The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Pharmacological targeting of the Wdr5-MLL interaction in C/EBPα N-terminal leukemia
Open accessAbstract
The CEBPA gene is mutated in 9% of patients with acute myeloid leukemia (AML). Selective expression of a short (30-kDa) CCAAT-enhancer binding protein-α (C/EBPα) translational isoform, termed p30, represents the most common type of CEBPA mutation in AML. The molecular mechanisms underlying p30-mediated transformation remain incompletely understood. We show that C/EBPα p30, but not the normal p42 isoform, preferentially interacts with Wdr5, a key component of SET/MLL (SET-domain/mixed-lineage leukemia) histone-methyltransferase complexes. Accordingly, p30-bound genomic regions were enriched for MLL-dependent H3K4me3 marks. The p30-dependent increase in self-renewal and inhibition of myeloid differentiation required Wdr5, as downregulation of the latter inhibited proliferation and restored differentiation in p30-dependent AML models. OICR-9429 is a new small-molecule antagonist of the Wdr5-MLL interaction. This compound selectively inhibited proliferation and induced differentiation in p30-expressing human AML cells. Our data reveal the mechanism of p30-dependent transformation and establish the essential p30 cofactor Wdr5 as a therapeutic target in CEBPA-mutant AML.
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?
In the citing paper
“Potent and selective compounds are also targeting the central cavity of WDR5, another WDR DCAF E3 ligase 71 .”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [71]
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
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
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
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Analyzing real-time PCR data by the comparative CT method
Schmittgen, T. D., & Livak, K. J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.73 · Cited by 26,190
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Model-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
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
Exploration, normalization, and summaries of high density oligonucleotide array probe level data
Irizarry, R. A. (2003) · Biostatistics · doi:10.1093/biostatistics/4.2.249 · Cited by 10,603
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
Flagged first, then by citations
Cited by
Sorted by citations
Targeted protein degradation: expanding the toolbox
Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960
Self-citationEpigenetic modifications of histones in cancer
Zhao, Z., & Shilatifard, A. (2019) · Genome biology · doi:10.1186/s13059-019-1870-5 · Cited by 591
Epigenetic balance of gene expression by Polycomb and COMPASS families
Piunti, A., & Shilatifard, A. (2016) · Science · doi:10.1126/science.aad9780 · Cited by 524
Gain-of-function p53 mutants co-opt chromatin pathways to drive cancer growth
Zhu, J., Sammons, M. A., Donahue, G., Dou, Z., Vedadi, M., Getlik, M., Barsyte-Lovejoy, D., Al-awar, R., Katona, B. W., Shilatifard, A., et al. (2015) · Nature · doi:10.1038/nature15251 · Cited by 493
Self-citationWD40 repeat domain proteins: a novel target class?
Schapira, M., Tyers, M., Torrent, M., & Arrowsmith, C. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.179 · Cited by 335
Self-citationChemical and Biochemical Perspectives of Protein Lysine Methylation
Luo, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00008 · Cited by 295
Diehl, C. J., & Ciulli, A. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00387b · Cited by 269
