Bat3 facilitates H3K79 dimethylation by DOT1L and promotes DNA damage‐induced 53BP1 foci at G1/G2 cell‐cycle phases

Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair

Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · see citing works

Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain

Feng, Q. F., Wang, H., Ng, H., Erdjument‐Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 866 · see citing works

Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core

van Leeuwen, F., Gafken, P. R., & Gottschling, D. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00759-6 · Cited by 853 · see citing works

hDOT1L Links Histone Methylation to Leukemogenesis

Okada, Y., Feng, Q. F., Lin, Y.-H., Jiang, Q., Li, Y., Coffield, V. M., Su, L., Xu, G., & Zhang, Y. (2005) · Cell · doi:10.1016/j.cell.2005.02.020 · Cited by 819 · see citing works

The Paf1 Complex Is Required for Histone H3 Methylation by COMPASS and Dot1p: Linking Transcriptional Elongation to Histone Methylation

Krogan, N. J., Dover, J., Wood, A., Schneider, J., Heidt, J. W., Boateng, M. A., Dean, K., Ryan, O. W., Golshani, A., Johnston, M., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00091-1 · Cited by 706 · see citing works

Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation

McGinty, R. K., Kim, J., Chatterjee, C., Roeder, R. G., & Muir, T. W. (2008) · Nature · doi:10.1038/nature06906 · Cited by 563 · see citing works

Methylation of Histone H4 Lysine 20 Controls Recruitment of Crb2 to Sites of DNA Damage

Sanders, S. L., Portoso, M., Mata, J., Bähler, J., Allshire, R. C., & Kouzarides, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.009 · Cited by 545 · see citing works

DOT1L/KMT4 Recruitment and H3K79 Methylation Are Ubiquitously Coupled with Gene Transcription in Mammalian Cells

Steger, D. J., Lefterova, M. I., Ying, L., Stonestrom, A. J., Schupp, M., Zhuo, D. X., Vakoc, A. L., Kim, J., Chen, J., Lazar, M. A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02076-07 · Cited by 499 · see citing works

A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems

Hofmann, K., & Falquet, L. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01835-7 · Cited by 449 · see citing works

Transformation of myeloid progenitors by MLL oncoproteins is dependent on Hoxa7 and Hoxa9Preprint

Ayton, P. M., & Cleary, M. L. (2003) · Genes & Development · doi:10.1101/gad.1111603 · Cited by 438 · see citing works

Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase

Min, J., Feng, Q. F., Li, Z., Zhang, Y., & Xu, R.-M. (2003) · Cell · doi:10.1016/s0092-8674(03)00114-4 · Cited by 431 · see citing works

MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites

Pei, H., Zhang, L. M., Luo, K., Qin, Y., Chesi, M., Fei, Y. F., Bergsagel, P. L., Wang, L., You, Z., & Lou, Z. (2011) · Nature · doi:10.1038/nature09658 · Cited by 412 · see citing works

Sustained metabolic scope.

Peterson, C. C., Nagy, K. A., & Diamond, J. M. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.6.2324 · Cited by 388 · see citing works

The Histone H3K79 Methyltransferase Dot1L Is Essential for Mammalian Development and Heterochromatin Structure

Jones, B. T., Su, H., Bhat, A., Lei, H., Bajko, J., Hevi, S., Baltus, G. A., Kadam, S., Zhai, H., Valdez, R., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000190 · Cited by 384 · see citing works

Role of Dot1-Dependent Histone H3 Methylation in G1 and S Phase DNA Damage Checkpoint Functions of Rad9

Wysocki, R., Javaheri, A., Allard, S., Sha, F., Côté, J., & Kron, S. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8430-8443.2005 · Cited by 288 · see citing works

The DNA Damage Checkpoint Response Requires Histone H2B Ubiquitination by Rad6-Bre1 and H3 Methylation by Dot1

Giannattasio, M., Lazzaro, F., Plevani, P., & Muzi-Falconi, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414453200 · Cited by 287 · see citing works

Histone methyltransferase Dot1 and Rad9 inhibit single‐stranded DNA accumulation at DSBs and uncapped telomeres

Lazzaro, F., Sapountzi, V., Granata, M., Pellicioli, A., Vaze, M. B., Haber, J. E., Plevani, P., Lydall, D. A., & Muzi-Falconi, M. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.81 · Cited by 190 · see citing works

Linking Cell Cycle to Histone Modifications: SBF and H2B Monoubiquitination Machinery and Cell-Cycle Regulation of H3K79 Dimethylation

Schulze-Hentrich, J. M., Jackson, J., Nakanishi, S., Gardner, J. M., Hentrich, T., Haug, J., Johnston, M., Jaspersen, S. L., Kobor, M. S., & Shilatifard, A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.017 · Cited by 180 · see citing works

Leukaemic transformation by CALM–AF10 involves upregulation of Hoxa5 by hDOT1L

Okada, Y., Jiang, Q., Lemieux, M., Jeannotte, L., Su, L., & Zhang, Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1464 · Cited by 179 · see citing works

A Proteomic Analysis of Ataxia Telangiectasia-mutated (ATM)/ATM-Rad3-related (ATR) Substrates Identifies the Ubiquitin-Proteasome System as a Regulator for DNA Damage Checkpoints

Mu, J., Wáng, Y., Luo, H., Leng, M., Zhang, J., Yang, T., Besusso, D., Jung, S. Y., & Qin, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700079200 · Cited by 172 · see citing works

Histone ubiquitination: a tagging tail unfolds?

