Overview of MYC and Its Interactome
Conacci-Sorrell, M., McFerrin, L., & Eisenman, R. N. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014357 · Cited by 408 · see citing works
Photoaffinity Labeling in Target- and Binding-Site Identification
Smith, E. M., & Collins, I. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.14.152 · Cited by 356 · see citing works
Clemons, P. A., Bodycombe, N. E., Carrinski, H. A., Wilson, J. A., Shamji, A. F., Wagner, B. K., Koehler, A. N., & Schreiber, S. L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012741107 · Cited by 343 · see citing works
Self-citationTsubuki, S., Saito, Y., Tomioka, M., Itô, H., & Kawashima, S. (1996) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021280 · Cited by 308 · see citing works
A small molecule that binds Hedgehog and blocks its signaling in human cells
Stanton, B. Z., Peng, L. F., Maloof, N., Nakai, K., Wang, X., Duffner, J. L., Taveras, K. M., Hyman, J. M., Lee, S. W., Koehler, A. N., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.142 · Cited by 297 · see citing works
Self-citationControl of cell growth by c-Myc in the absence of cell division
Schuhmacher, M., Staege, M. S., Pajic, A., Polack, A., Weidle, U. H., Bornkamm, G. W., Eick, D., & Kohlhuber, F. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80507-7 · Cited by 288 · see citing works
MYC Disrupts the Circadian Clock and Metabolism in Cancer Cells
Altman, B. J., Hsieh, A. L., Sengupta, A., Krishnanaiah, S. Y., Stine, Z. E., Walton, Z. E., Gouw, A. M., Venkataraman, A., Li, B., Goraksha-Hicks, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.003 · Cited by 273 · see citing works
Self-citationTherapeutic Strategies to Inhibit MYCPreprint
McKeown, M. R., & Bradner, J. E. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014266 · Cited by 226 · see citing works
Characterization of directed differentiation by high-throughput single-cell RNA-SeqPreprint
Soumillon, M., Cacchiarelli, D., Semrau, S., van Oudenaarden, A., & Mikkelsen, T. S. (2014) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/003236 · Cited by 217 · see citing works
Cell cycle activation by c-myc in a Burkitt lymphoma model cell line
Pajic, A., Spitkovsky, D., Christoph, B., Kempkes, B., Schuhmacher, M., Staege, M. S., Brielmeier, M., Ellwart, J. W., Kohlhuber, F., Bornkamm, G. W., et al. (2000) · International Journal of Cancer · doi:10.1002/1097-0215(20000915)87:6 · Cited by 204 · see citing works
A complex task? Direct modulation of transcription factors with small molecules
Koehler, A. N. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.03.022 · Cited by 189 · see citing works
Self-citationMAX and MYC: A Heritable Breakup
Cascón, A., & Robledo, M. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3891 · Cited by 177 · see citing works
Omomyc, a potential Myc dominant negative, enhances Myc-induced apoptosis.
Soucek, L., Jucker, R., Panacchia, L., Ricordy, R., Tatò, F., & Nasi, S. (2002) · PubMed · Cited by 160 · see citing works
Inhibitor of MYC identified in a Kröhnke pyridine library
Hart, J. R., Garner, A. L., Yu, J., Ito, Y., Sun, M., Ueno, L. A., Rhee, J., Baksh, M. M., Stefan, E., Hartl, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1319488111 · Cited by 150 · see citing works
Self-citationDevelopment and application of diazirines in biological and synthetic macromolecular systems
Blencowe, A., & Hayes, W. (2005) · Soft Matter · doi:10.1039/b501989c · Cited by 144 · see citing works
Lu, T., Lu, R., Liao, M., Yu, J., Chung, C.-H., Kao, C.-F., & Wu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077081 · Cited by 130 · see citing works
Target Identification by Diazirine Photo‐Cross‐Linking and Click Chemistry
MacKinnon, A. L., & Taunton, J. (2009) · Current Protocols in Chemical Biology · doi:10.1002/9780470559277.ch090167 · Cited by 128 · see citing works
Felsenstein, K. M., Saunders, L. B., Simmons, J. K., Leon, E. C., Calabrese, D. R., Zhang, S., Michalowski, A. M., Gareiss, P. C., Mock, B. A., & Schneekloth, J. S. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00577 · Cited by 125 · see citing works
