TET-TDG active DNA demethylation at CpG and non-CpG sites
Open accessAbstract
In mammalian genomes, cytosine methylation occurs predominantly at CG (or CpG) dinucleotide contexts. As part of dynamic epigenetic regulation, 5-methylcytosine (mC) can be erased by active DNA demethylation, whereby ten-eleven translocation (TET) enzymes catalyze the stepwise oxidation of mC to 5-hydroxymethylcytosine (hmC), 5-formylcytosine (fC), and 5-carboxycytosine (caC), thymine DNA glycosylase (TDG) excises fC or caC, and base excision repair yields unmodified cytosine. In certain cell types, mC is also enriched at some non-CG (or CH) dinucleotides, however hmC is not. To provide biochemical context for the distribution of modified cytosines observed in biological systems, we systematically analyzed the activity of human TET2 and TDG for substrates in CG and CH contexts. We find that while TET2 oxidizes mC more efficiently in CG versus CH sites, this context preference can be diminished for hmC oxidation. Remarkably, TDG excision of fC and caC is only modestly dependent on CG context, contrasting its strong context dependence for thymine excision. We show that collaborative TET-TDG oxidation-excision activity is only marginally reduced for CA versus CG contexts. Our findings demonstrate that the TET-TDG-mediated demethylation pathway is not limited to CG sites and suggest a rationale for the depletion of hmCH in genomes rich in mCH.
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Extensive active demethylation following neuronal activity through the Tet-TDG pathway-associated base excision repair can be a source of DNA breaks.
“extensive active demethylation following neuronal activity through the Tet-TDG pathway-associated base excision repair can also be a source of DNA breaks”
From Neuronal DNA double-strand breaks lead to genome structural variations and 3D genome disruption in neurodegeneration (2023) · cites this paper as [13]
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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 · see citing works
Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451 · see citing works
Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA
He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776 · see citing works
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 · see citing works
TET enzymes, TDG and the dynamics of DNA demethylation
Kohli, R. M., & Zhang, Y. (2013) · Nature · doi:10.1038/nature12750 · Cited by 1,623 · see citing works
Li, R., Liang, J., Ni, S., Zhou, T., Qing, X., Li, H., He, W., Chen, J., Li, F., Zhuang, Q., et al. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.04.014 · Cited by 1,129 · see citing works
Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives
Spruijt, C. G., Gnerlich, F., Smits, A. H., Pfaffeneder, T., Jansen, P. W. T. C., Bauer, C., Münzel, M., Wagner, M., Müller, M., Khan, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.004 · Cited by 973 · see citing works
Tissue Distribution of 5-Hydroxymethylcytosine and Search for Active Demethylation Intermediates
Globisch, D., Münzel, M., Müller, M., Michalakis, S., Wagner, M., Koch, S., Brückl, T., Biel, M., & Carell, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015367 · Cited by 865 · see citing works
Thymine DNA Glycosylase Can Rapidly Excise 5-Formylcytosine and 5-Carboxylcytosine
Maiti, A., & Drohat, A. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.284620 · Cited by 825 · see citing works
5-Hydroxymethylcytosine is a predominantly stable DNA modification
Bachman, M., Uribe‐Lewis, S., Yang, X., Williams, M., Murrell, A., & Balasubramanian, S. (2014) · Nature Chemistry · doi:10.1038/nchem.2064 · Cited by 554 · see citing works
The Discovery of 5‐Formylcytosine in Embryonic Stem Cell DNA
Pfaffeneder, T., Hackner, B., Truß, M., Münzel, M., Müller, M., Deiml, C. A., Hagemeier, C., & Carell, T. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201103899 · Cited by 483 · see citing works
Crystal Structure of TET2-DNA Complex: Insight into TET-Mediated 5mC Oxidation