Jason, L. J. M., Moore, S. C., Lewis, J. D., Lindsey, G. G., & Ausió, J. (2002) · BioEssays · doi:10.1002/bies.10038 · Cited by 164 · see citing works

Identical short peptide sequences in unrelated proteins can have different conformations: a testing ground for theories of immune recognition.

Wilson, I. A., Haft, D., Getzoff, E. D., Tainer, J. A., Lerner, R. A., & Brenner, S. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.16.5255 · Cited by 163 · see citing works

DOT1L regulates dystrophin expression and is critical for cardiac functionPreprint

Nguyen, A. T., Xiao, B., Neppl, R. L., Kallin, E. M., Li, J., Chen, T., Wang, D.-Z., Xiao, X., & Zhang, Y. (2011) · Genes & Development · doi:10.1101/gad.2018511 · Cited by 155 · see citing works

A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-like domain.

Banerji, J., Sands, J. F., Strominger, J. L., & Spies, T. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.6.2374 · Cited by 146 · see citing works

Complicated Tails: Histone Modifications and the DNA Damage Response

Vidanes, G. M., Bonilla, C. Y., & Toczyski, D. P. (2005) · Cell · doi:10.1016/j.cell.2005.06.013 · Cited by 141 · see citing works

Histone modification-dependent and -independent pathways for recruitment of checkpoint protein Crb2 to double-strand breaksPreprint

Du, L.-L., Nakamura, T., & Russell, P. R. (2006) · Genes & Development · doi:10.1101/gad.1422606 · Cited by 141 · see citing works

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Scythe: a novel reaper‐binding apoptotic regulator

Thress, K. S., Henzel, W. J., Shillinglaw, W., & Kornbluth, S. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6135 · Cited by 126 · see citing works

Structure–Activity Analysis of Semisynthetic Nucleosomes: Mechanistic Insights into the Stimulation of Dot1L by Ubiquitylated Histone H2B

McGinty, R. K., Köhn, M., Chatterjee, C., Chiang, K. P., Pratt, M. R., & Muir, T. W. (2009) · ACS Chemical Biology · doi:10.1021/cb9002255 · Cited by 120 · see citing works

Docking onto chromatin via the Saccharomyces cerevisiae Rad9 Tudor domain

Grenon, M., Costelloe, T., Jimeno, S., O'Shaughnessy, A. M., Fitzgerald, J., Zgheib, O., Degerth, L., & Lowndes, N. F. (2007) · Yeast · doi:10.1002/yea.1441 · Cited by 110 · see citing works

BAT3 and SET1A Form a Complex with CTCFL/BORIS To Modulate H3K4 Histone Dimethylation and Gene Expression

Nguyen, P., Bar‐Sela, G., Sun, L., Bisht, K. S., Cui, H., Kohn, E. C., Feinberg, A. P., & Gius, D. R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00568-08 · Cited by 96 · see citing works

ES Cell Cycle Progression and Differentiation Require the Action of the Histone Methyltransferase Dot1L

Barry, E., Krueger, W. H., Jakuba, C. M., Veilleux, E. S., Ambrosi, D. J., Nelson, C. E., & Rasmussen, T. P. (2009) · Stem Cells · doi:10.1002/stem.86 · Cited by 80 · see citing works

Scythe Regulates Apoptosis-inducing Factor Stability during Endoplasmic Reticulum Stress-induced Apoptosis

Desmots, F., Russell, H. R., Michel, D., & McKinnon, P. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706419200 · Cited by 75 · see citing works

Structure and regulation of the mDot1 gene, a mouse histone H3 methyltransferase

Zhang, W., Hayashizaki, Y., & Kone, B. C. (2004) · Biochemical Journal · doi:10.1042/bj20030839 · Cited by 65 · see citing works

Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis

Sasaki, T., Marcon, E., McQuire, T., Arai, Y., Møens, P. B., & Okada, H. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802113 · Cited by 54 · see citing works

Scythe/BAT3 regulates apoptotic cell death induced by papillomavirus binding factor in human osteosarcoma

Tsukahara, T., Kimura, S., Ichimiya, S., Torigoe, T., Kawaguchi, S., Wada, T., Yamashita, T., & Sato, N. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2008.00991.x · Cited by 52 · see citing works

Unique proteasome subunit Xrpn10c is a specific receptor for the antiapoptotic ubiquitin‐like protein Scythe

Kikukawa, Y., Minami, R., Shimada, M., Kobayashi, M., Tanaka, K., Yokosawa, H., & Kawahara, H. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05032.x · Cited by 45 · see citing works