He, W., Zhong, G., Jiang, N., Wang, B., Fan, X., Chen, C., Chen, X., Huang, J., & Lin, T. (2018) · Journal of Clinical Investigation · doi:10.1172/jci96218 · Cited by 209
Chiang, K., Zielinska, A. E., Shaaban, A. M., Sánchez-Bailón, M. P., Jarrold, J., Clarke, T. L., Zhang, J., Francis, A., Jones, J. L., Smith, S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.096 · Cited by 208
Erratum: Pharmacological targeting of the Wdr5-MLL interaction in C/EBPα N-terminal leukemia
Grebien, F., Vedadi, M., Getlik, M., Giambruno, R., Grover, A., Avellino, R., Skucha, A., Vittori, S., Kuznetsova, E., Smil, D. V., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio1015-815b · Cited by 206
Self-citationTargeting G protein-coupled receptor signalling by blocking G proteins
Campbell, A. P., & Smrcka, A. V. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.135 · Cited by 201
Chen, H., Lorton, B. M., Gupta, V., & Shechter, D. (2016) · Oncogene · doi:10.1038/onc.2016.205 · Cited by 188
MYC—Master Regulator of the Cancer Epigenome and Transcriptome
Poole, C. J., & van Riggelen, J. (2017) · Genes · doi:10.3390/genes8050142 · Cited by 180
KDM5 histone demethylases repress immune response via suppression of STING
Wu, L., Cao, J. P., Cai, W. L., Lang, S. M., Horton, J. R., Jansen, D. J., Liu, Z. Z., Chen, J. F.-Y., Zhang, M., Mott, B. T., et al. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2006134 · Cited by 182
Moonlighting with WDR5: A Cellular Multitasker
Guarnaccia, A. D., & Tansey, W. P. (2018) · Journal of Clinical Medicine · doi:10.3390/jcm7020021 · Cited by 151
A selective WDR5 degrader inhibits acute myeloid leukemia in patient-derived mouse models
Yu, X., Li, D., Kottur, J., Shen, Y., Kim, H. S., Park, K., Tsai, Y., Gong, W., Wang, J., Suzuki, K., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj1578 · Cited by 149
Nudt21 Controls Cell Fate by Connecting Alternative Polyadenylation to Chromatin Signaling
Brumbaugh, J., Stefano, B. D., Wang, X., Borkent, M., Forouzmand, E., Clowers, K. J., Ji, F., Schwarz, B. A., Kalocsay, M., Elledge, S. J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.11.023 · Cited by 148
Benítez, J. A., Ma, J., D’Antonio, M., Boyer, A. D., Camargo, M. F., Zanca, C., Kelly, S., Khodadadi‐Jamayran, A., Jameson, N. M., Andersen, M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15223 · Cited by 147
Carugo, A., Genovese, G., Seth, S., Nezi, L., Rose, J. L., Bossi, D., Cicalese, A., Shah, P. K., Viale, A., Pettazzoni, P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.063 · Cited by 140
Epigenetic stress responses induce muscle stem-cell ageing by Hoxa9 developmental signals
Schwörer, S., Becker, F., Feller, C., Baig, A. H., Köber, U., Henze, H., Kraus, J. M., Xin, B., Lechel, A., Lipka, D. B., et al. (2016) · Nature · doi:10.1038/nature20603 · Cited by 132
A chemical biology toolbox to study protein methyltransferases and epigenetic signaling
Scheer, S., Ackloo, S. Z., Medina, T. D. S., Schapira, M., Li, F., Ward, J. A., Lewis, A. M., Northrop, J. P., Richardson, P. L., Kanıskan, H. Ü., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07905-4 · Cited by 131
Self-citationDisplacement of WDR5 from Chromatin by a WIN Site Inhibitor with Picomolar Affinity
Aho, E. R., Wang, J., Gogliotti, R. D., Howard, G. C., Phan, J., Acharya, P., Macdonald, J. D., Cheng, K. C.-C., Lorey, S. L., Lu, B., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.047 · Cited by 120