Felsher, D. W. (2010) · Genes & Cancer · doi:10.1177/1947601910377798 · Cited by 122 · see citing works
Self-citationActivity‐Based Protein Profiling (ABPP) and Click Chemistry (CC)–ABPP by MudPIT Mass Spectrometry
Speers, A. E., & Cravatt, B. F. (2009) · Current Protocols in Chemical Biology · doi:10.1002/9780470559277.ch090138 · Cited by 117 · see citing works
Mlx, a Novel Max-like BHLHZip Protein That Interacts with the Max Network of Transcription Factors
Billin, A. N., Eilers, A. L., Quéva, C., & Ayer, D. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36344 · Cited by 99 · see citing works
Small-molecule microarrays as tools in ligand discovery
Vegas, A. J., Fuller, J. H., & Koehler, A. N. (2008) · Chemical Society Reviews · doi:10.1039/b703568n · Cited by 94 · see citing works
Self-citationThe Nerve Growth Factor-Responsive PC12 Cell Line Does Not Express the Myc Dimerization Partner Max
Hopewell, R., & Ziff, E. B. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3470 · Cited by 87 · see citing works
Therapeutic Effects of an Anti-Myc Drug on Mouse Pancreatic Cancer
Stellas, D., Szabolcs, M. J., Koul, S., Li, Z., Polyzos, A., Anagnostopoulos, C., Cournia, Z., Tamvakopoulos, C., Klinakis, A., & Efstratiadis, A. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju320 · Cited by 83 · see citing works
Targeted Disruption of Myc–Max Oncoprotein Complex by a Small Molecule
Choi, S. H., Mahankali, M., Lee, S. J., Hull, M. V., Petrassi, H. M., Chatterjee, A. K., Schultz, P. G., Jones, K. A., & Shen, W. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00799 · Cited by 75 · see citing works
A Small Molecule That Binds and Inhibits the ETV1 Transcription Factor Oncoprotein
Pop, M. S., Stransky, N., Garvie, C. W., Theurillat, J.-P. P., Hartman, E. C., Lewis, T. A., Zhong, C. F., Culyba, E. K., Lin, F., Daniels, D. S., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0689 · Cited by 65 · see citing works
Self-citationMitchell, J. M., & Shaw, J. T. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200503341 · Cited by 64 · see citing works
Stabilizers of the Max Homodimer Identified in Virtual Ligand Screening Inhibit Myc Function
Jiang, H., Bower, K. E., Beuscher, A. E., Zhou, B., Bobkov, A. A., Olson, A. J., & Vogt, P. K. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.054858 · Cited by 62 · see citing works
Derr, A. G., Yang, C., Žilionis, R., Sergushichev, A., Blodgett, D. M., Redick, S. D., Bortell, R., Luban, J., Harlan, D. M., Kadener, S., et al. (2016) · Genome Research · doi:10.1101/gr.207902.116 · Cited by 62 · see citing works
Soodgupta, D., Pan, D., Cui, G., Senpan, A., Yang, X., Lu, L., Weilbaecher, K. N., Prochownik, E. V., Lanza, G. M., & Tomasson, M. H. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0774-t · Cited by 59 · see citing works
Sauvé, S., Tremblay, L., & Lavigne, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.058 · Cited by 58 · see citing works
Direct inhibition of c-Myc-Max heterodimers by celastrol and celastrol-inspired triterpenoids
Wang, H., Teriete, P., Hu, A., Raveendra-Panickar, D., Pendelton, K., Lazo, J. S., Eiseman, J., Holien, T., Misund, K., Oliynyk, G., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6116 · Cited by 53 · see citing works
Brautigam, C. A. (2010) · Methods · doi:10.1016/j.ymeth.2010.12.029 · Cited by 48 · see citing works
Calderon, M. R., Verway, M. J., An, B., DiFeo, A. V., Bismar, T. A., Ann, D. K., Martignetti, J. A., Shalom‐Barak, T., & White, J. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311605 · Cited by 42 · see citing works
Recent discoveries and applications involving small-molecule microarrays
Hong, J. A., Neel, D. V., Wassaf, D., Caballero, F., & Koehler, A. N. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2013.09.020 · Cited by 41 · see citing works
Self-citationMYC degradation: deubiquitinating enzymes enter the dance
Amati, B. B., & Lobo, V. J. S.-A. (2007) · Nature Cell Biology · doi:10.1038/ncb0707-729 · Cited by 33 · see citing works
Naud, J., Frédéric, G., Wellinger, R. J., Chabot, B., & Lavigne, P. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00029-9 · Cited by 25 · see citing works
