Pharmacological targeting of the Wdr5-MLL interaction in C/EBPα N-terminal leukemia

Fast gapped-read alignment with Bowtie 2

Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400 · see citing works

Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles

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

[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 · see citing works

<i>Coot</i> : 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 · see citing works

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 · see citing works

<i>Phaser</i> 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 · see citing works

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 · see citing works

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 14,671 · see citing works

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 · see citing works

Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels.

Shevchenko, A., Wilm, M., Vorm, O., & Mann, M. F. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 9,047 · see citing works

PRODRG: a tool for high-throughput crystallography of protein–ligand complexes

Schüttelkopf, A. W., & van Aalten, D. M. F. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904011679 · Cited by 4,815 · see citing works

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Niesen, F., Berglund, H., & Vedadi, M. (2007) · Nature Protocols · doi:10.1038/nprot.2007.321 · Cited by 2,420 · see citing works

Identifying ChIP-seq enrichment using MACS

Feng, J., Liu, T., Qin, B., Zhang, Y., & Liu, X. S. (2012) · Nature Protocols · doi:10.1038/nprot.2012.101 · Cited by 1,805 · see citing works

Parts per Million Mass Accuracy on an Orbitrap Mass Spectrometer via Lock Mass Injection into a C-trap

Olsen, J. V., de Godoy, L. M. F., Li, G., Maček, B., Mortensen, P., Pesch, R., Makarov, A., Lange, O., Horning, S. R., & Mann, M. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500030-mcp200 · Cited by 1,513 · see citing works

MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes

Davis, I., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh398 · Cited by 1,032 · see citing works

WDR5 Associates with Histone H3 Methylated at K4 and Is Essential for H3 K4 Methylation and Vertebrate Development

Wysocka, J., Swigut, T., Milne, T. A., Dou, Y., Zhang, X., Burlingame, A. L., Roeder, R. G., Brivanlou, A. H., & Allis, C. D. (2005) · Cell · doi:10.1016/j.cell.2005.03.036 · Cited by 820 · see citing works

Regulation of MLL1 H3K4 methyltransferase activity by its core components

Dou, Y., Milne, T. A., Ruthenburg, A. J., Lee, S., Lee, J. W., Verdine, G. L., Allis, C. D., & Roeder, R. G. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1128 · Cited by 764 · see citing works

Physical Association and Coordinate Function of the H3 K4 Methyltransferase MLL1 and the H4 K16 Acetyltransferase MOF

Dou, Y., Milne, T. A., Tackett, A. J., Smith, E. R., Fukuda, A., Wysocka, J., Allis, C. D., Chait, B. T., Hess, J. L., & Roeder, R. G. (2005) · Cell · doi:10.1016/j.cell.2005.04.031 · Cited by 665 · see citing works

Wdr5 Mediates Self-Renewal and Reprogramming via the Embryonic Stem Cell Core Transcriptional Network

Ang, Y.-S., Tsai, S., Lee, D., Monk, J. M., Su, J., Ratnakumar, K., Ding, J., Ge, Y., Darr, H., Chang, B., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.003 · Cited by 545 · see citing works

Enhancement of Hematopoietic Stem Cell Repopulating Capacity and Self-Renewal in the Absence of the Transcription Factor C/EBPα

Zhang, P., Iwasaki-Arai, J., Iwasaki, H., Fenyus, M. L., Dayaram, T., Owens, B. M., Shigematsu, H., Levantini, E., Huettner, C. S., Lekstrom-Himes, J. A., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.11.006 · Cited by 506 · see citing works

Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy

Huber, K., Salah, E., Radic-Sarikas, B., Gridling, M., Elkins, J. M., Stukalov, A., Jemth, A., Göktürk, C., Sanjiv, K., Strömberg, K., et al. (2014) · Nature · doi:10.1038/nature13194 · Cited by 398 · see citing works

Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance

Migliori, V., Müller, J., Phalke, S., Low, D. H. P., Bezzi, M., Mok, W. C., Sahu, S. K., Gunaratne, J., Capasso, P., Bassi, C., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2209 · Cited by 351 · see citing works