Hu, L., Li, Z., Cheng, J., Rao, Q., Gong, W., Liu, M., Shi, Y. G., Zhu, J., Wang, P., & Xu, Y. (2013) · Cell · doi:10.1016/j.cell.2013.11.020 · Cited by 448 · see citing works
CpG and non-CpG methylation in epigenetic gene regulation and brain function
Jang, H., Shin, W., Lee, J., & Do, J. (2017) · Genes · doi:10.3390/genes8060148 · Cited by 427 · see citing works
Modulation of TET2 expression and 5-methylcytosine oxidation by the CXXC domain protein IDAX
Ko, M., An, J., Bandukwala, H. S., Chávez, L., Äijö, T., Pastor, W. A., Segal, M., Li, H., Koh, K. P., Lähdesmäki, H. J., et al. (2013) · Nature · doi:10.1038/nature12052 · Cited by 385 · see citing works
Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA
Zhang, L., Lu, X., Lu, J., Liang, H., Dai, Q., Xu, G., Luo, C., Jiang, H., & He, C. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.914 · Cited by 299 · see citing works
Structural insight into substrate preference for TET-mediated oxidation
Hu, L., Lu, J., Cheng, J., Rao, Q., Li, Z., Hou, H., Lou, Z., Zhang, L., Li, W., Gong, W., et al. (2015) · Nature · doi:10.1038/nature15713 · Cited by 276 · see citing works
Tet-assisted bisulfite sequencing of 5-hydroxymethylcytosine
Yu, M., Hon, G. C., Szulwach, K. E., Song, C., Jin, P., Ren, B., & He, C. (2012) · Nature Protocols · doi:10.1038/nprot.2012.137 · Cited by 250 · see citing works
Kinde, B., Gabel, H. W., Gilbert, C. S., Griffith, E. C., & Greenberg, M. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411269112 · Cited by 236 · see citing works
Weber, A. R., Krawczyk, C., Robertson, A. B., Kuśnierczyk, A., Vågbø, C. B., Schuermann, D., Klungland, A., & Schär, P. (2016) · Nature Communications · doi:10.1038/ncomms10806 · Cited by 233 · see citing works
Nondestructive, base-resolution sequencing of 5-hydroxymethylcytosine using a DNA deaminase
Schutsky, E. K., DeNizio, J. E., Hu, P., Liu, M. Y., Nabel, C. S., Fabyanic, E. B., Hwang, Y., Bushman, F. D., Wu, H., & Kohli, R. M. (2018) · Nature Biotechnology · doi:10.1038/nbt.4204 · Cited by 228 · see citing works
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 176 · see citing works
Wu, H., Wu, X., Shen, L., & Zhang, Y. (2014) · Nature Biotechnology · doi:10.1038/nbt.3073 · Cited by 152 · see citing works
Mellén, M., Ayata, P., & Heintz, N. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708044114 · Cited by 151 · see citing works
Hashimoto, H., Hong, S., Bhagwat, A. S., Zhang, X., & Cheng, X. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks845 · Cited by 147 · see citing works
Regulation and Function of Cdt1; A Key Factor in Cell Proliferation and Genome Stability
Pozo, P. N., & Cook, J. G. (2016) · Genes · doi:10.3390/genes8010002 · Cited by 123 · see citing works
Excision of 5-Halogenated Uracils by Human Thymine DNA Glycosylase
Morgan, M. T., Bennett, M. T., & Drohat, A. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704253200 · Cited by 100 · see citing works
Mammalian Non-CpG Methylation: Stem Cells and Beyond
Pinney, S. E. (2014) · Biology · doi:10.3390/biology3040739 · Cited by 97 · see citing works
Sun, Z., Dai, N., Borgaro, J. G., Quimby, A., Sun, D., Junior, I. R. C., Zheng, Y., Zhu, Z., & Guan, S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.035 · Cited by 84 · see citing works
Mutations along a TET2 active site scaffold stall oxidation at 5-hydroxymethylcytosine
Liu, M. Y., Torabifard, H., Crawford, D. J., DeNizio, J. E., Cao, X.-J., Garcia, B. A., Cisneros, G. A., & Kohli, R. M. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2250 · Cited by 82 · see citing works
Tet2 Catalyzes Stepwise 5-Methylcytosine Oxidation by an Iterative and de novo Mechanism
Crawford, D. J., Liu, M. Y., Nabel, C. S., Cao, X.-J., Garcia, B. A., & Kohli, R. M. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10554 · Cited by 68 · see citing works
Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues
Coey, C. T., Malik, S. S., Pidugu, L. S. M., Varney, K. M., Pozharski, E. V., & Drohat, A. C. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw768 · Cited by 64 · see citing works