Regulation of the DNA Damage Response and Gene Expression by the Dot1L Histone Methyltransferase and the 53Bp1 Tumour Suppressor

Fitzgerald, J., Moureau, S., Drogaris, P., O’Connell, E., Abshiru, N. A., Verreault, A., Thibault, P., Grenon, M., & Lowndes, N. F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014714 · Cited by 41 · see citing works

Targeting DOT1L action and interactions in leukemia: the role of DOT1L in transformation and development

Barry, E., Corry, G. N., & Rasmussen, T. (2010) · Expert opinion on therapeutic targets · doi:10.1517/14728221003623241 · Cited by 38 · see citing works

Impaired recruitment of the histone methyltransferase DOT1L contributes to the incomplete reactivation of tumor suppressor genes upon DNA demethylation

Jacinto, F. V., Ballestar, E., & Esteller, M. (2009) · Oncogene · doi:10.1038/onc.2009.267 · Cited by 31 · see citing works

Cooperative Control of Crb2 by ATM Family and Cdc2 Kinases Is Essential for the DNA Damage Checkpoint in Fission Yeast

Nakamura, T., Moser, B. A., Du, L.-L., & Russell, P. R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10721-10730.2005 · Cited by 27 · see citing works

Free and chromatin-associated mono-, di-, and trimethylation of histone H4-lysine 20 during development and cell cycle progression

Karachentsev, D., Druzhinina, M. K., & Steward, R. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.12.019 · Cited by 26 · see citing works

BAT3 Interacts with Transforming Growth Factor-β (TGF-β) Receptors and Enhances TGF-β1-induced Type I Collagen Expression in Mesangial Cells

Kwak, J. H., Kim, S. I., Kim, J. K., & Choi, M. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802285200 · Cited by 22 · see citing works

Solution structure of UIM and interaction of tandem ubiquitin binding domains in STAM1 with ubiquitin

Lim, J.-S., Son, W.-S., Park, J. K., Kim, E. E., Lee, B., & Ahn, H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.12.103 · Cited by 13 · see citing works

Putting the Pieces Together: Histone H2B Ubiquitylation Directly Stimulates Histone H3K79 Methylation

Jeltsch, A., & Rathert, P. (2008) · ChemBioChem · doi:10.1002/cbic.200800414 · Cited by 4 · see citing works

The roles of DNA, RNA and histone methylation in ageing and cancer

Michalak, E. M., Burr, M. L., Bannister, A. J., & Dawson, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0143-1 · Cited by 549 · see citing works

Histone methylation and the DNA damage response

Gong, F., & Miller, K. M. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.09.003 · Cited by 247 · see citing works

Histone ubiquitination in the DNA damage response

Uckelmann, M., & Sixma, T. K. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.06.011 · Cited by 211 · see citing works

DOT1L cooperates with the c-Myc–p300 complex to epigenetically derepress CDH1 transcription factors in breast cancer progression

Cho, M.-H., Park, J.-H., Choi, H.-J., Park, M.-K., Won, H.-Y., Park, Y.-J., Lee, C. H., Oh, S.-H., Song, Y.-S., Kim, H. S., et al. (2015) · Nature Communications · doi:10.1038/ncomms8821 · Cited by 211 · see citing works

DOT1L and H3K79 Methylation in Transcription and Genomic Stability

Wood, K., Tellier, M., & Murphy, S. (2018) · Biomolecules · doi:10.3390/biom8010011 · Cited by 209 · see citing works

Emerging role of PI3K/AKT in tumor-related epigenetic regulation

Yang, Q., Jiang, W., & Hou, P. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.04.001 · Cited by 206 · see citing works

A Chromatin-Dependent Role of the Fragile X Mental Retardation Protein FMRP in the DNA Damage Response

Alpatov, R., Lesch, B. J., Nakamoto-Kinoshita, M., Blanco, M. A., Chen, S., Stützer, A., Armache, K., Simon, M. D., Xu, C., Ali, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.040 · Cited by 163 · see citing works

Structural Basis of Dot1L Stimulation by Histone H2B Lysine 120 Ubiquitination

Valencia‐Sánchez, M. I., Ioannes, P. D., Wang, M., Vasilyev, N., Chen, R., Nudler, E., Armache, J., & Armache, K. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.029 · Cited by 150 · see citing works

Perspectives on translational and therapeutic aspects of SIRT1 in inflammaging and senescence

Yao, H., & Rahman, I. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.06.031 · Cited by 137 · see citing works

Histone H2B monoubiquitination: roles to play in human malignancy

Cole, A. J., Clifton-Bligh, R. J., & Marsh, D. J. (2014) · Endocrine Related Cancer · doi:10.1530/erc-14-0185 · Cited by 129 · see citing works

Chromatin modifications and DNA repair: beyond double-strand breaks

House, N. C. M., Koch, M. R., & Freudenreich, C. H. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00296 · Cited by 128 · see citing works

The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle

Kim, W., Choi, M., & Kim, J.-E. (2014) · Cell Cycle · doi:10.4161/cc.28104 · Cited by 121 · see citing works

