The Leukemogenicity of AML1-ETO Is Dependent on Site-Specific Lysine Acetylation

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works

Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain

Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559 · see citing works

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor

Bowers, E. M., Yan, G., Mukherjee, C., Orry, A., Wang, L., Holbert, M. A., Crump, N. T., Hazzalin, C. A., Liszczak, G., Yuan, H., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.006 · Cited by 666 · see citing works

AML1–ETO downregulates the granulocytic differentiation factor C/EBPα in t(8;21) myeloid leukemia

Pabst, T., Mueller, B. U., Harakawa, N., Schoch, C., Haferlach, T., Behre, G., Hiddemann, W., Zhang, D.-E., & Tenen, D. G. (2001) · Nature Medicine · doi:10.1038/86515 · Cited by 463 · see citing works

Interaction and functional cooperation of the leukemia‐associated factors AML1 and p300 in myeloid cell differentiation

Kitabayashi, I., Yokoyama, A., Shimizu, K., & Ohki, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.2994 · Cited by 305 · see citing works

Cell-cycle restriction limits DNA damage and maintains self-renewal of leukaemia stem cells

Viale, A., Franco, F., Orleth, A., Cambiaghi, V., Giuliani, V., Bossi, D., Ronchini, C., Ronzoni, S., Muradore, I., Monestiroli, S., et al. (2008) · Nature · doi:10.1038/nature07618 · Cited by 303 · see citing works

A previously unidentified alternatively spliced isoform of t(8;21) transcript promotes leukemogenesis.

Yan, M., Kanbe, E., Peterson, L. F., Boyapati, A., Miao, Y., Wang, Y., Chen, I.-M., Chen, Z., Rowley, J. D., Willman, C. L., et al. (2006) · Nature Medicine · doi:10.1038/nm1443 · Cited by 279 · see citing works

The myeloid master regulator transcription factor PU.1 is inactivated by AML1-ETO in t(8;21) myeloid leukemia

Vangala, R. K., Heiss-Neumann, M. S., Rangatia, J. S., Singh, S. M., Schoch, C., Tenen, D. G., Hiddemann, W., & Behre, G. (2003) · Blood · doi:10.1182/blood-2002-04-1288 · Cited by 245 · see citing works

Frequency analysis of human primitive haematopoietic stem cell subsets using a cobblestone area forming cell assay.

Breems, D. A., Blokland, E. A. W., Neben, S., & Ploemacher, R. (1994) · PubMed · Cited by 231 · see citing works

E Protein Silencing by the Leukemogenic AML1-ETO Fusion Protein

Zhang, J., Kalkum, M., Yamamura, S., Chait, B. T., & Roeder, R. G. (2004) · Science · doi:10.1126/science.1097937 · Cited by 211 · see citing works

The AML1-ETO fusion protein promotes the expansion of human hematopoietic stem cells

Mulloy, J. C., Cammenga, J., MacKenzie, K. L., Berguido, F. J., Moore, M. A. S., & Nimer, S. D. (2002) · Blood · doi:10.1182/blood.v99.1.15 · Cited by 208 · see citing works

Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias?

Minucci, S., Nervi, C., Lo‐Coco, F., & Pelicci, P. G. (2001) · Oncogene · doi:10.1038/sj.onc.1204336 · Cited by 202 · see citing works

Balancing dormant and self-renewing hematopoietic stem cells

Wilson, A., Laurenti, E., & Trumpp, A. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.08.005 · Cited by 201 · see citing works

Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activityPreprint

Zhao, X., Jankovic, V. S., Gural, A., Huang, G., Pardanani, A. D., Menéndez, S., Zhang, J., Dunne, R. F., Xiao, A., Erdjument‐Bromage, H., et al. (2008) · Genes & Development · doi:10.1101/gad.1632608 · Cited by 184 · see citing works

The AML1/ETO fusion protein activates transcription of BCL-2

Klampfer, L., Zhang, J., Zelenetz, A. O., Uchida, H., & Nimer, S. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.14059 · Cited by 182 · see citing works

The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity

Liu, Y., Cheney, M. D., Gaudet, J., Chruszcz, M., Lukasik, S. M., Sugiyama, D., Lary, J. W., Cole, J. L., Dauter, Z., Minor, W., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.012 · Cited by 137 · see citing works

Id1 restrains myeloid commitment, maintaining the self-renewal capacity of hematopoietic stem cells

Janković, V., Ciarrocchi, A., Boccuni, P., DeBlasio, T., Benezra, R., & Nimer, S. D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607894104 · Cited by 130 · see citing works

Synergistic up-regulation of the myeloid-specific promoter for the macrophage colony-stimulating factor receptor by AML1 and the t(8;21) fusion protein may contribute to leukemogenesis.