Maiti, A., Morgan, M. T., & Drohat, A. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.062356 · Cited by 56 · see citing works
Tamanaha, E., Guan, S., Marks, K., & Saleh, L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03243 · Cited by 56 · see citing works
Pais, J. E., Dai, N., Tamanaha, E., Vaisvila, R., Fomenkov, A. I., Bitinaite, J., Sun, Z., Guan, S., Junior, I. R. C., Noren, C. J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417939112 · Cited by 55 · see citing works
Stoichiometry and affinity for thymine DNA glycosylase binding to specific and nonspecific DNA
Morgan, M. T., Maiti, A., Fitzgerald, M. E., & Drohat, A. C. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1164 · Cited by 50 · see citing works
Selectivity and Promiscuity in TET-Mediated Oxidation of 5-Methylcytosine in DNA and RNA
DeNizio, J. E., Liu, M. Y., Leddin, E. M., Cisneros, G. A., & Kohli, R. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00912 · Cited by 49 · see citing works
Structural Basis for Excision of 5-Formylcytosine by Thymine DNA Glycosylase
Pidugu, L. S. M., Flowers, J. W., Coey, C. T., Pozharski, E. V., Greenberg, M. M., & Drohat, A. C. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00982 · Cited by 48 · see citing works
Insight into wild-type and T1372E TET2-mediated 5hmC oxidation using ab initio QM/MM calculations
Torabifard, H., & Cisneros, G. A. (2018) · Chemical Science · doi:10.1039/c8sc02961j · Cited by 43 · see citing works
Quantification of Oxidized 5-Methylcytosine Bases and TET Enzyme Activity
Liu, M. Y., DeNizio, J. E., & Kohli, R. M. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.12.006 · Cited by 42 · see citing works
Defining the Role of Nucleotide Flipping in Enzyme Specificity Using 19F NMR
Dow, B. J., Malik, S. S., & Drohat, A. C. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b00146 · Cited by 38 · see citing works
Seiler, C. L., Fernandez, J. A., Koerperich, Z. M., Andersen, M. P., Kotandeniya, D., Nguyen, M. E., Sham, Y. Y., & Tretyakova, N. Y. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00683 · Cited by 32 · see citing works
Excision of 5-Carboxylcytosine by Thymine DNA Glycosylase
Pidugu, L. S. M., Dai, Q., Malik, S. S., Pozharski, E. V., & Drohat, A. C. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10376 · Cited by 32 · see citing works
A computational investigation on the substrate preference of ten-eleven-translocation 2 (TET2)
Lu, J., Hu, L., Cheng, J., Fang, D., Wang, C., Yu, K., Jiang, H., Cui, Q., Xu, Y., & Luo, C. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp07266b · Cited by 31 · see citing works
Ghanty, U., DeNizio, J. E., Liu, M. Y., & Kohli, R. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b04722 · Cited by 27 · see citing works
Ghanty, U., Wang, T., & Kohli, R. M. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202002751 · Cited by 21 · see citing works
Defining the impact of sumoylation on substrate binding and catalysis by thymine DNA glycosylase
Coey, C. T., & Drohat, A. C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky278 · Cited by 18 · see citing works
Kizaki, S., Chandran, A., & Sugiyama, H. (2015) · ChemBioChem · doi:10.1002/cbic.201500646 · Cited by 4 · see citing works
Flagged first, then by citations
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Sorted by citations
Chromatin accessibility: biological functions, molecular mechanisms and therapeutic application
Chen, Y., Liang, R., Li, Y., Jiang, L., Ma, D., Luo, Q., & Song, G. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02030-9 · Cited by 174 · see citing works
Dileep, V., Boix, C. A., Mathys, H., Marco, A., Welch, G. M., Meharena, H. S., Loon, A., Jeloka, R., Peng, Z., Bennett, D. A., et al. (2023) · Cell · doi:10.1016/j.cell.2023.08.038 · Cited by 130 · see citing works
“Consistent with the observations in CK-p25 mice and etoposide-treated neurons, Hi-C in P301S neurons showed a decreased number of chromatin loops and a significant decrease in TAD integrity as measured by inclusion ratio (Figures S5E and S5F; Table S1, pages 12, 13).”