Role of histone deacetylase 2 in epigenetics and cellular senescence: implications in lung inflammaging and COPD

Yao, H., & Rahman, I. (2012) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00175.2012 · Cited by 107 · see citing works

The upstreams and downstreams of H3K79 methylation by DOT1L

Vlaming, H., & van Leeuwen, F. (2016) · Chromosoma · doi:10.1007/s00412-015-0570-5 · Cited by 102 · see citing works

Prognostic and therapeutic value of disruptor of telomeric silencing-1-like (DOT1L) expression in patients with ovarian cancer

Zhang, X., Liu, D., Li, M., Cao, C., Wan, D., Xi, B., Li, W., Tan, J., Wang, J., Wu, Z., et al. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0400-8 · Cited by 96 · see citing works

Preserving genome integrity and function: the DNA damage response and histone modifications

Kim, J. J., Lee, S. Y., & Miller, K. M. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1620676 · Cited by 95 · see citing works

Histone methylation and aging: Lessons learned from model systems

McCauley, B. S., & Dang, W. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.008 · Cited by 93 · see citing works

Aging as an Epigenetic Phenomenon

Ashapkin, V. V., Kutueva, L. I., & Vanyushin, B. F. (2017) · Current Genomics · doi:10.2174/1389202918666170412112130 · Cited by 92 · see citing works

BAT3 modulates p300-dependent acetylation of p53 and autophagy-related protein 7 (ATG7) during autophagy

Sebti, S., Prébois, C., Pérez-Gracia, E., Bauvy, C., Desmots, F., Pirot, N., Gongora, C., Bach, A.-S., Hubberstey, A. V., Palissot, V., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313618111 · Cited by 88 · see citing works

BAG6/BAT3: emerging roles in quality control for nascent polypeptides

Kawahara, H., Minami, R., & Yokota, N. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs149 · Cited by 85 · see citing works

A Ubiquitin-like Domain Recruits an Oligomeric Chaperone to a Retrotranslocation Complex in Endoplasmic Reticulum-associated Degradation

Xu, Y., Liu, Y., Lee, J., & Ye, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.449199 · Cited by 80 · see citing works

Small RNAs Recruit Chromatin-Modifying Enzymes MMSET and Tip60 to Reconfigure Damaged DNA upon Double-Strand Break and Facilitate Repair

Wang, Q., & Goldstein, M. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2334 · Cited by 78 · see citing works

The Chromatin Response to Double-Strand DNA Breaks and Their Repair

Aleksandrov, R., Hristova, R. H., Stoynov, S., & Gospodinov, A. G. (2020) · Cells · doi:10.3390/cells9081853 · Cited by 75 · see citing works

DOT1L: a key target in normal chromatin remodelling and in mixed-lineage leukaemia treatment

Sarno, F., Nebbioso, A., & Altucci, L. (2019) · Epigenetics · doi:10.1080/15592294.2019.1699991 · Cited by 76 · see citing works

DOT1L Inhibition Sensitizes MLL-Rearranged AML to Chemotherapy

Liu, W., Deng, L., Song, Y., & Redell, M. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098270 · Cited by 75 · see citing works

Bag6/Bat3/Scythe: A novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation

Lee, J., & Ye, Y. (2013) · BioEssays · doi:10.1002/bies.201200159 · Cited by 75 · see citing works

Menin “reads” H3K79me2 mark in a nucleosomal context

Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., Liu, Z., Jing, Y., Dang, S., Bao, X., et al. (2023) · Science · doi:10.1126/science.adc9318 · Cited by 71 · see citing works

Targeting the histone H3 lysine 79 methyltransferase DOT1L in MLL-rearranged leukemias

Yi, Y., & Ge, S. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01251-1 · Cited by 71 · see citing works

The histone methyltransferase DOT1L is required for proper DNA damage response, DNA repair, and modulates chemotherapy responsiveness

Kari, V., Raul, S. K., Henck, J. M., Kitz, J., Krämer, F., Kosinsky, R. L., Übelmesser, N., Mansour, W. Y., Eggert, J., Spitzner, M., et al. (2019) · Clinical Epigenetics · doi:10.1186/s13148-018-0601-1 · Cited by 72 · see citing works

DOT1L modulates the senescence-associated secretory phenotype through epigenetic regulation of IL1A

Leon, K. E., Buj, R., Lesko, E., Dahl, E. S., Chen, C.-W., Tangudu, N. K., Imamura-Kawasawa, Y., Kossenkov, A. V., Hobbs, R. P., & Aird, K. M. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202008101 · Cited by 70 · see citing works

Histone modifications and the DNA double-strand break response

Van, H. T., & Santos, M. A. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1542899 · Cited by 62 · see citing works

BAG-6, a jack of all trades in health and disease

Binici, J., & Koch, J. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1522-y · Cited by 63 · see citing works

Histone Methyltransferases as Therapeutic Targets for Kidney Diseases

Yu, C., & Zhuang, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01393 · Cited by 62 · see citing works

Dot1-Dependent Histone H3K79 Methylation Promotes Activation of the Mek1 Meiotic Checkpoint Effector Kinase by Regulating the Hop1 Adaptor