Thomas, L. R., Adams, C. M., Wang, J., Weissmiller, A. M., Creighton, J. H., Lorey, S. L., Liu, Q., Fesik, S. W., Eischen, C. M., & Tansey, W. P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910391116 · Cited by 122
Epigenomic regulation of oncogenesis by chromatin remodeling
Kumar, R., Li, D.-Q., Müller, S., & Knapp, S. (2016) · Oncogene · doi:10.1038/onc.2015.513 · Cited by 117
Sun, Y., Bell, J. L., Carter, D. R., Gherardi, S., Poulos, R. C., Milazzo, G., Wong, J. W. H., Al‐awar, R., Tee, A. E., Liu, P. Y., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-0423 · Cited by 115
Self-citationPROTAC’ing oncoproteins: targeted protein degradation for cancer therapy
Kelm, J. M., Pandey, D. S., Malin, E., Kansou, H. W., Arora, S., Kumar, R., & Gavande, N. S. (2023) · Molecular Cancer · doi:10.1186/s12943-022-01707-5 · Cited by 122
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Bochyńska, A., Lüscher‐Firzlaff, J., & Lüscher, B. (2018) · Cells · doi:10.3390/cells7030017 · Cited by 105
Bayo, J., Fiore, E. J., Domínguez, L. M., Real, A., Malvicini, M., Rizzo, M., Atorrasagasti, C., García, M. G., Argemí, J., Martínez, E. D., et al. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.03.007 · Cited by 111
Stefano, B. D., Collombet, S., Jakobsen, J. S., Wierer, M., Sardina, J. L., Lackner, A., Stadhouders, R., Segura-Morales, C., Francesconi, M., Limone, F., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3326 · Cited by 106
WDR5 modulates cell motility and morphology and controls nuclear changes induced by a 3D environment
Wang, P., Dreger, M., Madrazo, E., Williams, C. J., Samaniego, R., Hodson, N. W., Monroy, F., Baena, E., Sánchez‐Mateos, P., Hurlstone, A. F. L., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1719405115 · Cited by 101
Karataş, H., Li, Y., Liu, L., Ji, J., Lee, S. H. F., Chen, Y., Yang, J., Huang, L., Bernard, D., Xu, J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01796 · Cited by 103
Shen, Y., Szewczyk, M. M., Eram, M. S., Smil, D. V., Kanıskan, H. Ü., de Freitas, R. F., Senisterra, G. A., Li, F., Schapira, M., Brown, P. J., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01033 · Cited by 97
Self-citationGetlik, M., Smil, D. V., Zepeda‐Velázquez, C., Bolshan, Y., Poda, G. I., Wu, H. Y., Dong, A., Kuznetsova, E., Marcellus, R. C., Senisterra, G. A., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01630 · Cited by 94
Self-citationThe Histone H3 Lysine 4 Presenter WDR5 as an Oncogenic Protein and Novel Epigenetic Target in Cancer
Lu, K., Tao, H., Si, X., & Chen, Q. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00502 · Cited by 89
Quevedo, M., Meert, L., Dekker, M. R., Dekkers, D. H. W., Brandsma, J. H., van den Berg, D. L. C., Özgür, Z., van IJcken, W. F. J., Demmers, J., Fornerod, M. W. J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10502-8 · Cited by 95
Zhang, J., Zhou, Q., Xie, K., Liang Cheng, C., Peng, S., Xie, R., Liu, L., Zhang, Y., Dong, W., Han, J., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01989-5 · Cited by 87
Design, Synthesis, and Evaluation of WD-Repeat-Containing Protein 5 (WDR5) Degraders
Dölle, A., Adhikari, B., Krämer, A., Weckesser, J., Berner, N., Berger, L. M., Diebold, M., Szewczyk, M. M., Baršytė-Lovejoy, D., Arrowsmith, C. H., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00146 · Cited by 86
Self-citationWDR5 is a conserved regulator of protein synthesis gene expression
Bryan, A. F., Wang, J., Howard, G. C., Guarnaccia, A. D., Woodley, C. M., Aho, E. R., Rellinger, E. J., Matlock, B. K., Flaherty, D. K., Lorey, S. L., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa051 · Cited by 80