BackgroundResultSimultaneous sequencing of genetic and epigenetic bases in DNA
Füllgrabe, J., Gosal, W. S., Creed, P., Liu, S., Lumby, C. K., Morley, D. J., Ost, T. W. B., Vilella, A. J., Yu, S., Bignell, H., et al. (2023) · Nature Biotechnology · doi:10.1038/s41587-022-01652-0 · Cited by 127 · see citing works
The base excision repair process: comparison between higher and lower eukaryotes
Hindi, N. N., Elsakrmy, N., & Ramotar, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03990-9 · Cited by 55 · see citing works
“Thus, TDG cooperates with TET to erase methylated cytosines at CpG, through an oxidation-excision process, and there is evidence for similar roles in non-CG regions of the genome [47].”
BackgroundAdam, S., Bräcker, J., Klingel, V., Osteresch, B., Radde, N. E., Brockmeyer, J., Bashtrykov, P., & Jeltsch, A. (2022) · Communications Biology · doi:10.1038/s42003-022-03033-4 · Cited by 31 · see citing works
“This finding could explain a discrepancy in previous reports regarding the second-best mCpX target site of TET2 following mCpG. Hu et al. (2013) reported a preference for mCpC20 while DeNizio et al. (2021) reported mCpA23.”
Result5-methylcytosine turnover: Mechanisms and therapeutic implications in cancer
Turpin, M., & Salbert, G. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.976862 · Cited by 28 · see citing works
“On the other hand, TET2 has a strong preference for mCpGs and to a lesser extent for mCpAs with a T at the +1 position as well as mCpCs with a at the +1 base (DeNizio et al., 2021).”
BackgroundTET3 epigenetically controls feeding and stress response behaviors via AGRP neurons
Xie, D., Stutz, B., Li, F., Chen, F., Lv, H., Šestan-Peša, M., Catarino, J. D. S., Gu, J., Zhao, H., Stoddard, C. E., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci162365 · Cited by 27 · see citing works
“5mC and 5hmC have been detected at both CpG and non-CpG (CpH, where H = A/C/T) dinucleotides (30, 73, 74) and can function to enhance or inhibit the binding of regulatory protein factors in a contextdependent manner (29, 30).”
Targeted DNA Demethylation: Vectors, Effectors and Perspectives
Yano, N., & Fedulov, A. V. (2023) · Biomedicines · doi:10.3390/biomedicines11051334 · Cited by 27 · see citing works
“The first half of the oxidation reactions are catalyzed by the ten-eleven translocation protein (TET) family enzymes, while the second half, removal of 5fC and 5caC, is catalyzed by thymine DNA glycosylase (TDG) [67].”
