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TET1 and hydroxymethylcytosine in transcription and DNA methylation fidelity
Open accessAbstract
Enzymes catalysing the methylation of the 5-position of cytosine (mC) have essential roles in regulating gene expression and maintaining cellular identity. Recently, TET1 was found to hydroxylate the methyl group of mC, converting it to 5-hydroxymethyl cytosine (hmC). Here we show that TET1 binds throughout the genome of embryonic stem cells, with the majority of binding sites located at transcription start sites (TSSs) of CpG-rich promoters and within genes. The hmC modification is found in gene bodies and in contrast to mC is also enriched at CpG-rich TSSs. We provide evidence further that TET1 has a role in transcriptional repression. TET1 binds a significant proportion of Polycomb group target genes. Furthermore, TET1 associates and colocalizes with the SIN3A co-repressor complex. We propose that TET1 fine-tunes transcription, opposes aberrant DNA methylation at CpG-rich sequences and thereby contributes to the regulation of DNA methylation fidelity.
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“identifying 22 differentially expressed E3 ligase genes that may undergo epigenetic regulation by Tet1 (supplemental Table 1).”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [47]
Experimental — accuracy not yet measuredIn the citing paper
“This is perhaps unsurprising since HDAC1/2 themselves (Fig. 4C) and their related complex components, Sin3A37 and LSD138, all map within the vicinity of TSS.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [37]
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Cites
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
Genome-wide maps of chromatin state in pluripotent and lineage-committed cells
Mikkelsen, T. S., Ku, M., Jaffe, D. B., Issac, B., Lieberman, E., Giannoukos, G., Alvarez, P., Brockman, W., Kim, T.-K., Koche, R. P., et al. (2007) · Nature · doi:10.1038/nature06008 · Cited by 4,129
DNA methylation landscapes: Provocative insights from epigenomics
Suzuki, M. M., & Bird, A. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2341 · Cited by 3,039
The Nuclear DNA Base 5-Hydroxymethylcytosine Is Present in Purkinje Neurons and the Brain
Kriaucionis, S., & Heintz, N. (2009) · Science · doi:10.1126/science.1169786 · Cited by 2,700
Ito, S., D’Alessio, A. C., Taranova, O., Hong, K., Sowers, L. C., & Zhang, Y. (2010) · Nature · doi:10.1038/nature09303 · Cited by 2,628
Genome-scale DNA methylation maps of pluripotent and differentiated cells
Meissner, A., Mikkelsen, T. S., Gu, H., Wernig, M., Hanna, J., Sivachenko, A., Zhang, X., Bernstein, B. E., Nusbaum, C., Jaffe, D. B., et al. (2008) · Nature · doi:10.1038/nature07107 · Cited by 2,536
Linking DNA methylation and histone modification: patterns and paradigms
Cedar, H., & Bergman, Y. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2540 · Cited by 2,267
Weber, M., Davies, J. J., Wittig, D., Oakeley, E. J., Haase, M., Lam, W. L., & Schübeler, D. (2005) · Nature Genetics · doi:10.1038/ng1598 · Cited by 1,785
Mutation in TET2 in Myeloid Cancers
Delhommeau, F., Dupont, S., Valle, V. D., James, C., Trannoy, S., Massé, A., Kosmider, O., Le Couedic, J.-P., Robert, F., Alberdi, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810069 · Cited by 1,776
Conserved role of intragenic DNA methylation in regulating alternative promoters