Li, X., & Song, Y. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01057-7 · Cited by 79
Alicea‐Velázquez, N. L., Shinsky, S. A., Loh, D. M., Lee, J., Skalnik, D. G., & Cosgrove, M. S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.752626 · Cited by 71
Zhou, Q., Chen, X., He, H., Peng, S., Zhang, Y., Zhang, J., Liang Cheng, C., Liu, S., Huang, M. X., Xie, R., et al. (2021) · Theranostics · doi:10.7150/thno.55814 · Cited by 75
WDR5 high expression and its effect on tumorigenesis in leukemia
Ge, Z., Song, E. J., Kawasawa, Y. I., Li, J., Dovat, S., & Song, C. (2016) · Oncotarget · doi:10.18632/oncotarget.9312 · Cited by 75
Wang, F., Jeon, K. O., Salovich, J. M., Macdonald, J. D., Alvarado, J., Gogliotti, R. D., Phan, J., Olejniczak, E. T., Sun, Q., Wang, S., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00375 · Cited by 75
The molecular mechanics of mixed lineage leukemia
Slany, R. K. (2016) · Oncogene · doi:10.1038/onc.2016.30 · Cited by 72
C/EBPα deregulation as a paradigm for leukemogenesis
Pulikkan, J. A., Tenen, D. G., & Behre, G. (2017) · Leukemia · doi:10.1038/leu.2017.229 · Cited by 76
Wang, Z., Wang, P., Li, Y., Peng, H., Zhu, Y., Mohandas, N., & Liu, J. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00422-1 · Cited by 68
The multifaceted functions of C/EBPα in normal and malignant haematopoiesis
Ohlsson, E., Schuster, M. B., Hasemann, M. S., & Porse, B. T. (2015) · Leukemia · doi:10.1038/leu.2015.324 · Cited by 84
Direct and Indirect Targeting of HOXA9 Transcription Factor in Acute Myeloid Leukemia
Lambert, M., Alioui, M., Jambon, S., Depauw, S., SEUNINGEN, I. V., & David‐Cordonnier, M. (2019) · Cancers · doi:10.3390/cancers11060837 · Cited by 73
Impact of WIN site inhibitor on the WDR5 interactome
Guarnaccia, A. D., Rose, K. L., Wang, J., Zhao, B., Popay, T. M., Wang, C. E., Guerrazzi, K., Hill, S., Woodley, C. M., Hansen, T. J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108636 · Cited by 62
Kirtonia, A., Pandya, G., Sethi, G., Pandey, A. K., Das, B. C., & Garg, M. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01944-5 · Cited by 68
Targeting human SET1/MLL family of proteins
Vedadi, M., Blazer, L. L., Eram, M. S., Baršytė-Lovejoy, D., Arrowsmith, C. H., & Hajian, T. (2017) · Protein Science · doi:10.1002/pro.3129 · Cited by 68
Self-citationMacdonald, J. D., Chacón Simon, S., Han, C., Wang, F., Shaw, J. G., Howes, J. E., Sai, J., Yuh, J. P., Camper, D., Alicie, B. M., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01411 · Cited by 66
Tian, J., Teuscher, K. B., Aho, E. R., Alvarado, J., Mills, J. J., Meyers, K. M., Gogliotti, R. D., Han, C., Macdonald, J. D., Sai, J., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01608 · Cited by 65
Targeting WD Repeat-Containing Protein 5 (WDR5): A Medicinal Chemistry Perspective
Chen, X., Xu, J., Wang, X., Long, G., You, Q., & Guo, X. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00037 · Cited by 63
MLL-fusion-driven leukemia requires SETD2 to safeguard genomic integrity
Skucha, A., Ebner, J., Schmoellerl, J., Roth, M., Eder, T., César‐Razquin, A., Stukalov, A., Vittori, S., Muhar, M., Lu, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04329-y · Cited by 66
Self-citationLSD1 inhibition induces differentiation and cell death in Merkel cell carcinoma
Leiendecker, L., Jung, P. S., Kręcioch, I., Neumann, T., Schleiffer, A., Mechtler, K., Wiesner, T., & Obenauf, A. C. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012525 · Cited by 65
Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing SWI/SNF