Flagged first, then by citations
2 of the 76 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The MYC oncogene — the grand orchestrator of cancer growth and immune evasion
Dhanasekaran, R., Deutzmann, A., Mahauad‐Fernandez, W. D., Hansen, A. S., Gouw, A. M., & Felsher, D. W. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-021-00549-2 · Cited by 1,010 · see citing works
Self-citationTargeting transcription factors in cancer — from undruggable to reality
Bushweller, J. H. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0196-7 · Cited by 919 · see citing works
MYC as a target for cancer treatment
Duffy, M. J., O’Grady, S., Tang, M., & Crown, J. P. (2021) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2021.102154 · Cited by 524 · see citing works
Therapeutic targeting of “undruggable” MYC
Llombart, V., & Mansour, M. R. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103756 · Cited by 483 · see citing works
Advances in Targeting ‘Undruggable’ transcription Factors With Small Molecules
Henley, M. J., & Koehler, A. N. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00199-0 · Cited by 409 · see citing works
Self-citationTaking the Myc out of cancer: toward therapeutic strategies to directly inhibit c-Myc
Madden, S. K., de Araujo, A. D., Gerhardt, M., Fairlie, D. P., & Mason, J. M. (2021) · Molecular Cancer · doi:10.1186/s12943-020-01291-6 · Cited by 404 · 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
Alternative approaches to target Myc for cancer treatment
Wang, C., Zhang, J., Yin, J., Gan, Y., Xu, S., Gu, Y., & Huang, W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00500-y · Cited by 243 · see citing works
New insights into protein–protein interaction modulators in drug discovery and therapeutic advance
Nada, H., Choi, Y., Kim, S.-D., Jeong, K. S., Meanwell, N. A., & Lee, K. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02036-3 · Cited by 233 · see citing works
MYC: a multipurpose oncogene with prognostic and therapeutic implications in blood malignancies
Ahmadi, S. E., Rahimi, S., Zarandi, B., Chegeni, R., & Safa, M. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01111-4 · Cited by 211 · see citing works
Unifying principles of bifunctional, proximity-inducing small molecules
Gerry, C. J., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0469-1 · Cited by 199 · see citing works
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
Inhibition of YTHDF2 triggers proteotoxic cell death in MYC-driven breast cancer
Einstein, J. M., Perelis, M., Chaim, I. A., Meena, J. K., Nussbacher, J. K., Tankka, A. T., Yee, B. A., Li, H., Madrigal, A. A., Neill, N. J., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.06.014 · Cited by 186 · see citing works
Targeted degradation of transcription factors by TRAFTACs: TRAnscription Factor TArgeting Chimeras
Samarasinghe, K. T. G., Jaime-Figueroa, S., Burgess, M., Nalawansha, D. A., Dai, K., Hu, Z., Bebenek, A., Holley, S. A., & Crews, C. M. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.03.011 · Cited by 182 · see citing works
c-MYC mediates the crosstalk between breast cancer cells and tumor microenvironment
Gao, F., Li, X.-T., Xu, K., Wang, R., & Guan, X. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01043-1 · Cited by 175 · see citing works
Discovery of a Functional Covalent Ligand Targeting an Intrinsically Disordered Cysteine within MYC
Boike, L., Cioffi, A. G., Majewski, F. C., Co, J., Henning, N. J., Jones, M. D., Liu, G., McKenna, J. M., Tallarico, J. A., Schirle, M., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.09.001 · Cited by 154 · see citing works
Mission Possible: Advances in MYC Therapeutic Targeting in Cancer
Allen-Petersen, B. L., & Sears, R. C. (2019) · BioDrugs · doi:10.1007/s40259-019-00370-5 · Cited by 143 · see citing works
Inhibition of RNA-binding proteins with small molecules
Wu, P. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0201-4 · Cited by 129 · see citing works
Transcription Factor Inhibition: Lessons Learned and Emerging Targets