Ontoso, D., Acosta, I., van Leeuwen, F., Freire, R., & San-Segundo, P. A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003262 · Cited by 61 · see citing works

Epigenetic therapy with inhibitors of histone methylation suppresses DNA damage signaling and increases glioma cell radiosensitivity

Gürsoy-Yüzügüllü, Ö., Carman, C. L., Serafim, R. B., Myronakis, M. E., Valente, V., & Price, B. D. (2017) · Oncotarget · doi:10.18632/oncotarget.15543 · Cited by 59 · see citing works

Down-regulation of G9a triggers DNA damage response and inhibits colorectal cancer cells proliferation

Zhang, J., He, P., Xi, Y., Geng, M., Chen, Y., & Ding, J. (2015) · Oncotarget · doi:10.18632/oncotarget.2784 · Cited by 58 · see citing works

The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.

Wong, M., Polly, P., & Liu, T. (2015) · Europe PMC (PubMed Central) · Cited by 57 · see citing works

Interpreting the Epstein-Barr Virus (EBV) Epigenome Using High-Throughput Data

Arvey, A. J., Tempera, I., & Lieberman, P. M. (2013) · Viruses · doi:10.3390/v5041042 · Cited by 55 · see citing works

Silencing or inhibition of H3K79 methyltransferase DOT1L induces cell cycle arrest by epigenetically modulating c-Myc expression in colorectal cancer

Yang, L., Lei, Q., Li, L., Yang, J., Dong, Z., & Cui, H. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0778-y · Cited by 54 · see citing works

Biological function and regulation of histone and non-histone lysine methylation in response to DNA damage

Chen, Y., & Zhu, W. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmw050 · Cited by 52 · see citing works

Targeting the epigenetic machinery of cancer cells

Montenegro, M. F., Sánchez‐del‐Campo, L., Fernández-Pérez, M. P., Sáez‐Ayala, M., Cabezas‐Herrera, J., & Rodríguez‐López, J. N. (2014) · Oncogene · doi:10.1038/onc.2013.605 · Cited by 51 · see citing works

The chromatin network helps prevent cancer-associated mutagenesis at transcription-replication conflicts

Bayona‐Feliú, A., Herrera‐Moyano, E., Badra-Fajardo, N., Galván‐Femenía, I., Soler-Oliva, M. E., & Aguilera, A. (2023) · Nature Communications · doi:10.1038/s41467-023-42653-0 · Cited by 51 · see citing works

Histone methyltransferases: novel targets for tumor and developmental defects.

Yi, X., Jiang, X., Li, X., & Jiang, D. (2015) · PubMed Central · Cited by 50 · see citing works

DOT1L Activity Promotes Proliferation and Protects Cortical Neural Stem Cells from Activation of ATF4-DDIT3-Mediated ER Stress In Vitro

Roidl, D., Hellbach, N., Bovio, P. P., Villarreal, A., Heidrich, S., Nestel, S., Grüning, B. A., Bönisch, U., & Vogel, T. (2015) · Stem Cells · doi:10.1002/stem.2187 · Cited by 48 · see citing works

H3K9me3 and H4K20me3 represent the epigenetic landscape for 53BP1 binding to DNA lesions

Kovaříková, A. S., Legartová, S., Krejčí, J., & Bártová, E. (2018) · Aging · doi:10.18632/aging.101572 · Cited by 47 · see citing works

Histone modifications in DNA damage response

Cao, L., Shen, C., & Zhu, W. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5011-z · Cited by 45 · see citing works

The Chromatin Landscape Channels DNA Double-Strand Breaks to Distinct Repair Pathways

Chen, Z., & Tyler, J. K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.909696 · Cited by 42 · see citing works

Nuclear cathepsin D enhances TRPS1 transcriptional repressor function to regulate cell cycle progression and transformation in human breast cancer cells

Bach, A.-S., Derocq, D., Laurent‐Matha, V., Montcourrier, P., Sebti, S., Orsetti, B., Theillet, C. G., Gongora, C., Pattingre, S., Ibing, E., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4394 · Cited by 41 · see citing works

Nuclear BAG6-UBL4A-GET4 Complex Mediates DNA Damage Signaling and Cell Death

Krenciute, G., Liu, S., Yucer, N., Shi, Y., Ortiz, P., Liu, Q., Kim, B., Odejimi, A. O., Leng, M., Qin, J., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.443416 · Cited by 41 · see citing works

Role of Histone Methylation in Maintenance of Genome Integrity

Mushtaq, A., Mir, U. S., Hunt, C. R., Pandita, S., Tantray, W. W., Bhat, A., PANDITA, R. K., Altaf, M., & Pandita, T. K. (2021) · Genes · doi:10.3390/genes12071000 · Cited by 42 · see citing works

PHRF1 promotes genome integrity by modulating non-homologous end-joining

Chang, C.-F., Chu, P.-C., Wu, P.-Y., Yu, M.-Y., Lee, J.-Y., Tsai, M.-D., & Chang, M.-S. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.81 · Cited by 38 · see citing works