Radko-Juettner, S., Yue, H., Myers, J., Carter, R. D., Robertson, A. N., Mittal, P., Zhu, Z., Hansen, B. S., Donovan, K. A., Hunkeler, M., et al. (2024) · Nature · doi:10.1038/s41586-024-07250-1 · Cited by 68
Discovery of a dual WDR5 and Ikaros PROTAC degrader as an anti-cancer therapeutic
Li, D., Yu, X., Kottur, J., Gong, W., Zhang, Z., Storey, A. J., Tsai, Y., Uryu, H., Shen, Y., Byrum, S. D., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02340-8 · Cited by 61
WDR5 represents a therapeutically exploitable target for cancer stem cells in glioblastomaPreprint
Mitchell, K., Sprowls, S. A., Arora, S., Shakya, S., Silver, D. J., Goins, C. M., Wallace, L. C., Roversi, G. A., Schafer, R., Kay, K. E., et al. (2023) · Genes & Development · doi:10.1101/gad.349803.122 · Cited by 62
The complex activities of the SET1/MLL complex core subunits in development and disease
Jiang, H. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194560 · Cited by 58
Targeting non-bromodomain chromatin readers
Arrowsmith, C. H., & Schapira, M. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0290-2 · Cited by 57
Self-citationMethyltransferase Inhibitors: Competing with, or Exploiting the Bound Cofactor
de Freitas, R. F., Ivanochko, D., & Schapira, M. (2019) · Molecules · doi:10.3390/molecules24244492 · Cited by 57
Self-citationShimoda, H., Doi, S., Nakashima, A., Sasaki, K., Doi, T., & Masaki, T. (2019) · Kidney International · doi:10.1016/j.kint.2019.06.021 · Cited by 58
Li, D., Chen, W., Xu, X., Jiang, F., Wang, L., Xie, Y.-Y., Zhang, X., Guo, X., You, Q., & Sun, H.-P. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.04.032 · Cited by 55
Di, Y., Jing, X., Hu, K., Wen, X., Ye, L., Zhang, X., Qin, J., Ye, J., Lin, R., Wang, Z., et al. (2022) · Drug Resistance Updates · doi:10.1016/j.drup.2022.100909 · Cited by 53
Li, D., Chen, W., Wang, Z., Xie, Y.-Y., Xu, X., Jiang, Z., Zhang, X., You, Q., & Guo, X. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.08.036 · Cited by 53
Ma, M., Zhang, Y., Weng, M., Hu, Y., Xuan, Y., Hu, Y., & Lv, K. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.09.002 · Cited by 52
Discovery of Small-Molecule Antagonists of the H3K9me3 Binding to UHRF1 Tandem Tudor Domain
Senisterra, G. A., Zhu, H. Y. H., Luo, X., Zhang, H., Xun, G., Lu, C., Xiao, W., Hajian, T., Loppnau, P., Chau, I., et al. (2018) · SLAS DISCOVERY · doi:10.1177/2472555218766278 · Cited by 48
Self-citationWDR5 supports colon cancer cells by promoting methylation of H3K4 and suppressing DNA damage
Neilsen, B. K., Chakraborty, B., McCall, J. L., Frodyma, D. E., Sleightholm, R. L., Fisher, K. W., & Lewis, R. E. (2018) · BMC Cancer · doi:10.1186/s12885-018-4580-6 · Cited by 51
Epigenetic small molecule modulators of histone and DNA methylation
Hauser, A., Robaa, D., & Jung, M. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.03.003 · Cited by 50
Chemical Inhibition of Protein Methyltransferases
Schapira, M. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.07.014 · Cited by 49
Self-citationDrug Discovery and Chemical Biology of Cancer Epigenetics
Ribich, S. A., Harvey, D. M., & Copeland, R. A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.020 · Cited by 50
Yoshino, S., Yokoyama, T., Sunami, Y., Takahara, T., Nakamura, A., Yamazaki, Y., Tsutsumi, S., Aburatani, H., & Nakamura, T. (2020) · Blood · doi:10.1182/blood.2019004586 · Cited by 50
Open Access Chemical Probes for Epigenetic Targets
Brown, P. J., & Müller, S. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.127 · Cited by 48
Self-citationČermáková, K., & Hodges, H. C. (2018) · Molecules · doi:10.3390/molecules23081958 · Cited by 51