Chen, A. W., & Koehler, A. N. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.01.004 · Cited by 118 · see citing works
Self-citationTarget c-Myc to treat pancreatic cancer
Ala, M. (2022) · Cancer Biology & Therapy · doi:10.1080/15384047.2021.2017223 · Cited by 119 · see citing works
MYC, MYCL, and MYCN as therapeutic targets in lung cancer
Massó-Vallés, D., Beaulieu, M.-È., & Soucek, L. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1723548 · Cited by 116 · see citing works
Molecular glues and bifunctional compounds: Therapeutic modalities based on induced proximity
Schreiber, S. L. (2024) · Cell Chemical Biology · doi:10.1016/j.chembiol.2024.05.004 · Cited by 112 · see citing works
Recent achievements and current trajectories of diversity-oriented synthesis
Gerry, C. J., & Schreiber, S. L. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.08.008 · Cited by 106 · see citing works
MYC in cancer: from undruggable target to clinical trials
Whitfield, J. R., & Soucek, L. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01143-2 · Cited by 106 · see citing works
MYC function and regulation in physiological perspective
Jha, R., Kouzine, F., & Levens, D. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1268275 · Cited by 106 · see citing works
The long journey to bring a Myc inhibitor to the clinic
Whitfield, J. R., & Soucek, L. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202103090 · Cited by 97 · see citing works
Targeting MYCN in Pediatric and Adult Cancers
Liu, Z., Chen, S. S., Clarke, S., Veschi, V., & Thiele, C. J. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.623679 · Cited by 94 · see citing works
Omomyc Reveals New Mechanisms To Inhibit the MYC Oncogene
Demma, M. J., Mapelli, C., Sun, A., Bodea, S., Ruprecht, B., Javaid, S., Wiswell, D., Muise, E., Chen, S., Zelina, J., et al. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00248-19 · Cited by 92 · see citing works
Genomic Analysis of Vascular Invasion in HCC Reveals Molecular Drivers and Predictive Biomarkers
Krishnan, M. S., Rajan, A., Park, J., Arjunan, V., Garcia-Marques, F. J., Bermudez, A., Girvan, O., Hoang, N. S., Yin, J., Nguyen, M. H., et al. (2020) · Hepatology · doi:10.1002/hep.31614 · Cited by 90 · see citing works
Self-citationModulating Androgen Receptor-Driven Transcription in Prostate Cancer with Selective CDK9 Inhibitors
Richters, A., Doyle, S. K., Freeman, D. B., Lee, C., Leifer, B. S., Jagannathan, S., Kabinger, F., Koren, J. V., Struntz, N. B., Urgiles, J., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.10.001 · Cited by 86 · see citing works
Self-citationMAX functions as a tumor suppressor and rewires metabolism in small cell lung cancer
Augert, A., Mathsyaraja, H., Ibrahim, A., Freie, B., Geuenich, M., Cheng, P.-F., Alibeckoff, S. P., Wu, N., Hiatt, J., Basom, R. S., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.04.016 · Cited by 68 · see citing works
MYC Dysregulates Mitosis, Revealing Cancer Vulnerabilities
Rohrberg, J., de Mark, D. V., Amouzgar, M., Lee, J. V., Taileb, M., Corella, A. N., Kilinc, S., Williams, J. R., Jokisch, M., Camarda, R., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.041 · Cited by 76 · see citing works
Targeting MYC Proteins for Tumor Therapy
Wolf, E., & Eilers, M. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055826 · Cited by 63 · see citing works
Holmes, A. G., Parker, J. B., Sagar, V., Truica, M. I., Soni, P. N., Han, H., Schiltz, G. E., Abdulkadir, S. A., & Chakravarti, D. (2022) · Science Advances · doi:10.1126/sciadv.abh3635 · Cited by 61 · see citing works
Geiger, T. M., Schäfer, S. C., Dreizler, J. K., Walz, M., & Hausch, F. (2021) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2021.100018 · Cited by 55 · see citing works
Capitalizing on Synthetic Lethality of MYC to Treat Cancer in the Digital Age
Thng, D. K. H., Toh, T. B., & Chow, E. K. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.11.014 · Cited by 52 · see citing works
<i>Max</i> deletion destabilizes MYC protein and abrogates Eµ- <i>Myc</i> lymphomagenesis