JMJD2 promotes acquired cisplatin resistance in non-small cell lung carcinoma cells

Duan, L., Perez, R. E., Chastain, P. D., Mathew, M. T., Bijukumar, D. R., & Maki, C. G. (2019) · Oncogene · doi:10.1038/s41388-019-0814-6 · Cited by 38 · see citing works

The role of H3K79 methylation in transcription and the DNA damage response

Ljungman, M. E., Parks, L., Hulbatte, R. S., & Bedi, K. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.11.001 · Cited by 36 · see citing works

Targeting the epigenetics of the DNA damage response in breast cancer

Montenegro, M. F., González-Guerrero, R., Sánchez‐del‐Campo, L., Piñero, A., Cabezas‐Herrera, J., & Rodríguez‐López, J. N. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.85 · Cited by 34 · see citing works

A role of the 53BP1 protein in genome protection: structural and functional characteristics of 53BP1-dependent DNA repair

Bártová, E., Legartová, S., Dundr, M., & Suchánková, J. (2019) · Aging · doi:10.18632/aging.101917 · Cited by 34 · see citing works

Transcription-coupled DNA double-strand break repair

Guha, S., & Bhaumik, S. R. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103211 · Cited by 32 · see citing works

The nucleosome: orchestrating DNA damage signaling and repair within chromatin

Agarwal, P., & Miller, K. M. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0017 · Cited by 27 · see citing works

Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties

Stulemeijer, I. J. E., Vos, D. E. D., van Harten, K., Joshi, O., Blomberg, O. S., van Welsem, T., Terweij, M., Vlaming, H., de Graaf, E. L., Altelaar, M. A. F., et al. (2015) · Scientific Reports · doi:10.1038/srep09824 · Cited by 25 · see citing works

Metabolic modulation of chromatin: implications for DNA repair and genomic integrity

Liu, J. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00182 · Cited by 25 · see citing works

Lysine Methyltransferase Inhibitors Impair H4K20me2 and 53BP1 Foci in Response to DNA Damage in Sarcomas, a Synthetic Lethality Strategy

Campillo‐Marcos, I., Monte-Serrano, E., Navarro-Carrasco, E., García-González, R., & Lazo, P. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.715126 · Cited by 23 · see citing works

Functional Roles of Acetylated Histone Marks at Mouse Meiotic Recombination Hot Spots

Getun, I. V., Wu, Z., Fallahi, M., Ouizem, S., Liu, Q., Li, W., Costi, R., Roush, W. R., Cleveland, J. L., & Bois, P. R. J. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00942-15 · Cited by 23 · see citing works

Structural basis for regulation of the nucleo-cytoplasmic distribution of Bag6 by TRC35

Mock, J., Xu, Y., Ye, Y., & Clemons, W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702940114 · Cited by 23 · see citing works

PARP1-DOT1L transcription axis drives acquired resistance to PARP inhibitor in ovarian cancer

Liu, C., Li, J., Xu, F., Chen, L., Ni, M., Wu, J., Zhao, H., Wu, Y., Li, J., Wu, X., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02025-8 · Cited by 22 · see citing works

A Novel, Non-Apoptotic Role for Scythe/BAT3: A Functional Switch between the Pro- and Anti-Proliferative Roles of p21 during the Cell Cycle

Yong, S. T., & Wang, X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038085 · Cited by 22 · see citing works

Characterization of Copy Number Variations in Oral Cavity Squamous Cell Carcinoma Reveals a Novel Role for MLLT3 in Cell Invasiveness

Wang, C., Kao, H., Chen, T.-W., Huang, Y., Cheng, H.-W., Yi, J., Hung, S., Wu, C., Lee, Y.-S., & Chang, K. (2019) · The Oncologist · doi:10.1634/theoncologist.2019-0063 · Cited by 22 · see citing works

Primitive Erythropoiesis in the Mouse is Independent of DOT1L Methyltransferase Activity

Malcom, C. A., Ratri, A., Piasecka‐Srader, J., Borosha, S., Chakravarthi, V. P., Alvarez, N. S., Vivian, J. L., Fields, T. A., Rumi, M. A. K., & Fields, P. E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.813503 · Cited by 21 · see citing works

Targeting of histone methyltransferase DOT1L plays a dual role in chemosensitization of retinoblastoma cells and enhances the efficacy of chemotherapy

Mao, Y., Sun, Y., Wu, Z., Zheng, J., Zhang, J., Zeng, J., Lee, C., & Kim, J. K. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04431-y · Cited by 20 · see citing works

Novel therapeutic strategies for MLL-rearranged leukemias

Wong, N.-H. M., & So, C. W. E. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194584 · Cited by 20 · see citing works

DOT1L-mediated RAP80 methylation promotes BRCA1 recruitment to elicit DNA repair

Tang, H., Lu, Y.-F., Zeng, R., Liu, C., Shu, Y., Wu, Y., Su, J., Di, L., Qian, J., Zhang, J., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320804121 · Cited by 19 · see citing works