Lysine methyltransferase inhibitors: where we are now
Feoli, A., Viviano, M., Cipriano, A., Milite, C., Castellano, S., & Sbardella, G. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00196e · Cited by 50
Zaware, N., & Zhou, M. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.012 · Cited by 49
Targeting transcription factors in acute myeloid leukemia
Takei, H., & Kobayashi, S. S. (2018) · International Journal of Hematology · doi:10.1007/s12185-018-2488-1 · Cited by 47
Singhal, N. K., Sternbach, S., Fleming, S. M., Alkhayer, K., Shelestak, J., Popescu, D. C., Weaver, A., Clements, R. J., Wasek, B. L., Bottiglieri, T., et al. (2020) · Epigenetics · doi:10.1080/15592294.2020.1735075 · Cited by 47
Chen, W., Chen, X., Li, D., Zhou, J., Jiang, Z., You, Q., & Guo, X. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00091 · Cited by 42
Targeting epigenetic machinery: Emerging novel allosteric inhibitors
Ye, F., Huang, J. L., Wang, H., Luo, C., & Zhao, K. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107406 · Cited by 47
Disease Association and Druggability of WD40 Repeat Proteins
Song, R., Wang, Z.-D., & Schapira, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00451 · Cited by 45
Self-citationFOXQ1 recruits the MLL complex to activate transcription of EMT and promote breast cancer metastasis
Mitchell, A. V., Wu, L., Block, C. J., Zhang, M., Hackett, J. B., Craig, D. B., Chen, W., Zhao, Y., Zhang, B., Dang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34239-z · Cited by 47
Mutant CEBPA directly drives the expression of the targetable tumor-promoting factor CD73 in AML
Jakobsen, J. S., Laursen, L. G., Schuster, M. B., Pundhir, S., Schoof, E. M., Ge, Y. C., D’Altri, T., Vitting‐Seerup, K., Rapin, N., Gentil, C., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw4304 · Cited by 49
Discovery of Potent Small-Molecule Inhibitors of WDR5-MYC Interaction
Ding, J. H., Li, G., Liu, H., Liu, L., Lin, Y., Gao, J., Zhou, G., Shen, L., Zhao, M., Yu, Y., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00843 · Cited by 43
Yu, X., Li, D., Kottur, J., Kim, H. S., Herring, L. E., Yu, Y., Xie, L., Hu, X., Chen, X., Cai, L., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01521 · Cited by 42
Wilhelmson, A. S., & Porse, B. T. (2020) · British Journal of Haematology · doi:10.1111/bjh.16534 · Cited by 45
Teuscher, K. B., Chowdhury, S., Meyers, K. M., Tian, J., Sai, J., Meveren, M. V., South, T. M., Sensintaffar, J., Rietz, T. A., Goswami, S., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2211297120 · Cited by 41
Boddu, P. C., Gupta, A. K., Roy, R., Avalos, B. D. L. P., Olazabal‐Herrero, A., Neuenkirchen, N., Zimmer, J. T., Chandhok, N. S., King, D. P., Nannya, Y., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.032 · Cited by 41
Mabanglo, M. F., Wilson, B., Noureldin, M., Kimani, S., Mamai, A., Krausser, C., González-Álvarez, H., Srivastava, S., Mohammed, M., Hoffer, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54500-x · Cited by 40
Self-citationHeparanase and Chemotherapy Synergize to Drive Macrophage Activation and Enhance Tumor Growth
Bhattacharya, U., Gutter-Kapon, L., Kan, T., Boyango, I., Barash, U., Yang, S., Liu, J., Gross-Cohen, M., Sanderson, R. D., Shaked, Y., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1676 · Cited by 40
Kato, I., Kasukabe, T., & Kumakura, S. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5116 · Cited by 38
WIN site inhibition disrupts a subset of WDR5 function