Maunakea, A. K., Nagarajan, R. P., Bilenky, M., Ballinger, T. J., D’Souza, C., Fouse, S. D., Johnson, B. E., Hong, C., Nielsen, C., Zhao, Y., et al. (2010) · Nature · doi:10.1038/nature09165 · Cited by 1,743
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Guo, J. U., Su, Y., Zhong, C., Ming, G.-L., & Song, H. (2011) · Cell Cycle · doi:10.4161/cc.10.16.17093 · Cited by 235
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Song, C., Clark, T. A., Lu, X., Kislyuk, A. O., Dai, Q., Turner, S. W., He, C., & Korlach, J. (2011) · Nature Methods · doi:10.1038/nmeth.1779 · Cited by 235
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Xu, Y., Lv, L., Liu, Y., Smith, M. D., Li, W., Tan, X. M., Cheng, M., Li, Z., Bovino, M., Aubé, J., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci129317 · Cited by 230
Embryonic stem cell and induced pluripotent stem cell: an epigenetic perspective
Liang, G., & Zhang, Y. (2012) · Cell Research · doi:10.1038/cr.2012.175 · Cited by 232
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Huang, H., Jiang, X., Li, Z., Li, Y., Song, C., He, C., Sun, M., Chen, P., Gurbuxani, S. K., Wang, J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310656110 · Cited by 228
Transcription Factor Occupancy Can Mediate Active Turnover of DNA Methylation at Regulatory Regions
Feldmann, A., Ivánek, R., Murr, R., Gaidatzis, D., Burger, L., & Schübeler, D. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003994 · Cited by 228
DNA methylation methods: Global DNA methylation and methylomic analyses
Li, S., & Tollefsbol, T. O. (2020) · Methods · doi:10.1016/j.ymeth.2020.10.002 · Cited by 230
Active turnover of DNA methylation during cell fate decisions
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Song, C., Yi, C., & He, C. (2012) · Nature Biotechnology · doi:10.1038/nbt.2398 · Cited by 202
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Verma, N., Pan, H., Doré, L. C., Shukla, A., Li, Q. V., Pelham‐Webb, B., Teijeiro, V., Gonzãlez, F., Krivtsov, A. V., Chang, C.-J., et al. (2017) · Nature Genetics · doi:10.1038/s41588-017-0002-y · Cited by 208
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Yu, H., Su, Y., Shin, J., Zhong, C., Guo, J. U., Weng, Y., Gao, F., Geschwind, D. H., Coppola, G., Ming, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4008 · Cited by 199
Dynamics of 5-hydroxymethylcytosine during mouse spermatogenesis
Gan, H., Wen, L., Liao, S., Lin, X., Ma, T., Liu, J., Song, C., Wang, M., He, C., Han, C., et al. (2013) · Nature Communications · doi:10.1038/ncomms2995 · Cited by 203
Li, X., Wei, W., Zhao, Q., Widagdo, J., Baker‐Andresen, D., Flavell, C. R., D’Alessio, A. C., Zhang, Y., & Bredy, T. W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318906111 · Cited by 192
Nabel, C. S., Manning, S. A., & Kohli, R. M. (2011) · ACS Chemical Biology · doi:10.1021/cb2002895 · Cited by 197
Dynamics and Context-Dependent Roles of DNA Methylation
Ambrosi, C. M., Manzo, M., & Baubec, T. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.02.008 · Cited by 201
Dynamic hydroxymethylation of deoxyribonucleic acid marks differentiation-associated enhancers
Sérandour, A. A., Avner, S., Oger, F., Bizot, M., Percevault, F., Lucchetti-Miganeh, C., Palierne, G., Gheeraert, C., Barloy-Hubler, F., Péron, C. L., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks595 · Cited by 199
Neri, F., Incarnato, D., Krepelova, A., Rapelli, S., Pagnani, A., Zecchina, R., Parlato, C., & Oliviero, S. (2013) · Genome Biology · doi:10.1186/gb-2013-14-8-r91 · Cited by 179
DNA methylation dynamics in aging: how far are we from understanding the mechanisms?