E2F Repression by C/EBPα Is Required for Adipogenesis and Granulopoiesis In Vivo

Porse, B. T., Pedersen, T. Å., Xu, X., Lindberg, B. G., Wewer, U. M., Friis-Hansen, L. J., & Nerlov, C. (2001) · Cell · doi:10.1016/s0092-8674(01)00516-5 · Cited by 316 · see citing works

Insights into GATA-1-Mediated Gene Activation versus Repression via Genome-wide Chromatin Occupancy Analysis

Yu, M., Riva, L., Xie, H., Schindler, Y. L., Moran, T. B., Cheng, Y., Yu, D., Hardison, R. C., Weiss, M. J., Orkin, S. H., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.002 · Cited by 308 · see citing works

Targeting MLL1 H3K4 Methyltransferase Activity in Mixed-Lineage Leukemia

Cao, F., Townsend, E. C., Karataş, H., Xu, J., Li, L., Lee, S. H. F., Liu, L., Chen, Y., Ouillette, P. D., Zhu, J., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.001 · Cited by 306 · see citing works

OLAV: Towards high‐throughput tandem mass spectrometry data identification

Colinge, J., Masselot, A., Giron, M., Dessingy, T., & Magnin, J. (2003) · PROTEOMICS · doi:10.1002/pmic.200300485 · Cited by 297 · see citing works

Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors

Yu, W., Chory, E. J., Wernimont, A. K., Tempel, W., Scopton, A. P., Alexander Joel Federation, Marineau, J., Qi, J., Baršytė-Lovejoy, D., Yi, J., et al. (2012) · Nature Communications · doi:10.1038/ncomms2304 · Cited by 283 · see citing works

C/EBPα mutations in acute myeloid leukaemias

Nerlov, C. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1363 · Cited by 277 · see citing works

Toolkit for evaluating genes required for proliferation and survival using tetracycline-regulated RNAi

Zuber, J., McJunkin, K., Fellmann, C., Dow, L. E., Taylor, M. J., Hannon, G., & Lowe, S. (2010) · Nature Biotechnology · doi:10.1038/nbt.1720 · Cited by 277 · see citing works

Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex

Ruthenburg, A. J., Wang, W., Graybosch, D. M., Li, H., Allis, C. D., Patel, D. J., & Verdine, G. L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1119 · Cited by 261 · see citing works

Molecular recognition of histone H3 by the WD40 protein WDR5

Couture, J., Collazo, E., & Trievel, R. C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1116 · Cited by 256 · see citing works

Modeling of C/EBPα Mutant Acute Myeloid Leukemia Reveals a Common Expression Signature of Committed Myeloid Leukemia-Initiating Cells

Kirstetter, P., Schuster, M. B., Bereshchenko, O., Moore, S., Dvinge, H., Kurz, E., Theilgaard-Mönch, K., Månsson, R., Pedersen, T. Å., Pabst, T., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.02.008 · Cited by 251 · see citing works

E2F Activation of S Phase Promoters via Association with HCF-1 and the MLL Family of Histone H3K4 Methyltransferases

Tyagi, S., Chabes, A. L., Wysocka, J., & Herr, W. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.030 · Cited by 247 · see citing works

PeakAnalyzer: Genome-wide annotation of chromatin binding and modification loci

Salmon‐Divon, M., Dvinge, H., Koort, K., & Bertone, P. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-415 · Cited by 238 · see citing works

Dysregulation of the C/EBPα Differentiation Pathway in Human Cancer

Koschmieder, S., Halmos, B., Levantini, E., & Tenen, D. G. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2008.17.9812 · Cited by 211 · see citing works

Cooperation between C/EBPα TBP/TFIIB and SWI/SNF recruiting domains is required for adipocyte differentiationPreprint

Pedersen, T. Å., Kowenz‐Leutz, E., Leutz, A., & Nerlov, C. (2001) · Genes & Development · doi:10.1101/gad.209901 · Cited by 196 · see citing works