Mathsyaraja, H., Freie, B., Cheng, P.-F., Babaeva, E., Catchpole, J. T., Janssens, D., Henikoff, S., & Eisenman, R. N. (2019) · Genes & Development · doi:10.1101/gad.325878.119 · Cited by 54 · see citing works
Engineering Bioactive Dimeric Transcription Factor Analogs via Palladium Rebound Reagents
Jbara, M., Pomplun, S. J., Schissel, C. K., Hawken, S. W., Boija, A., Klein, I. A., Rodriguez, J., Buchwald, S. L., & Pentelute, B. L. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05666 · Cited by 53 · see citing works
Antitumor Effect of Anti‐c‐Myc Aptamer‐Based PROTAC for Degradation of the c‐Myc Protein
Wang, Y., Yang, G., Zhang, X., Bai, R., Yuan, D., Gao, D., He, Q., Yuan, Y., Zhang, X., Kou, J., et al. (2024) · Advanced Science · doi:10.1002/advs.202309639 · Cited by 51 · see citing works
Demystifying the Druggability of the MYC Family of Oncogenes
Karadkhelkar, N. M., Lin, M., Eubanks, L. M., & Janda, K. D. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12732 · Cited by 50 · see citing works
Aditham, A. K., Markin, C. J., Mokhtari, D. A., DelRosso, N. V., & Fordyce, P. M. (2020) · Cell Systems · doi:10.1016/j.cels.2020.11.012 · Cited by 45 · see citing works
Emergent mechanical control of vascular morphogenesis
Whisler, J. A., Shahreza, S., Schlegelmilch, K., Ege, N., Javanmardi, Y., Malandrino, A., Agrawal, A., Fantin, A., Serwinski, B., Azizgolshani, H., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg9781 · Cited by 45 · see citing works
Self-citationMYC Oncogene: A Druggable Target for Treating Cancers with Natural Products
Chan, K. I., Zhang, S., Li, G., Xu, Y., Cui, L., Wang, Y., Su, H., Tan, W., & Zhong, Z. (2024) · Aging and Disease · doi:10.14336/ad.2023.0520 · Cited by 45 · see citing works
Mathsyaraja, H., Catchpole, J., Freie, B. W., Eastwood, E., Babaeva, E., Geuenich, M., Cheng, P. F., Ayers, J., Yu, M., Wu, N., et al. (2021) · eLife · doi:10.7554/elife.64212 · Cited by 39 · see citing works
Emerging Pharmacotherapeutic Strategies to Overcome Undruggable Proteins in Cancer
Lu, Y., Yang, Y., Zhu, G., Zeng, H., Fan, Y., Guo, F., Xu, D., Wang, B., Chen, D., & Ge, G. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83026 · Cited by 41 · see citing works
Strategies to target the cancer driver MYC in tumor cells
Weber, L. I., & Hartl, M. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1142111 · Cited by 40 · see citing works
Protein homodimer sequestration with small molecules: Focus on PD-L1
Bailly, C., & Vergoten, G. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113821 · Cited by 38 · see citing works
Hu, X., Zhou, Z., Li, F., Xiao, Y., Wang, Z., Xu, J., Dong, F., Zheng, H., & Yu, R. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e06387 · Cited by 38 · see citing works
MYC the oncogene from hell: Novel opportunities for cancer therapy
Papadimitropoulou, A., Makri, M., & Zoidis, G. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116194 · Cited by 38 · see citing works
Pomplun, S. J., Jbara, M., Schissel, C. K., Hawken, S. W., Boija, A., Li, C. H., Klein, I. A., & Pentelute, B. L. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00663 · Cited by 37 · see citing works
Targeting MYC: From understanding its biology to drug discovery
Ross, J., Miron, C. E., Plescia, J., LaPlante, P., McBride, K. M., Moitessier, N., & Möröy, T. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113137 · Cited by 34 · see citing works
Drugging the undruggable proteins in cancer: A systems biology approach
Pathmanathan, S., Grozavu, I., Lyakisheva, A., & Štagljar, I. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.07.004 · Cited by 32 · see citing works
A novel molecular class that recruits HDAC/MECP2 complexes to PU.1 motifs reduces neuroinflammation
Ralvenius, W. T., Mungenast, A. E., Woolf, H., Huston, M. M., Gillingham, T. Z., Godin, S. K., Penney, J., Cam, H. P., Gao, F., Fernandez, C. G., et al. (2023) · Journal of Experimental Medicine · doi:10.1084/jem.20222105 · Cited by 31 · see citing works
“Small molecules that stabilize repressive transcription factor assemblies at gene promoters offer a promising avenue for drug development (Fontaine et al., 2017; Struntz et al., 2019).”