Siladi, A. J., Wang, J., Florian, A. C., Thomas, L. R., Creighton, J. H., Matlock, B. K., Flaherty, D. K., Lorey, S. L., Howard, G. C., Fesik, S. W., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-05947-9 · Cited by 35
Small molecule targeting of chromatin writers in cancer
Conery, A. R., Rocnik, J. L., & Trojer, P. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00920-5 · Cited by 36
CEBPA-mutated leukemia is sensitive to genetic and pharmacological targeting of the MLL1 complex
Schmidt, L., Heyes, E. C., Scheiblecker, L., Eder, T., Volpe, G., Frampton, J., Nerlov, C., Valent, P., Grembecka, J. E., & Grebien, F. (2019) · Leukemia · doi:10.1038/s41375-019-0382-3 · Cited by 35
Self-citationTargeting protein methylation: from chemical tools to precision medicines
Dilworth, D., & Baršytė-Lovejoy, D. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03147-9 · Cited by 35
Histone H3K4 Methyltransferases as Targets for Drug-Resistant Cancers
Liu, Y., Jin, M., & Jeong, K. W. (2021) · Biology · doi:10.3390/biology10070581 · Cited by 36
He, B., Pan, H., Zheng, F., Chen, S., Bie, Q., Cao, J., Zhao, R., Liang, J., Wei, L., Zeng, J., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02282-9 · Cited by 35
Chemically induced degradation of epigenetic targets
Kabir, M., Yu, X., Kanıskan, H. Ü., & Jin, J. J. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00100h · Cited by 36
Structure-based view of the druggable genome
Wang, J., Yazdani, S., Han, A., & Schapira, M. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.02.006 · Cited by 36
Self-citation
Metadata
- Authors
- Grebien, F., Vedadi, M., Getlik, M., Giambruno, R., Grover, A., Avellino, R., Skucha, A., Vittori, S., Kuznetsova, E., Smil, D., Barsyte-Lovejoy, D., Li, F., Poda, G., Schapira, M., Wu, H., Dong, A., Senisterra, G., Stukalov, A., Huber, K. V. M., Schönegger, A., Marcellus, R., Bilban, M., Bock, C., Brown, P. J., Zuber, J., Bennett, K. L., Al-awar, R., Delwel, R., Nerlov, C., Arrowsmith, C. H., & Superti-Furga, G.
- Affiliations
- Austrian Academy of Sciences (AT)
- University of Toronto (CA)
- Ontario Institute for Cancer Research (CA)
- MRC Weatherall Institute of Molecular Medicine (GB)
- Erasmus MC (NL)
- Medical University of Vienna (AT)
- Research Institute of Molecular Pathology (AT)
- Corresponding author
- Grebien, Florian
- Arrowsmith, Cheryl H
- ORCID
- Grebien, Florian
- Vedadi, Masoud
- Giambruno, Roberto
- Grover, Amit
- Avellino, Roberto
- Skucha, Anna
- Kuznetsova, Ekaterina
- Smil, David
- Li, Fengling
- Schapira, Matthieu
- Dong, Aiping
- Stukalov, Alexey
- Huber, Kilian V M
- Marcellus, Richard
- Bilban, Martin
- Bock, Christoph
- Brown, Peter J
- Zuber, Johannes
- Bennett, Keiryn L
- Delwel, Ruud
- Nerlov, Claus
- Arrowsmith, Cheryl H
- Superti-Furga, Giulio
- Venue
- Nature Chemical Biology
- Published
- 2015-07-13
- Volume
- 11
- Issue
- 8
- Pages
- 571-578
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W4294309410
- Cited by
- 284
- References
- 59
- Citations by year
- 2026: 19 · 2025: 20 · 2024: 33 · 2023: 26 · 2022: 27 · 2021: 35 · 2020: 21 · 2019: 30 · 2018: 25 · 2017: 16 · 2016: 24 · 2015: 8
- FWCI
- 20.44
- Type
- journal article
- Language
- en
- Update notices
- erratum (2015-09-17)
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Nature Chemical Biology (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (106169, 092809/Z/10/Z)
- Topics
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- WDR5, acute myeloid leukemia, CEBPA mutation, H3K4me3, myeloid differentiation, small molecule drug targets
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