CEBPA point mutations in hematological malignancies

Leroy, H., Roumier, C., Huyghe, P., Biggio, V., Fenaux, P., & Preudhomme, C. (2005) · Leukemia · doi:10.1038/sj.leu.2403614 · Cited by 191 · see citing works

WDR5 Interacts with Mixed Lineage Leukemia (MLL) Protein via the Histone H3-binding Pocket

Song, J., & Kingston, R. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806900200 · Cited by 189 · see citing works

The role of different genetic subtypes of CEBPA mutated AML

Fasan, A., Haferlach, C., Alpermann, T., Jeromin, S., Grossmann, V., Eder, C., Weißmann, S., Dicker, F., Kohlmann, A., Schindela, S., et al. (2013) · Leukemia · doi:10.1038/leu.2013.273 · Cited by 179 · see citing works

Structure of WDR5 Bound to Mixed Lineage Leukemia Protein-1 Peptide

Patel, A. B., Dharmarajan, V., & Cosgrove, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800164200 · Cited by 173 · see citing works

C/EBPα Inhibits Cell Growth via Direct Repression of E2F-DP-Mediated Transcription

Slomiany, B. A., D'Arigo, K. L., Kelly, M. M., & Kurtz, D. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5986-5997.2000 · Cited by 166 · see citing works

Small-molecule inhibition of MLL activity by disruption of its interaction with WDR5

Senisterra, G. A., Wu, H. Y., Allali‐Hassani, A., Wasney, G. A., Baršytė-Lovejoy, D., Dombrovski, L., Dong, A., Nguyen, K. T., Smil, D. V., Bolshan, Y., et al. (2012) · Biochemical Journal · doi:10.1042/bj20121280 · Cited by 165 · see citing works

Identification of two polypeptide segments of CCAAT/enhancer-binding protein required for transcriptional activation of the serum albumin gene.

Friedman, A. D., & McKnight, S. L. (1990) · Genes &amp; Development · doi:10.1101/gad.4.8.1416 · Cited by 162 · see citing works

The nuclear corepressor, NCoR, regulates thyroid hormone action in vivo

Astapova, I. I., Lee, L. J., Morales, C., Tauber, S., Bilban, M., & Hollenberg, A. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804604105 · Cited by 149 · see citing works

Three levels of functional interaction determine the activity of CCAAT/enhancer binding protein-alpha on the serum albumin promoter.Preprint

Nerlov, C., & Ziff, E. B. (1994) · Genes & Development · doi:10.1101/gad.8.3.350 · Cited by 131 · see citing works

Structural analysis of the KANSL1/WDR5/KANSL2 complex reveals that WDR5 is required for efficient assembly and chromatin targeting of the NSL complexPreprint

Dias, J. C., Nguyen, N. V., Georgiev, P., Gaub, A., Brettschneider, J., Cusack, S., Kadlec, J., & Akhtar, A. (2014) · Genes & Development · doi:10.1101/gad.240200.114 · Cited by 115 · see citing works

Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA binding and Runx1‐C/EBPα interaction

Fujimoto, T., Anderson, K., Jacobsen, S. E. W., Nishikawa, S.-I., & Nerlov, C. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601675 · Cited by 110 · see citing works

An Allosteric Inhibitor of Protein Arginine Methyltransferase 3

Siarheyeva, A., Senisterra, G. A., Allali‐Hassani, A., Dong, A., Dobrovetsky, E., Wasney, G. A., Chau, I., Marcellus, R. C., Hajian, T., Liu, F., et al. (2012) · Structure · doi:10.1016/j.str.2012.06.001 · Cited by 102 · see citing works

The amino terminal and E2F interaction domains are critical for C/EBPα-mediated induction of granulopoietic development of hematopoietic cells

D’Alò, F., Johansen, L. M., Nelson, E. A., Radomska, H. S., Evans, E. K., Zhang, P., Nerlov, C., & Tenen, D. G. (2003) · Blood · doi:10.1182/blood-2003-02-0479 · Cited by 98 · see citing works

Proteomic analysis of human cataract aqueous humour: Comparison of one-dimensional gel LCMS with two-dimensional LCMS of unlabelled and iTRAQ®-labelled specimens