Multiple roles of HOX proteins in Metastasis: Let me count the ways
Jonkers, J., Pai, P., & Sukumar, S. V. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09908-4 · Cited by 29 · see citing works
Emerging modes-of-action in drug discovery
Valeur, E., Narjes, F., Ottmann, C., & Plowright, A. T. (2019) · MedChemComm · doi:10.1039/c9md00263d · Cited by 27 · see citing works
McAnulty, J., & DiFeo, A. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249486 · Cited by 27 · see citing works
Zhang, X., Lou, H. E., Gopalan, V., Liu, Z., Jafarah, H. M., Lei, H., Jones, P., Sayers, C. M., Yohe, M. E., Chittiboina, P., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111363 · Cited by 26 · see citing works
Zhu, C.-G., Kim, S.-J., Mooradian, A., Wang, F.-L., Li, Z.-Q., Holohan, S., Collins, P., Wang, K.-R., Guo, Z.-F., Hoog, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108749 · Cited by 29 · see citing works
Inhibition of Myc transcriptional activity by a mini‐protein based upon Mxd1
Demma, M. J., Hohn, M. J., Sun, A., Mapelli, C., Hall, B. E., Walji, A. M., & O’Neil, J. (2020) · FEBS Letters · doi:10.1002/1873-3468.13759 · Cited by 25 · see citing works
Biological Role of MYCN in Medulloblastoma: Novel Therapeutic Opportunities and Challenges Ahead
Shrestha, S., Morcavallo, A., Gorrini, C., & Chesler, L. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.694320 · Cited by 24 · see citing works
A Review of the Regulatory Mechanisms of N-Myc on Cell Cycle
Li, H., Dong, L., Jin, M.-J., Li, Q.-Y., Wang, X. Q., Jia, M., Song, J., Zhang, S., & Yuan, S. (2023) · Molecules · doi:10.3390/molecules28031141 · Cited by 25 · see citing works
MYC modulators in cancer: a patent review
Wang, X., Su, X., Cheng, S.-Q., Zhi-yin, S., Huang, Z., & Ou, T. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1612878 · Cited by 25 · see citing works
Du, J., Wang, S., Wang, R., Wang, S., Han, Q., Xu, H., Yang, P., & Liu, Y. (2019) · Pathology & Oncology Research · doi:10.1007/s12253-019-00770-6 · Cited by 23 · see citing works
Antitumor efficacy of a sequence-specific DNA-targeted γPNA-based c-Myc inhibitor
Malik, S., Pradeep, S. P., Kumar, V., Xiao, Y., Deng, Y., Fan, R., Vasquez, J. C., Singh, V., & Bahal, R. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101354 · Cited by 22 · see citing works
de Jonge, A. V., Mutis, T., Roemer, M. G. M., Scheijen, B., & Chamuleau, M. E. D. (2020) · Cancers · doi:10.3390/cancers12103052 · Cited by 23 · see citing works
MYC-Targeting PROTACs Lead to Bimodal Degradation and N-Terminal Truncation
Boyd, S. R., Chamakuri, S., Trostle, A. J., Chen, H., Liu, Z., Jain, A., Wang, J., Malovannaya, A., & Young, D. W. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.4c00864 · Cited by 21 · see citing works
Castell, A., Yan, Q., Fawkner, K., Bazzar, W., Zhang, F., Wickström, M., Alzrigat, M., Franco, M., Krona, C. C., Cameron, D. P., et al. (2022) · Cancer Research Communications · doi:10.1158/2767-9764.crc-21-0019 · Cited by 21 · see citing works
Targeting MYC: Multidimensional regulation and therapeutic strategies in oncology
Duan, Y., Liu, Z., Wang, Q., Zhang, J., Liu, J., Zhang, Z., & Li, C. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101435 · Cited by 21 · see citing works
Inamoto, I., Sheoran, I. S., Popa, S. C., Hussain, M., & Shin, J. A. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00684 · Cited by 20 · see citing works
A Small-Molecule Inhibitor to the Cytokine Interleukin-4
Quinnell, S. P., Leifer, B. S., Nestor, S. T., Tan, K., Sheehy, D. F., Ceo, L. M., Doyle, S. K., Koehler, A. N., & Vegas, A. J. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00615 · Cited by 19 · see citing works
Self-citationNuclear to cytoplasmic transport is a druggable dependency in MYC-driven hepatocellular carcinoma
Deutzmann, A., Sullivan, D. K., Dhanasekaran, R., Li, W., Chen, X., Tong, L., Mahauad‐Fernandez, W. D., Bell, J., Mosley, A. R., Koehler, A. N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45128-y · Cited by 20 · see citing works