Ciccarone, F., Tagliatesta, S., Caiafa, P., & Zampieri, M. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.12.002 · Cited by 191
de Groote, M. L., Verschure, P. J., & Rots, M. G. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks863 · Cited by 180
An Intrinsic Epigenetic Barrier for Functional Axon Regeneration
Weng, Y., An, R., Cassin, J., Joseph, J., Mi, R., Wang, C., Zhong, C., Jin, S., Pfeifer, G. P., Bellacosa, A., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.034 · Cited by 178
Guallar, D., Bi, X., Pardavila, J. Á., Huang, X., Sáenz, C., Shi, X., Zhou, H., Faiola, F., Ding, J., Haruehanroengra, P., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0060-9 · Cited by 183
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
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Feng, J., Shao, N., Szulwach, K. E., Vialou, V., Huynh, J. L., Zhong, C., Le, T. T., Ferguson, D., Cahill, M. E., Li, Y., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.3976 · Cited by 181
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Orr, B. A., Haffner, M. C., Nelson, W. G., Yegnasubramanian, S., & Eberhart, C. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041036 · Cited by 180
Wang, T., Pan, Q., Li, L., Szulwach, K. E., Song, C., He, C., Wu, H., Warren, S. T., Jin, P., Duan, R., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds394 · Cited by 181
A heterozygous IDH1R132H/WT mutation induces genome-wide alterations in DNA methylationPreprint
Duncan, C. G., Barwick, B. G., Jin, G., Rago, C., Kapoor-Vazirani, P., Powell, D. R., Chi, J., Bigner, D. D., Vertino, P. M., & Yan, H. (2012) · Genome Research · doi:10.1101/gr.132738.111 · Cited by 183
High-Resolution Enzymatic Mapping of Genomic 5-Hydroxymethylcytosine in Mouse Embryonic Stem Cells
Sun, Z., Terragni, J., Borgaro, J. G., Liu, Y., Yu, L., Guan, S., Wang, H., Sun, D., Cheng, X., Zhu, Z., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.001 · Cited by 173
Tissue-specific Distribution and Dynamic Changes of 5-Hydroxymethylcytosine in Mammalian Genomes
Kinney, S. R. M., Chin, H. G., Vaisvila, R., Bitinaite, J., Zheng, Y., Estève, P., Feng, S., Stroud, H., Jacobsen, S. E., & Pradhan, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.217083 · Cited by 172
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Carty, S. A., Gohil, M., Banks, L. B., Cotton, R. M., Johnson, M. E., Stelekati, E., Wells, A. D., Wherry, E. J., Koretzky, G. A., & Jordan, M. S. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700559 · Cited by 175
TET1-Mediated Hydroxymethylation Facilitates Hypoxic Gene Induction in Neuroblastoma
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Genomic patterns and context specific interpretation of DNA methylation
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Personalized treatment strategies in glioblastoma: MGMT promoter methylation status
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Mechanisms that regulate the activities of TET proteins
Joshi, K., Liu, S., Breslin, P., & Zhang, J. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04396-x · Cited by 177
Induced DNA demethylation by targeting Ten-Eleven Translocation 2 to the human ICAM-1 promoter
Chen, H., Kazemier, H. G., de Groote, M. L., Ruiters, M. H. J., Xu, G., & Rots, M. G. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1019 · Cited by 164
Hore, T. A., von Meyenn, F., Ravichandran, M., Bachman, M., Ficz, G., Oxley, D., Santos, F., Balasubramanian, S., Jurkowski, T. P., & Reik, W. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608679113 · Cited by 172
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Hartnett, L., & Egan, L. J. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs006 · Cited by 165
Shi, F.-T., Kim, H., Lu, W., He, Q., Liu, D., Goodell, M. A., Wan, M., & Songyang, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.460386 · Cited by 168
He, Q., Kim, H., Huang, R., Lu, W., Tang, M., Shi, F.-T., Dong, Y., Zhang, X., Huang, J., Liu, D., et al. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.07.022 · Cited by 165
Functions of DNA Methylation and Hydroxymethylation in Mammalian Development
Guibert, S., & Weber, M. (2013) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-416027-9.00002-4 · Cited by 173
Hill, P. W. S., Amouroux, R., & Hájková, P. (2014) · Genomics · doi:10.1016/j.ygeno.2014.08.012 · Cited by 161
DNMT3A and TET1 cooperate to regulate promoter epigenetic landscapes in mouse embryonic stem cells
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TET1 regulates hypoxia-induced epithelial-mesenchymal transition by acting as a co-activator