BackgroundStructure and Function of TET Enzymes
Yin, X., Hu, L., & Xu, Y. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-11454-0_10 · Cited by 23 · see citing works
Ding, J.-H., Li, G., Xiong, J., Liu, F.-L., Xie, N., Ji, T., Wang, M., Guo, X., Feng, Y., Ci, W., et al. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c00425 · Cited by 22 · see citing works
Schnable, B. L., Schaich, M. A., Roginskaya, V. Y., Leary, L. P., Weaver, T., Freudenthal, B., Drohat, A. C., & Houten, B. V. (2024) · Nature Communications · doi:10.1038/s41467-024-53497-7 · Cited by 18 · see citing works
Effects of Environmental Non-Essential Toxic Heavy Metals on Epigenetics During Development
Kurita, H., Ohuchi, K., & Inden, M. (2025) · Toxics · doi:10.3390/toxics13030167 · Cited by 19 · see citing works
“Active demethylation is performed by the TET (ten eleven translocation) enzyme, a member of the DNA hydroxylase family [12].”
Yang, S. C., Du, Cui, H., Zheng, M., He, W., Gao, X., Hu, Z. Q., Jia, S., Lu, Q., & Zhao, M. (2023) · JCI Insight · doi:10.1172/jci.insight.165546 · Cited by 16 · see citing works
“Currently, the most widely accepted DNA demethylation involves the oxidation of mC and production of 5-hydroxymethylcytosine (hmC), 5-formylcytosine, and 5-carboxylcytosine (caC) via stepwise oxidation (42, 43).”
BackgroundGuo, Y., Jiang, H., Wang, J., Li, P., Zeng, X., Zhang, T., Feng, J., Nie, R., Liu, Y., Dong, X., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1053697 · Cited by 11 · see citing works
Xiang, J., Yuhui, L., Zhang, B., Ke, K., & Li, H. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1670574 · Cited by 10 · see citing works
Watanabe, R., Nakachi, Y., Matsubara, H., Ueda, J., Ishii, T., Ukai, W., Hashimoto, E., Kasai, K., Simizu, S., Kato, T., et al. (2023) · Neuroscience Research · doi:10.1016/j.neures.2023.05.001 · Cited by 13 · see citing works
Kumar, S. H., Acharyya, S., Chouksey, A., Soni, N., Nazeer, N., & Mishra, P. K. (2024) · Reproductive Toxicology · doi:10.1016/j.reprotox.2024.108675 · Cited by 9 · see citing works
Panoramic on Epigenetics in Coronary Artery Disease and the Approach of Personalized Medicine
Bergonzini, M., Loreni, F., Lio, A., Russo, M., Saitto, G., Cammardella, A. G., Irace, L., Tramontin, C., Chello, M., Lusini, M., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11102864 · Cited by 9 · see citing works
Epigenetic regulation of epithelial–mesenchymal transition during cancer development
Yoodee, S., & Thongboonkerd, V. (2023) · International review of cytology · doi:10.1016/bs.ircmb.2023.05.007 · Cited by 5 · see citing works
Wu, D., Huang, K., Shi, J., Liu, S., Wang, W., Jiang, J., Ren, H., Chen, T., Ye, S., Chen, J., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00554 · Cited by 3 · see citing works
Kong, X., Gu, H., Zhang, Y., Meng, Q., Li, Q., Song, K., Li, Y., Liu, K., Liu, Z., Hu, R., et al. (2025) · Advanced Science · doi:10.1002/advs.202505077 · Cited by 3 · see citing works
Erlitzki, N., & Kohli, R. M. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4051-7_17 · Cited by 3 · see citing works
A critique of the hypothesis that CA repeats are primary targets of neuronal MeCP2
Chhatbar, K., Connelly, J. C., Webb, S., Kriaučionis, S., & Bird, A. P. (2022) · Life Science Alliance · doi:10.26508/lsa.202201522 · Cited by 3 · see citing works
“This is presumably attributable to the strong preference of Tet enzymes for mCG over mCA as a substrate for mC oxidation (Hu et al, 2015; DeNizio et al, 2021).”