Rhoades, K. L., Hetherington, C. J., Rowley, J. D., Hiebert, S. W., Nucifora, G., Tenen, D. G., & Zhang, D. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11895 · Cited by 129 · see citing works

Eriocalyxin B induces apoptosis of t(8;21) leukemia cells through NF-κB and MAPK signaling pathways and triggers degradation of AML1-ETO oncoprotein in a caspase-3-dependent manner

Wang, L., Zhao, W.-L., Yan, J.-S., et al. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401996 · Cited by 121 · see citing works

AML1 Is Functionally Regulated through p300-mediated Acetylation on Specific Lysine Residues

Yamaguchi, Y., Kurokawa, M., Imai, Y., Izutsu, K., Asai, T., Ichikawa, M., Yamamoto, G., Nitta, E., Yamagata, T., Sasaki, K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400355200 · Cited by 111 · see citing works

Synthesis and Evaluation of a Potent and Selective Cell-Permeable p300 Histone Acetyltransferase Inhibitor

Zheng, Y. G., Balasubramanyam, K., Cebrat, M., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0558544 · Cited by 69 · see citing works

Effects of the leukemia-associated AML1-ETO protein on hematopoietic stem and progenitor cells

Nimer, S. D., & Moore, M. A. S. (2004) · Oncogene · doi:10.1038/sj.onc.1207673 · Cited by 56 · see citing works

RUNX1/AML1 DNA-binding domain and ETO/MTG8 NHR2-dimerization domain are critical to AML1-ETO9a leukemogenesis

Yan, M., Ahn, E.-Y. E., Hiebert, S. W., & Zhang, D. (2008) · Blood · doi:10.1182/blood-2008-04-153742 · Cited by 51 · see citing works

Transforming activity of AML1-ETO is independent of CBFβ and ETO interaction but requires formation of homo-oligomeric complexes

Kwok, C., Zeisig, B. B., Qiu, J. J., Dong, S., & So, C. W. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810558106 · Cited by 47 · see citing works

The t(8;21) translocation converts AML1 into a constitutive transcriptional repressor

Wildonger, J., & Mann, R. S. (2005) · Development · doi:10.1242/dev.01824 · Cited by 46 · see citing works

Post-translational modifications of Runx1 regulate its activity in the cell

Wang, L., Huang, G., Zhao, X., Hatlen, M. A., Vu, L., Liu, F., & Nimer, S. D. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2009.03.005 · Cited by 42 · see citing works

t(8;21)(q22;q22) fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression

Okumura, A. J., Peterson, L. F., Okumura, F., Boyapati, A., & Zhang, D. (2008) · Blood · doi:10.1182/blood-2007-11-124735 · Cited by 41 · see citing works

Structure of the AML1-ETO eTAFH domain–HEB peptide complex and its contribution to AML1-ETO activity

Park, S., Chen, W., Cierpicki, T., et al. (2009) · Blood · doi:10.1182/blood-2008-06-161307 · Cited by 39 · see citing works

A novel exon in AML1-ETO negatively influences the clonogenic potential of the t(8;21) in acute myeloid leukemia

Mannari, D., Gascoyne, D. M., Dunne, J., Chaplin, T., & Young, B. D. (2010) · Leukemia · doi:10.1038/leu.2009.288 · Cited by 12 · see citing works

Discovery of a selective catalytic p300/CBP inhibitor that targets lineage-specific tumours

Lasko, L. M., Jakob, C. G., Edalji, R. P., Qiu, W., Montgomery, D., Digiammarino, E. L., Hansen, T. M., Risi, R. M., Frey, R., Manaves, V., et al. (2017) · Nature · doi:10.1038/nature24028 · Cited by 858 · see citing works