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Hypothesis: Environmental regulation of 5-hydroxymethylcytosine by oxidative stress
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Xia, B., Han, D., Lu, X., Sun, Z., Zhou, A., Yin, Q., Zeng, H., Liu, M., Jiang, X., Xie, W., et al. (2015) · Nature Methods · doi:10.1038/nmeth.3569 · Cited by 153
Potential functional roles of DNA demethylation intermediates
Song, C.-X., & He, C. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.07.003 · Cited by 154
Etchegaray, J., Chávez, L., Huang, Y., Ross, K. N., Choi, J., Martínez-Pastor, B., Walsh, R. M., Sommer, C., Lienhard, M., Gladden, A. D., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3147 · Cited by 158
Nucleic acid modifications with epigenetic significance
Fu, Y., & He, C. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.10.002 · Cited by 149
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Wang, F., Yang, Y., Lin, X., Wang, J.-Q., Yong-sheng, W., Xie, W., Wang, D., Zhu, S., Liao, Y.-Q., Sun, Q., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt214 · Cited by 155
EGR1 recruits TET1 to shape the brain methylome during development and upon neuronal activity
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Myeloid malignancies: mutations, models and management
Murati, A., Brecqueville, M., Devillier, R., Mozziconacci, J., Gelsi‐Boyer, V., & Birnbaum, D. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-304 · Cited by 163
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Teif, V. B., Beshnova, D. A., Vainshtein, Y., Marth, C., Mallm, J., Höfer, T., & Rippe, K. (2014) · Genome Research · doi:10.1101/gr.164418.113 · Cited by 154
Molecular Mechanisms of Arsenic-Induced Disruption of DNA Repair
Tam, L. M., Price, N. E., & Wang, Y. (2020) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00464 · Cited by 157
ChromID identifies the protein interactome at chromatin marks
Villaseñor, R., Pfaendler, R., Ambrosi, C. M., Butz, S., Giuliani, S., Bryan, E., Sheahan, T. W., Gable, A. L., Schmolka, N., Manzo, M., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-020-0434-2 · Cited by 145
Zhang, Q., Liu, X., Gao, W., Li, P., Hou, J., Li, J., & Wong, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.524140 · Cited by 156
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Diverse epigenetic strategies interact to control epidermal differentiation
Mulder, K. W., Wang, X., Escriu, C., Ito, Y., Schwarz, R. F., Gillis, J., Sirokmány, G., Donati, G., Uribe‐Lewis, S., Pavlidis, P., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2520 · Cited by 149
Epigenetic regulation of epithelial–mesenchymal transition
Sun, L., & Fang, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2303-1 · Cited by 149
Breathing-in epigenetic change with vitamin C
Monfort, A., & Wutz, A. (2013) · The EMBO Reports · doi:10.1038/embor.2013.29 · Cited by 140
Epigenetic regulation of smooth muscle cell plasticity
Liu, R., Leslie, K. L., & Martin, K. A. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.06.004 · Cited by 142
Asmar, F., Punj, V., Christensen, J. F., Pedersen, M. T., Pedersen, A., Nielsen, A. B., Hother, C. E., Ralfkiær, U., Brown, P. D. N., Ralfkiaer, E. M., et al. (2013) · Haematologica · doi:10.3324/haematol.2013.088740 · Cited by 147
Self-citationTargeting the nucleotide salvage factor DNPH1 sensitizes BRCA -deficient cells to PARP inhibitors
Fugger, K., Bajrami, I., dos Santos, M. S., Young, S. J., Kunzelmann, S., Kelly, G. P., Hewitt, G., Patel, H., Goldstone, R. J., Carell, T., et al. (2021) · Science · doi:10.1126/science.abb4542 · Cited by 141
Dnmt3a restrains mast cell inflammatory responses
Leoni, C., Montagner, S., Rinaldi, A., Bertoni, F., Polletti, S., Balestrieri, C., & Monticelli, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616420114 · Cited by 138
Jiang, L., Wang, J., Wang, K., Wang, H., Wu, Q., Yang, C., Yu, Y., Ni, P., Zhong, Y., Song, Z., et al. (2021) · Blood · doi:10.1182/blood.2020008986 · Cited by 138
Kelly, R. D. W., Chandru, A., Watson, P. J., Song, Y., Blades, M., Robertson, N. S., Jamieson, A. G., Schwabe, J. W. R., & Cowley, S. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-32927-9 · Cited by 138
Epigenetic memory of environmental organisms: A reflection of lifetime stressor exposures
Mirbahai, L., & Chipman, J. K. (2013) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2013.10.003 · Cited by 147
Jin, S.-G., Zhang, Z.-M., Dunwell, T. L., Harter, M. R., Wu, X., Johnson, J., Li, Z., Liu, J., Szabó, P. E., Lu, Q., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.044 · Cited by 138
Silencing of endogenous retroviruses: when and why do histone marks predominate?