Bennett, K. L., Funk, M., Tschernutter, M., Breitwieser, F. P., Planyavsky, M., Ubaida‐Mohien, C., Müller, A. C., Trajanoski, Z., Colinge, J., Superti‐Furga, G., et al. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.10.002 · Cited by 87 · see citing works

Deregulated expression of fat and muscle genes in B-cell chronic lymphocytic leukemia with high lipoprotein lipase expression

Bilban, M., Heintel, D., Scharl, T., Woelfel, T., Auer, M. M., Porpaczy, E. A., Kainz, B., Kröber, A., Carey, V. J., Shehata, M. M., et al. (2006) · Leukemia · doi:10.1038/sj.leu.2404220 · Cited by 78 · see citing works

Synthesis, Optimization, and Evaluation of Novel Small Molecules as Antagonists of WDR5-MLL Interaction

Bolshan, Y., Getlik, M., Kuznetsova, E., Wasney, G. A., Hajian, T., Poda, G. I., Nguyen, K. T., Wu, H. Y., Dombrovski, L., Dong, A., et al. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300467n · Cited by 74 · see citing works

C/EBPα and DEK coordinately regulate myeloid differentiation

Koleva, R., Ficarro, S. B., Radomska, H. S., Carrasco-Alfonso, M. J., Alberta, J. A., Webber, J. T., Luckey, C. J., Marcucci, G., Tenen, D. G., & Marto, J. A. (2012) · Blood · doi:10.1182/blood-2011-10-383083 · Cited by 53 · see citing works

Proteomic identification of C/EBP-DBD multiprotein complex: JNK1 activates stem cell regulator C/EBPα by inhibiting its ubiquitination

Trivedi, A. K., Bararia, D., Christopeit, M., Zada, A. A. P., Singh, S. M., Kieser, A., Hiddemann, W., Behre, H. M., & Behre, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209964 · Cited by 51 · see citing works

Modeling Contaminants in AP-MS/MS Experiments

Lavallée‐Adam, M., Cloutier, P., Coulombe, B., & Blanchette, M. (2010) · Journal of Proteome Research · doi:10.1021/pr100795z · Cited by 49 · see citing works

Cell cycle inhibition mediated by the outer surface of the C/EBPα basic region is required but not sufficient for granulopoiesis

Wang, Q., Cleaves, R., Kummalue, T., Nerlov, C., & Friedman, A. D. (2003) · Oncogene · doi:10.1038/sj.onc.1206360 · Cited by 46 · see citing works

C/EBPαp30, a myeloid leukemia oncoprotein, limits G-CSF receptor expression but not terminal granulopoiesis via site-selective inhibition of C/EBP DNA binding

Cleaves, R., Wang, Q., & Friedman, A. D. (2004) · Oncogene · doi:10.1038/sj.onc.1207172 · Cited by 45 · see citing works

Proteomic identification of the MYST domain histone acetyltransferase TIP60 (HTATIP) as a co-activator of the myeloid transcription factor C/EBPα

Bararia, D., Trivedi, A. K., Zada, A. A. P., Greif, P. A., Mulaw, M. A., Christopeit, M., Hiddemann, W., Bohlander, S. K., & Behre, G. (2008) · Leukemia · doi:10.1038/sj.leu.2405101 · Cited by 44 · see citing works

Proteomic discovery of Max as a novel interacting partner of C/EBPα: a Myc/Max/Mad link

Zada, A. A., Pulikkan, J. A., Bararia, D., Geletu, M., Trivedi, A. K., Balkhi, M. Y., Hiddemann, W., Tenen, D. G., Behre, H. M., & Behre, G. (2006) · Leukemia · doi:10.1038/sj.leu.2404438 · Cited by 31 · see citing works

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 · see citing works

Epigenetic modifications of histones in cancer

Zhao, Z., & Shilatifard, A. (2019) · Genome biology · doi:10.1186/s13059-019-1870-5 · Cited by 561 · see citing works