Self-citationSelective targeting of MYC mRNA by stabilized antisense oligonucleotides
Gill, T., Wang, H., Bandaru, R., Lawlor, M. A., Lu, C., Nieman, L. T., Tao, J., Zhang, Y., Anderson, D. G., Ting, D. T., et al. (2021) · Oncogene · doi:10.1038/s41388-021-02053-4 · Cited by 18 · see citing works
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 · see citing works
Freie, B. W., Ibrahim, A. H., Carroll, P. A., Bronson, R. T., Augert, A., MacPherson, D. P., & Eisenman, R. N. (2025) · Science Advances · doi:10.1126/sciadv.adt3177 · Cited by 18 · see citing works
Tan, Z. Y., Adade, J. K. A., Gu, X., Hecht, C. J. S., Salcius, M., Tong, B., Liu, S., Hwang, S., Zécri, F. J., Graham, D. B., et al. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2024.12.002 · Cited by 17 · see citing works
Hypoxic, glycolytic metabolism is a vulnerability of B-acute lymphoblastic leukemia-initiating cells
Morris, V., Wang, D., Li, Z., Marion, W., Hughes, T. K., Sousa, P., Harada, T., Sui, S. H., Naumenko, S., Kalfon, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110752 · Cited by 16 · see citing works
Self-citationRuprecht, B., Wei, L., Zheng, L., Bodea, S., Mo, X., Maschberger, M., Stoehr, G., Hahne, H., Cornella‐Taracido, I., & Chi, A. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.10.008 · Cited by 15 · see citing works
Functional implications and therapeutic targeting of androgen response elements in prostate cancer
Senapati, D., Sharma, V., Rath, S. K., Rai, U., & Panigrahi, N. (2023) · Biochimie · doi:10.1016/j.biochi.2023.07.012 · Cited by 14 · see citing works
Small-Molecule Approaches to Target Transcription Factors
Cui, H., Stilgenbauer, M., & Koehler, A. N. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062722-012209 · Cited by 16 · see citing works
Self-citationEllenbroek, B. D., Kahler, J. P., Arella, D., Lin, C., Jespers, W., Züger, E. A.-K., Drukker, M., & Pomplun, S. J. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202416082 · Cited by 14 · see citing works
Self-citationYang, 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 · see citing works
Chen, L., Cheng, B., Sun, Q., & Lai, L. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127711 · Cited by 13 · see citing works
Proteomimetic Strategy for the Modulation of Intrinsically Disordered Protein MYC
Nguyễn, T. T., Hong, S. H., & Arora, P. S. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c18144 · Cited by 12 · see citing works
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 · see citing works
Henley, M. J., Doyle, S. K., & Koehler, A. N. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.014 · Cited by 11 · see citing works
Self-citationSynthetic peptides: promising modalities for the targeting of disease related nucleic acids.
Ellenbroek, B., Kahler, J. P., Evers, S. R., & Pomplun, S. (2024) · Angewandte Chemie · doi:10.1002/anie.202401704 · Cited by 10 · see citing works
Transcriptional regulation of MYC through G-quadruplex structures
Balaratnam, S., & Schneekloth, J. S. (2020) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2020.05.002 · Cited by 12 · see citing works
Bordone, R., Ivy, D. M., D'Amico, R., Barba, M. C., Gaggianesi, M., Pastena, F. D., Cesaro, B., Bufalieri, F., Balzerano, A., Smaele, E. D., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03170-6 · Cited by 10 · see citing works
Dalin, S., Grauman-Boss, B., Lauffenburger, D. A., & Hemann, M. T. (2022) · Scientific Reports · doi:10.1038/s41598-022-09319-1 · Cited by 9 · see citing works
Exploring Myc puzzle: Insights into cancer, stem cell biology, and PPI networks
Ghasemi, N., & Azizi, H. (2024) · Gene · doi:10.1016/j.gene.2024.148447 · Cited by 9 · see citing works
Targeting protein synthesis pathways in MYC-amplified medulloblastoma
Kumar, D., Kanchan, R. K., & Chaturvedi, N. K. (2025) · Discover Oncology · doi:10.1007/s12672-025-01761-7 · Cited by 9 · see citing works
Neuroendocrine Tumors: Germline Genetics and Hereditary Syndromes
Lauricella, E., Chaoul, N., D’Angelo, G., Giglio, A., Cafiero, C., Porta, C., & Palmirotta, R. (2025) · Current Treatment Options in Oncology · doi:10.1007/s11864-024-01288-z · Cited by 8 · see citing works