Leung, D., & Lorincz, M. C. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.006 · Cited by 140
miR-22 has a potent anti-tumour role with therapeutic potential in acute myeloid leukaemia
Jiang, X., Hu, C., Arnovitz, S., Bugno, J., Yu, M., Zuo, Z., Chen, P., Huang, H., Ulrich, B. C., Gurbuxani, S. K., et al. (2016) · Nature Communications · doi:10.1038/ncomms11452 · Cited by 143
Epigenomics and Interindividual Differences in Drug Response
Ivanov, M., Kacevska, M., & Ingelman‐Sundberg, M. (2012) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2012.152 · Cited by 139
Okashita, N., Kumaki, Y., Ebi, K., Nishi, M., Okamoto, Y., Nakayama, M., Hashimoto, S., Nakamura, T., Sugasawa, K., Kojima, N., et al. (2013) · Development · doi:10.1242/dev.099622 · Cited by 134
Bauer, C., Göbel, K., Nagaraj, N., Colantuoni, C., Wang, M., Müller, U., Kremmer, E., Rottach, A., & Leonhardt, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.605881 · Cited by 144
Transcriptional repressors: multifaceted regulators of gene expression
Reynolds, N., O’Shaughnessy, A., & Hendrich, B. (2013) · Development · doi:10.1242/dev.083105 · Cited by 139
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Metadata
- Authors
- Williams, K., Christensen, J., Pedersen, M. T., Johansen, J. V., Cloos, P. A. C., Rappsilber, J., & Helin, K.
- Affiliations
- University of Copenhagen (DK)
- Wellcome Centre for Cell Biology (GB)
- Corresponding author
- Helin, Kristian
- ORCID
- Venue
- Nature
- Published
- 2011-04-13
- Volume
- 473
- Issue
- 7347
- Pages
- 343-348
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3408592
- OpenAlex
- W2014623973
- Cited by
- 1,021
- References
- 30
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 29 · 2023: 37 · 2022: 44 · 2021: 57 · 2020: 49 · 2019: 55 · 2018: 63 · 2017: 65 · 2016: 87 · 2015: 72 · 2014: 108 · 2013: 125 · 2012: 114
- FWCI
- 53.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (084229)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic Syndromes and Imprinting
- Keywords
- TET1, 5-hydroxymethylcytosine, DNA demethylation, transcription start sites, transcriptional repression, mouse embryonic stem cells, TET enzymes, genome-wide binding sites
- MeSH terms
- DNA (Cytosine-5-)-Methyltransferase 1, Animals, Cell Line, Cytosine, DNA (Cytosine-5-)-Methyltransferases, DNA-Binding Proteins, Protein Binding, Proto-Oncogene Proteins, Repressor Proteins, Transcription, Genetic, Down-Regulation, CpG Islands, DNA Methylation, Transcription Initiation Site, 5-Methylcytosine, Mice, Embryonic Stem Cells, Gene Knockdown Techniques, Sin3 Histone Deacetylase and Corepressor Complex
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