Epigenetic balance of gene expression by Polycomb and COMPASS families

Piunti, A., & Shilatifard, A. (2016) · Science · doi:10.1126/science.aad9780 · Cited by 524 · see citing works

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 · see citing works

WD40 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 · see citing works

Chemical and Biochemical Perspectives of Protein Lysine Methylation

Luo, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00008 · Cited by 288 · see citing works

Discovery of small molecule ligands for the von Hippel-Lindau (VHL) E3 ligase and their use as inhibitors and PROTAC degraders

Diehl, C. J., & Ciulli, A. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00387b · Cited by 259 · see citing works

Long noncoding RNA BLACAT2 promotes bladder cancer–associated lymphangiogenesis and lymphatic metastasis

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 · see citing works

PRMT5 Is a Critical Regulator of Breast Cancer Stem Cell Function via Histone Methylation and FOXP1 Expression

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 · see citing works

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 · see citing works

Targeting 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 189 · see citing works

A TGFβ-PRMT5-MEP50 axis regulates cancer cell invasion through histone H3 and H4 arginine methylation coupled transcriptional activation and repression

Chen, H., Lorton, B. M., Gupta, V., & Shechter, D. (2016) · Oncogene · doi:10.1038/onc.2016.205 · Cited by 184 · see citing works

MYC—Master Regulator of the Cancer Epigenome and Transcriptome

Poole, C. J., & van Riggelen, J. (2017) · Genes · doi:10.3390/genes8050142 · Cited by 177 · see citing works

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 175 · see citing works

Moonlighting with WDR5: A Cellular Multitasker

Guarnaccia, A. D., & Tansey, W. P. (2018) · Journal of Clinical Medicine · doi:10.3390/jcm7020021 · Cited by 151 · see citing works

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 154 · see citing works

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 147 · see citing works

PTEN regulates glioblastoma oncogenesis through chromatin-associated complexes of DAXX and histone H3.3

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 143 · see citing works

In Vivo Functional Platform Targeting Patient-Derived Xenografts Identifies WDR5-Myc Association as a Critical Determinant of Pancreatic Cancer

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 145 · see citing works

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 131 · see citing works

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 136 · see citing works

Displacement 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 128 · see citing works

Interaction of the oncoprotein transcription factor MYC with its chromatin cofactor WDR5 is essential for tumor maintenance

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 · see citing works

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 118 · see citing works

WDR5 Supports an N-Myc Transcriptional Complex That Drives a Protumorigenic Gene Expression Signature in Neuroblastoma

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 111 · see citing works

PROTAC’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 115 · see citing works

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 104 · see citing works

A comprehensive study of epigenetic alterations in hepatocellular carcinoma identifies potential therapeutic targets

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 107 · see citing works

C/EBPα creates elite cells for iPSC reprogramming by upregulating Klf4 and increasing the levels of Lsd1 and Brd4

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 103 · see citing works

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 106 · see citing works

Discovery of a Highly Potent, Cell-Permeable Macrocyclic Peptidomimetic (MM-589) Targeting the WD Repeat Domain 5 Protein (WDR5)–Mixed Lineage Leukemia (MLL) Protein–Protein Interaction

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 · see citing works

Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6

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 · see citing works

Structure-Based Optimization of a Small Molecule Antagonist of the Interaction Between WD Repeat-Containing Protein 5 (WDR5) and Mixed-Lineage Leukemia 1 (MLL1)

Getlik, 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 · see citing works

The 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 88 · see citing works

Mediator complex interaction partners organize the transcriptional network that defines neural stem cells

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 88 · see citing works

Targeting WD repeat domain 5 enhances chemosensitivity and inhibits proliferation and programmed death-ligand 1 expression in bladder cancer

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 · see citing works

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 · see citing works

WDR5 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 84 · see citing works

Structure, function and inhibition of critical protein–protein interactions involving mixed lineage leukemia 1 and its fusion oncoproteins

Li, X., & Song, Y. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01057-7 · Cited by 79 · see citing works

Targeted Disruption of the Interaction between WD-40 Repeat Protein 5 (WDR5) and Mixed Lineage Leukemia (MLL)/SET1 Family Proteins Specifically Inhibits MLL1 and SETd1A Methyltransferase Complexes