Bromodomain Protein-directed Agents and MYC in Small Cell Lung Cancer
Hamilton, G., Stickler, S., & Rath, B. (2024) · Current Cancer Drug Targets · doi:10.2174/0115680096272757231211113206 · Cited by 7 · see citing works
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 · see citing works
Harada, T., Perez, M. W., Kalfon, J., Braes, F. D., Batley, R., Eagle, K., Nabet, B., Leifer, B. S., Kruell, J. A., Paralkar, V. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.07.536032 · Cited by 6 · see citing works
Self-citationUnlocking the Radiosensitizing Potential of MYC Inhibition in Neuroendocrine Malignancies
Guo, Q., Yang, W., Robinson, G., Chaludiya, K., Abdulkadir, A. N., Roy, F. G., Shivakumar, D., Ahmad, A. N., Abdulkadir, S. A., & Kirschner, A. N. (2025) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2025.04.034 · Cited by 5 · see citing works
Max-imizing the Attenuation of Myc Using Small Molecules
Boyd, S. R., & Young, D. W. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.06.002 · Cited by 5 · see citing works
Chemical Probe Discovery for DEAD-Box RNA-Binding Protein DDX21 Using Small-Molecule Microarrays
Aiba, T., Calo, E., & Koehler, A. N. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00302 · Cited by 3 · see citing works
Self-citationBeyond small molecules: advancing MYC-targeted cancer therapies through protein engineering
Edaibis, R., Akel, R., & Shin, J. A. (2025) · Transcription · doi:10.1080/21541264.2025.2453315 · Cited by 4 · see citing works
Conformational modulation of intrinsically disordered transactivation domains for cancer therapy
Vosselman, T., Sahin, C., Lane, D. P., Arsenian‐Henriksson, M., Landreh, M., & Lama, D. (2025) · PNAS Nexus · doi:10.1093/pnasnexus/pgaf152 · Cited by 4 · see citing works
- Authors
- Struntz, N. B., Chen, A., Deutzmann, A., Wilson, R. M., Stefan, E., Evans, H. L., Ramirez, M. A., Liang, T., Caballero, F., Wildschut, M. H. E., Neel, D. V., Freeman, D. B., Pop, M. S., McConkey, M., Muller, S., Curtin, B. H., Tseng, H., Frombach, K. R., Butty, V. L., Levine, S. S., Feau, C., Elmiligy, S., Hong, J. A., Lewis, T. A., Vetere, A., Clemons, P. A., Malstrom, S. E., Ebert, B. L., Lin, C. Y., Felsher, D. W., & Koehler, A. N.
- Affiliations
- Koch Institute for Integrative Cancer Research At MIT (US)
- Stanford Medicine (US)
- Baylor College of Medicine (US)
- Cambridge Intellectual Property (United Kingdom) (GB)
- Broad Institute (US)
- Boston Children's Hospital (US)
- Corresponding author
- Koehler, Angela N.
- ORCID
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 26
- Issue
- 5
- Pages
- 711-723.e14
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W2921930449
- Cited by
- 130
- References
- 76
- Citations by year
- 2026: 9 · 2025: 24 · 2024: 22 · 2023: 11 · 2022: 8 · 2021: 25 · 2020: 20 · 2019: 11
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-nd)
- Funders
- National Cancer Institute (R01-CA160860, P30-CA14051)
- Koch Institute Cancer Center (U01-CA176152)
- NIH (CA170378PQ2, 1U01CA188383-01/S1, 1R01CA215452-01)
- Leukemia & Lymphoma Society
- Ono Pharma Foundation
- MIT Deshpande Center
- MIT Center for Precision Cancer Medicine
- AACR
- Merkin Institute
- Cancer Prevention Research Institute of Texas (RR150093)
- MIT
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- Max protein, Myc-Max heterodimer, bHLH transcription factors, small molecule inhibitors, tumor cell growth inhibition, tumor growth inhibition, chemical probes
- MeSH terms
- Animals, Cell Line, Disease Models, Animal, Humans, Lactams, Male, Neoplasms, Polycyclic Compounds, Promoter Regions, Genetic, Protein Binding, Repressor Proteins, Transcription, Genetic, Ultraviolet Rays, Proto-Oncogene Proteins c-myc, Mice, SCID, Mice, Inbred NOD, Dimerization, Mice, Rats, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Small Molecule Libraries
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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.
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