Histone lysine modifying enzymes and their critical roles in DNA double-strand break repair

Zhang, J., Lu, X., MoghaddamKohi, S., Shi, L., Xu, X., & Zhu, W. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103206 · Cited by 18 · see citing works

Ubiquitin-H2AX fusions render 53BP1 recruitment to DNA damage sites independent of RNF8 or RNF168

Kocylowski, M. K., Rey, A. J., Stewart, G. S., & Halazonetis, T. D. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1010918 · Cited by 18 · see citing works

A cell cycle-independent mode of the Rad9-Dpb11 interaction is induced by DNA damage

di Cicco, G., Bantele, S. C. S., Reußwig, K.-U., & Pfander, B. (2017) · Scientific Reports · doi:10.1038/s41598-017-11937-z · Cited by 18 · see citing works

A PHF8 Homolog in C. elegans Promotes DNA Repair via Homologous Recombination

Lee, C., Hong, S., Lee, M. H., & Koo, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123865 · Cited by 17 · see citing works

Chromatin Ubiquitination Guides DNA Double Strand Break Signaling and Repair

Kolobynina, K. G., Rapp, A. W., & Cardoso, M. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.928113 · Cited by 17 · see citing works

An emerging maestro of immune regulation: how DOT1L orchestrates the harmonies of the immune system

Kealy, L. C., Runting, J., Thiele, D., & Scheer, S. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1385319 · Cited by 15 · see citing works

Chromatin modification and NBS1: their relationship in DNA double-strand break repair

Saito, Y., Zhou, H., & Kobayashi, J. (2015) · Genes & Genetic Systems · doi:10.1266/ggs.15-00010 · Cited by 15 · see citing works

Rare de novo gain-of-function missense variants in DOT1L are associated with developmental delay and congenital anomalies

Nil, Z., Deshwar, A. R., Huang, Y., Barish, S., Zhang, X., Choufani, S., Stabej, P. L. Q., Hayes, I., Yap, P., Haldeman‐Englert, C. R., et al. (2023) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2023.09.009 · Cited by 14 · see citing works

The in vivo dynamic interplay of MDC1 and 53BP1 at DNA damage-induced nuclear foci

Mok, M. T. S., & Henderson, B. R. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.025 · Cited by 13 · see citing works

Discovery of the first-in-class DOT1L PROTAC degrader

Yim, H., Sun, R., Xu, Z., Kim, H. S., Kim, M. J., Cao, T., Xie, L., Chen, X., Kanıskan, H. Ü., & Jin, J. J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117595 · Cited by 12 · see citing works

A DOT1B/Ribonuclease H2 Protein Complex Is Involved in R-Loop Processing, Genomic Integrity, and Antigenic Variation in Trypanosoma brucei

Eisenhuth, N., Vellmer, T., Rauh, E. T., Butter, F., & Janzen, C. J. (2021) · mBio · doi:10.1128/mbio.01352-21 · Cited by 10 · see citing works

Msl2 Is a Novel Component of the Vertebrate DNA Damage Response

Lai, Z., Moravcová, S., Canitrot, Y., Andrzejewski, L. P., Walshe, D. M., & Rea, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068549 · Cited by 9 · see citing works

DOT1L inhibition reprograms innate immunity to potentiate immunomodulatory drug responses in multiple myeloma.

Ishiguro, K., Kitajima, H., Niinuma, T., Maruyama, R., Tsukahara, T., Hirohashi, Y., Takaya, A., Kumegawa, K., Yoshido, A., Sekiguchi, S., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217941 · Cited by 8 · see citing works

Histone H3K36me3 mediates the genomic instability of Benzo[a]pyrene in human bronchial epithelial cells

Chen, S., Zhang, Z., Peng, H., Jiang, S., Xu, C., Ma, X., Zhang, L., Zhou, H., Xing, X., Chen, L., et al. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.123564 · Cited by 7 · see citing works

Genome maintenance in retinoblastoma: Implications for therapeutic vulnerabilities (Review)

Lee, C., & Kim, J. K. (2022) · Oncology Letters · doi:10.3892/ol.2022.13312 · Cited by 5 · see citing works

The Relationship Between DOT1L, Histone H3 Methylation, and Genome Stability in Cancer

Guppy, B. J., Jeusset, L. M., & McManus, K. J. (2017) · Current Molecular Biology Reports · doi:10.1007/s40610-017-0051-0 · Cited by 5 · see citing works

UVA irradiation strengthened an interaction between UBF1/2 proteins and H4K20 di-/tri-methylation

Stixová, L., Komůrková, D., Kovaříková, A. S., & Bártová, E. (2019) · Chromosome Research · doi:10.1007/s10577-018-9596-x · Cited by 5 · see citing works

The Role of RING Finger Proteins in Chromatin Remodeling and Biological Functions

Chai, X., Tao, Q., & Li, L. (2023) · Epigenomics · doi:10.2217/epi-2023-0234 · Cited by 5 · see citing works