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 77 · see citing works

WD repeat domain 5 promotes chemoresistance and Programmed Death-Ligand 1 expression in prostate cancer

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 · see citing works

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 · see citing works

Discovery of Potent 2-Aryl-6,7-dihydro-5 H -pyrrolo[1,2- a ]imidazoles as WDR5-WIN-Site Inhibitors Using Fragment-Based Methods and Structure-Based Design

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 · see citing works

The molecular mechanics of mixed lineage leukemia

Slany, R. K. (2016) · Oncogene · doi:10.1038/onc.2016.30 · Cited by 72 · see citing works

C/EBPα deregulation as a paradigm for leukemogenesis

Pulikkan, J., Tenen, D., & Behre, G. (2017) · Leukemia · doi:10.1038/leu.2017.229 · Cited by 62 · see citing works

Interplay between cofactors and transcription factors in hematopoiesis and hematological malignancies

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 · see citing works

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 72 · see citing works

Direct and Indirect Targeting of HOXA9 Transcription Factor in Acute Myeloid Leukemia

Lambert, M., Alioui, M., Jambon, S., Depauw, S., van Seuningen, I., & David-Cordonnier, M. (2019) · Cancers · doi:10.3390/cancers11060837 · Cited by 58 · see citing works

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 68 · see citing works

A comprehensive review of genetic alterations and molecular targeted therapies for the implementation of personalized medicine in acute myeloid leukemia

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 67 · see citing works

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 67 · see citing works

Discovery and Optimization of Salicylic Acid-Derived Sulfonamide Inhibitors of the WD Repeat-Containing Protein 5–MYC Protein–Protein Interaction

Macdonald, 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 · see citing works

Discovery and Structure-Based Optimization of Potent and Selective WD Repeat Domain 5 (WDR5) Inhibitors Containing a Dihydroisoquinolinone Bicyclic Core

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 · see citing works

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 · see citing works

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 62 · see citing works

LSD1 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 62 · see citing works

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 65 · see citing works

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 · see citing works

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 61 · see citing works

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 · see citing works

Targeting non-bromodomain chromatin readers

Arrowsmith, C. H., & Schapira, M. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0290-2 · Cited by 58 · see citing works

Methyltransferase Inhibitors: Competing with, or Exploiting the Bound Cofactor

de Freitas, R. F., Ivanochko, D., & Schapira, M. (2019) · Molecules · doi:10.3390/molecules24244492 · Cited by 54 · see citing works

Inhibition of the H3K4 methyltransferase MLL1/WDR5 complex attenuates renal senescence in ischemia reperfusion mice by reduction of p16

Shimoda, H., Doi, S., Nakashima, A., Sasaki, K., Doi, T., & Masaki, T. (2019) · Kidney International · doi:10.1016/j.kint.2019.06.021 · Cited by 54 · see citing works

Structure-based design and synthesis of small molecular inhibitors disturbing the interaction of MLL1-WDR5

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 · see citing works

The c-MYC-WDR43 signalling axis promotes chemoresistance and tumour growth in colorectal cancer by inhibiting p53 activity

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 · see citing works

High-affinity small molecular blockers of mixed lineage leukemia 1 (MLL1)-WDR5 interaction inhibit MLL1 complex H3K4 methyltransferase activity

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 · see citing works

lncRNA GCAWKR Promotes Gastric Cancer Development by Scaffolding the Chromatin Modification Factors WDR5 and KAT2A

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 · see citing works

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 51 · see citing works

WDR5 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 · see citing works

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 · see citing works

Chemical Inhibition of Protein Methyltransferases

Schapira, M. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.07.014 · Cited by 49 · see citing works

Drug 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 49 · see citing works

Trib1 promotes acute myeloid leukemia progression by modulating the transcriptional programs of Hoxa9

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 49 · see citing works

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 · see citing works

Next-Generation Drugs and Probes for Chromatin Biology: From Targeted Protein Degradation to Phase Separation