Depletion of RUNX1/ETO in t(8;21) AML cells leads to genome-wide changes in chromatin structure and transcription factor binding

Ptasinska, A., Assi, S. A., Mannari, D., James, S. R., Williamson, D., Dunne, J., Hoogenkamp, M., Wu, M., Care, M., McNeill, H., et al. (2012) · Leukemia · doi:10.1038/leu.2012.49 · Cited by 184 · see citing works

Cancers with wrong HATs: the impact of acetylation

Di Cerbo, V., & Schneider, R. (2013) · Briefings in Functional Genomics · doi:10.1093/bfgp/els065 · Cited by 178 · see citing works

Targeted degradation of the enhancer lysine acetyltransferases CBP and p300

Vannam, R., Sayilgan, J., Ojeda, S., Karakyriakou, B., Hu, E., Kreuzer, J., Morris, R., Herrera Lopez, X. I., Rai, S., Haas, W., et al. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.12.004 · Cited by 177 · see citing works

Discovery of Highly Potent, Selective, and Orally Efficacious p300/CBP Histone Acetyltransferases Inhibitors

Yang, Y., Zhang, R., Li, Z., Mei, L., Wan, S., Ding, H., Chen, Z., Xing, J., Feng, H., Han, J., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01721 · Cited by 132 · see citing works

IKZF2 Drives Leukemia Stem Cell Self-Renewal and Inhibits Myeloid Differentiation

Park, S.-M., Cho, H., Thornton, A. M., Barlowe, T. S., Chou, T., Chhangawala, S., Fairchild, L., Taggart, J., Chow, A., Schurer, A., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.10.016 · Cited by 97 · see citing works

Vitamin C-induced epigenomic remodelling in IDH1 mutant acute myeloid leukaemia

Mingay, M., Chaturvedi, A., Bilenky, M., Cao, Q., Jackson, L., Hui, T., Moksa, M., Heravi-Moussavi, A., Humphries, R. K., Heuser, M., et al. (2018) · Leukemia · doi:10.1038/leu.2017.171 · Cited by 94 · see citing works

Inhibition of acetylation, is it enough to fight cancer?

López-Bañuelos, L., & Vega, L. (2022) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2022.103752 · Cited by 32 · see citing works

DBC1, p300, HDAC3, and Siah1 coordinately regulate ELL stability and function for expression of its target genes

Basu, S., Barad, M., Yadav, D., Nandy, A., Mukherjee, B., Sarkar, J., Chakrabarti, P., Mukhopadhyay, S., & Biswas, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912375117 · Cited by 22 · see citing works

Covalent Modifications of RUNX Proteins: Structure Affects Function

Blumenthal, E., Greenblatt, S., Huang, G., Ando, K., Xu, Y., & Nimer, S. D. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-10-3233-2_3 · Cited by 16 · see citing works

Site-Specific Quantification of Lysine Acetylation Using Isotopic Labeling

Miyagi, M. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.029 · Cited by 9 · see citing works

Versatility of ARD1/NAA10-mediated protein lysine acetylation

Vo, T. T. L., Jeong, C., Lee, S., Kim, K., Ha, E., & Seo, J. H. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0100-7 · Cited by 17 · see citing works

Measurement and Analysis of Lysine Acetylation by KAT Complexes In Vitro and In Vivo

Lashgari, A., Lambert, J., & Côté, J. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9434-2_5 · Cited by 3 · see citing works

A Method to Determine Lysine Acetylation Stoichiometries

Nakayasu, E. S., Wu, S., Sydor, M. A., Shukla, A. K., Weitz, K., Moore, R. J., Hixson, K. K., Kim, J., Petyuk, V., Monroe, M. E., et al. (2014) · International Journal of Proteomics · doi:10.1155/2014/730725 · Cited by 37 · see citing works

Acetylome analysis reveals the involvement of lysine acetylation in diverse biological processes in Phytophthora sojae

Li, D., Lv, B., Tan, L., Yang, Q., & Liang, W. (2016) · Scientific Reports · doi:10.1038/srep29897 · Cited by 40 · see citing works