The Role of DOT1L Methyltransferase Activity in Fetal HematopoiesisPreprint

Malcom, C. A., Piasecka‐Srader, J., Chakravarthi, V. P., Borosha, S., Ratri, A., Alvarez, N. S., Vivian, J. L., Fields, T. A., Rumi, M. A. K., & Fields, P. E. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.319889 · Cited by 5 · see citing works

Circular SNX25 encoded radioresistance augmenter facilitates DNA damage repair in hepatocellular carcinoma by targeting BAG6-GET4 interaction

Li, S., Gao, Y., Tang, Y., Dong, A., Hu, S., Wang, R., Gong, X., & Peng, Z. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08026-9 · Cited by 4 · see citing works

HLA-B-associated transcript 3 (Bat3) stabilizes and activates p53 in a HAUSP-dependent manner

Zhang, R., Cui, D., Xue, T., Lang, Y., Zhang, Y., Li, L., Sun, H., Kuang, Y., Li, G., & Tang, J. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz102 · Cited by 4 · see citing works

Loss of DOT1L disrupts neuronal transcription, behavior, and leads to a neurodevelopmental disorderPreprint

Maroni, M. J., Barton, M., Lynch, K., Deshwar, A. R., Campbell, P. D., Millard, J., Lee, R., Cohen, A., Ahmad, R., Paranjapye, A., et al. (2024) · medRxiv · doi:10.1101/2024.10.31.24314716 · Cited by 3 · see citing works

BAG6 promotes hepatocellular carcinoma growth via enhancing PLK1-mediated aerobic glycolysis

Zhang, W., Du, D., Lu, H., Zhang, W., & Lei, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149653 · Cited by 2 · see citing works

DOT1L Drives Endothelial‐to‐Mesenchymal Transition and Fibrotic Vascular Remodeling via H3K79 Methylation

Wang, Y., Peng, X., Chen, J., Zhang, Y., Zhang, T., Zhang, J., Fan, J., Zheng, H., Liu, Q., Song, Z., et al. (2026) · Advanced Science · doi:10.1002/advs.202515581 · Cited by 2 · see citing works

Screening of ApDOT1.9 interacting proteins and the potential function of interactor ApSNARE in the rapid growth regulation of Alexandrium pacificum

Zhu, Z., Zhang, Q., & Sui, Z. (2024) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2024.117080 · Cited by 2 · see citing works

Dot1L-dependent H3K79 methylation facilitates histone variant H2A.Z exchange at DNA double strand breaks and is required for high fidelity, homology-directed DNA repairPreprint

Alvarez, N. S., Brachova, P., Fields, T. A., & Fields, P. E. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/544981 · Cited by 2 · see citing works

Histone Post-Translational Modifications and DNA Double-Strand Break Repair in Neurodegenerative Diseases: An Epigenetic Perspective

Yeasmin, A., & Torrente, M. P. (2025) · Biology · doi:10.3390/biology14111556 · Cited by 1 · see citing works

DOT1L inhibition exerts the anti-tumor effect by activating interferon signaling in breast cancer cells

Yoshido, A., Ishiguro, K., Kitajima, H., Niinuma, T., Kumegawa, K., MAEZAWA, M., Tsukahara, T., Toyota, M., Yorozu, A., Sasaki, H., et al. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-02017-5 · Cited by 1 · see citing works

Impacts of Histone Lysine Methylation on Chromatin

Lanouette, S., Haddad, J. F., Zhang, P., & Couture, J.-F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00002-2 · Cited by 1 · see citing works

The histone methyltransferase DOT1L is required for DNA damage recognition and repair

Raul, S. K. (2017) · doi:10.53846/goediss-6102

Abstract 2482: Bat3 facilitates histone H3 lysine 79 dimethylation by DOT1L to promote ionizing radiation-induced 53BP1 foci formation during G1- and G2-phases of the cell cycle

Wakeman, T. P., Feng, J., & Wang, X. (2011) · Cancer Research · doi:10.1158/1538-7445.am2011-2482

Regulation of the dna damage response and gene expression by the dot1l histone methyltransferase and the 53bp1 tumour suppressor

Fitzgerald, J., Moureau, S., Drogaris, P., O’Connell, E., Abshiru, N. A., Verreault, A., Thibault, P., Grenon, M., & Lowndes, N. F. (2011) · ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) · doi:10.13025/27983

Role of Dot1-Dependent Histone H3 Methylation in G1 and S Phase DNA Damage Checkpoint Functions of Rad9

Wysocki, R., Javaheri, A., Allard, S., Sha, F., Côté, J., & Kron, S. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8430-8443.2005 · Cited by 288 · see citing works

Regulation and function of the tumour suppressor 53BP1 at sites of DNA damage

Moureau, S. (2013) · Arrow@dit (Dublin Institute of Technology) · doi:10.13025/17159

Deficiency in Bre1 Impairs Homologous Recombination Repair and Cell Cycle Checkpoint Response to Radiation Damage in Mammalian Cells

Chernikova, S. B., Dorth, J. A., Razorenova, O. V., Game, J. C., & Brown, J. M. (2010) · Radiation Research · doi:10.1667/rr2184.1 · Cited by 59 · see citing works