Čermáková, K., & Hodges, H. C. (2018) · Molecules · doi:10.3390/molecules23081958 · Cited by 49 · see citing works

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 48 · see citing works

Chemical modulators for epigenome reader domains as emerging epigenetic therapies for cancer and inflammation

Zaware, N., & Zhou, M. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.012 · Cited by 47 · see citing works

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 45 · see citing works

Betaine restores epigenetic control and supports neuronal mitochondria in the cuprizone mouse model of multiple sclerosis

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 · see citing works

Discovery of DDO-2213 as a Potent and Orally Bioavailable Inhibitor of the WDR5–Mixed Lineage Leukemia 1 Protein–Protein Interaction for the Treatment of MLL Fusion Leukemia

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 46 · see citing works

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 45 · see citing works

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 · see citing works

FOXQ1 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 45 · see citing works

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 44 · see citing works

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 · see citing works

Discovery of Potent and Selective WDR5 Proteolysis Targeting Chimeras as Potential Therapeutics for Pancreatic Cancer

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 43 · see citing works

CCAAT enhancer binding protein alpha (CEBPA) biallelic acute myeloid leukaemia: cooperating lesions, molecular mechanisms and clinical relevance

Wilhelmson, A. S., & Porse, B. T. (2020) · British Journal of Haematology · doi:10.1111/bjh.16534 · Cited by 43 · see citing works

Structure-based discovery of potent WD repeat domain 5 inhibitors that demonstrate efficacy and safety in preclinical animal models

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 · see citing works

Transcription elongation defects link oncogenic SF3B1 mutations to targetable alterations in chromatin landscape

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 39 · see citing works

Crystal structures of DCAF1-PROTAC-WDR5 ternary complexes provide insight into DCAF1 substrate specificity

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 · see citing works

Heparanase 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 · see citing works

Menin‑MLL inhibitors induce ferroptosis and enhance the anti‑proliferative activity of auranofin in several types of cancer cells

Kato, I., Kasukabe, T., & Kumakura, S. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5116 · Cited by 37 · see citing works

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 37 · see citing works

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 · see citing works

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 · see citing works

Targeting 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 · see citing works

Histone H3K4 Methyltransferases as Targets for Drug-Resistant Cancers

Liu, Y., Jin, M., & Jeong, K. W. (2021) · Biology · doi:10.3390/biology10070581 · Cited by 35 · see citing works

Long noncoding RNA LINC00930 promotes PFKFB3-mediated tumor glycolysis and cell proliferation in nasopharyngeal carcinoma

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 · see citing works

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 35 · see citing works

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 34 · see citing works

Recruitment of the MLL complex via specific interaction of the p30 variant of C/EBPα with Wdr5 is essential for development of acute myeloid leukemia

Grebien, F., Giambruno, R., Grover, A., Vittori, S., Schönegger, A., Bilban, M., Bock, C., Zuber, J. A., Bennett, K. L., Nerlov, C., et al. (2013) · Experimental Hematology · doi:10.1016/j.exphem.2013.05.075

CEBPA-Mutant Acute Myeloid Leukemia is Sensitive to Small-Molecule-Mediated Inhibition of the Menin-MLL Interaction

Schmidt, L., Heyes, E. C., Scheiblecker, L., Eder, T., Volpe, G., Frampton, J., Nerlov, C., Valent, P., Grembecka, J. E., & Grebien, F. (2018) · Experimental Hematology · doi:10.1016/j.exphem.2018.06.142

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 · see citing works

Identification of gene targets of mutant C/EBPα reveals a critical role for MSI2 in CEBPA-mutated AML

Heyes, E. C., Schmidt, L., Manhart, G., Eder, T., Proietti, L., & Grebien, F. (2021) · Leukemia · doi:10.1038/s41375-021-01169-6 · Cited by 22 · see citing works

Dissecting the Molecular Mechanisms of Mutant C/EBPalpha (p30) in Normal and Malignant Human Hematopoiesis.

Cammenga, J., Niebuhr, B., Horn, S., Delwel, R., & Stocking, C. (2005) · Blood · doi:10.1182/blood.v106.11.2995.2995