Epigenetic Regulation of Production Traits in Ruminants: Implications for Breeding and Selection
Liu, H., Qumu, M., Lu, Y., Li, K., Qian, Y., Sheng, Z., Shi, J., Xi, D., & Wu, J. (2026) · Biology · doi:10.3390/biology15050416 · Cited by 2 · see citing works
“…mediated by the ten-eleven translocation (TET1/2/3) enzymes, which iteratively oxidize 5mC to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5-carboxylcytosine (5caC), followed by thymine DNA glycosylase (TDG)-dependent base excision repair to restore unmethylated cytosines [20].”
Kinetic Analysis of the Effect of N-Terminal Acetylation on Thymine DNA Glycosylase
Tarantino, M. E., & Delaney, S. (2022) · Biochemistry · doi:10.1021/acs.biochem.1c00823 · Cited by 2 · see citing works
Characterizing the excision of 7,8-dihydro-8-oxoadenine by thymine DNA glycosylase
Servius, H. W., & Drohat, A. C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110363 · Cited by 1 · see citing works
Cadet, J., & Wagner, J. R. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1636255 · Cited by 1 · see citing works
Demethylation of Non-CpG Sites in DNA Is Initiated by TET2 5-Methylcytosine Dioxygenase
Dey, A. S., Bhattacharya, C., Guan, Y., Jha, B. K., & Mukherji, M. (2021) · DNA · doi:10.3390/dna1010004 · Cited by 1 · see citing works
“[36], that TDG can excise fC and caC in CpH contexts [36,40], which may allow the replacement of these modified cytosine bases with cytosine.”
BackgroundResultEpigenetics of Memory Processes
Pulya, S., & Ghosh, B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91909-8.00018-9 · Cited by 1 · see citing works
Li, S., Hu, D., Mei, X., Kinkpe, L., Wang, S., Wei, J., Hou, S., ZHANG, Y., & Wang, X. (2026) · Microbiology Spectrum · doi:10.1128/spectrum.00565-26
“This mark can be actively modified through oxidation by ten-eleven translocation enzymes, yielding 5-hydroxymethylcytosine (5hmC) and other intermediates in a dynamic demethylation pathway (14, 15).”
Espinosa, K., Ding, X., Servius, H. W., Pidugu, L. S. M., Lee, J. K., & Drohat, A. C. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113446
“21, 76, 77).”
Erlitzki, N., Loo, C. E., Fowler, J. M., Zhou, W., & Kohli, R. M. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag956
“Prior biochemical studies on the intrinsic substrate preferences of TET in vitro have offered a view into the enzymatic properties that contribute to gene regulation in the more complex in vivo setting [ 17 , 18 , 28 , 39 , 52 ].”
- Authors
- DeNizio, J. E., Dow, B. J., Serrano, J. C., Ghanty, U., Drohat, A. C., & Kohli, R. M.
- Affiliations
- University of Maryland, Baltimore (US)
- University of Pennsylvania (US)
- Corresponding author
- Drohat, Alexander C.
- Kohli, Rahul M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 433
- Issue
- 8
- Pages
- 166877
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC8005466
- OpenAlex
- W3127372781
- Cited by
- 32
- References
- 47
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 8 · 2021: 2
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (DGE-1321851)
- National Institutes of Health (F31-CA254260, R01-GM072711, R01-GM118501, R01-HG010646, R35-GM136225, T32-GM007229, T32-GM071339)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- active DNA demethylation, TET2, thymine DNA glycosylase, 5-methylcytosine, 5-hydroxymethylcytosine, 5-formylcytosine, 5-carboxycytosine, non-CG methylation, base excision repair, epigenetic regulation, cytosine methylation
- MeSH terms
- DNA Demethylation, Cytosine, DNA Repair, DNA-Binding Proteins, Humans, Oxidation-Reduction, Proto-Oncogene Proteins, CpG Islands, Epigenesis, Genetic, Thymine DNA Glycosylase, 5-Methylcytosine, Dioxygenases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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