The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The diverse functions of Dot1 and H3K79 methylation
Open accessAbstract
DOT1 (disruptor of telomeric silencing; also called Kmt4) was initially discovered in budding yeast in a genetic screen for genes whose deletion confers defects in telomeric silencing. Since the discovery ∼10 years ago that Dot1 and its mammalian homolog, DOT1L (DOT1-Like), possess histone methyltransferase activity toward histone H3 Lys 79, great progress has been made in characterizing their enzymatic activities and the role of Dot1/DOT1L-mediated H3K79 methylation in transcriptional regulation, cell cycle regulation, and the DNA damage response. In addition, gene disruption in mice has revealed that mouse DOT1L plays an essential role in embryonic development, hematopoiesis, cardiac function, and the development of leukemia. The involvement of DOT1L enzymatic activity in leukemogenesis driven by a subset of MLL (mixed-lineage leukemia) fusion proteins raises the possibility of targeting DOT1L for therapeutic intervention.
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Citations
Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845 · cited 3×
“This was further supported by Zhao and colleagues (Barski et al. 2007) using ChIP coupled with deep sequencing (ChIP-seq) to map mono-, di-, and trimethyl H3K79 in human CD4+ T cells.”
BackgroundInfluentialXu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875
Self-citationCombinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290
Self-citationMethylated 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 · cited 3×
“The first evidence that suggested a link between DOT1L-mediated H3K79 methylation and DNA damage repair came from the demonstration that the tandem tudor domain of the human 53BP1 protein binds to methylated H3K79 and is recruited to DNA DSBs (Huyen et al. 2004).”
BackgroundInfluentialMany paths to methyltransfer: a chronicle of convergence
Schubert, H. L., Blumenthal, R. M., & Cheng, X. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00090-2 · Cited by 876
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
PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression.
Liu, W., Tanasa, B., Tyurina, O. V., Zhou, T. Y., Gassmann, R., Liu, W. T., Ohgi, K. A., Benner, C., Garcia-Bassets, I., Aggarwal, A. K., et al. (2010) · Nature · doi:10.1038/nature09272 · Cited by 441 · cited 1×
“Thus far, with the exception of H3K79, all other known histone lysine residues subject to methylation can be demethylated by at least one histone demethylase (Klose et al. 2006; Klose and Zhang 2007; Cloos et al. 2008; Liu et al. 2010; Qi et al. 2010).”
Background
Cited by
Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
Black, J. C., Van Rechem, C., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,308
Potent inhibition of DOT1L as treatment of MLL-fusion leukemia
Daigle, S. R., Olhava, E. J., Therkelsen, C. A., Basavapathruni, A., Jin, L., Boriack-Sjodin, P. A., Allain, C. J., Klaus, C. R., Raimondi, A., Scott, M. P., et al. (2013) · Blood · doi:10.1182/blood-2013-04-497644 · Cited by 722
Resolving the 3D Landscape of Transcription-Linked Mammalian Chromatin Folding
Hsieh, T.-H. S., Cattoglio, C., Slobodyanyuk, E., Hansen, A. S., Rando, O. J., Tjian, R., & Darzacq, X. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.002 · Cited by 661
Epigenetic modifications of histones in cancer
Zhao, Z., & Shilatifard, A. (2019) · Genome Biology · doi:10.1186/s13059-019-1870-5 · Cited by 552
Metadata
- Authors
- Nguyen, A. T., & Zhang, Y.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-07-01
- Volume
- 25
- Issue
- 13
- Pages
- 1345-1358
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2094498537
- Cited by
- 597
- References
- 9
- Type
- posted content
- Language
- en
- Open access
- diamond
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