Tet2 and Tet3 cooperate with B-lineage transcription factors to regulate DNA modification and chromatin accessibility
Open accessAbstract
Ten-eleven translocation (TET) enzymes oxidize 5-methylcytosine, facilitating DNA demethylation and generating new epigenetic marks. Here we show that concomitant loss of Tet2 and Tet3 in mice at early B cell stage blocked the pro- to pre-B cell transition in the bone marrow, decreased Irf4 expression and impaired the germline transcription and rearrangement of the Igκ locus. Tet2/3-deficient pro-B cells showed increased CpG methylation at the Igκ 3’ and distal enhancers that was mimicked by depletion of E2A or PU.1, as well as a global decrease in chromatin accessibility at enhancers. Importantly, re-expression of the Tet2 catalytic domain in Tet2/3-deficient B cells resulted in demethylation of the Igκ enhancers and restored their chromatin accessibility. Our data suggest that TET proteins and lineage-specific transcription factors cooperate to influence chromatin accessibility and Igκ enhancer function by modulating the modification status of DNA.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
PU.1 can physically interact with the myeloid master transcription factor.
“which can physically interact with the myeloid master transcription factor (TF; Supplementary Fig. S5K and S5L; ref. 34).”
From PU.1-Dependent Enhancer Inhibition Separates <i>Tet2</i> -Deficient Hematopoiesis from Malignant Transformation (2022) · cites this paper as [34]
The Results section (‘Functional and physical interaction between TET proteins and E2A/PU.1’; page unavailable) reports a direct interaction between TET2 and PU.1. The Discussion identifies PU.1 as a key transcription factor in the myeloid lineage. The paper does not establish the claim as phrased—that PU.1 interacts with a separate myeloid master transcription factor. (LLM, conf=0.84)
Experimental — accuracy not yet measuredTet2 binds and governs site-specific DNA demethylation upon being recruited to chromatin by DNA-binding transcription factors, such as RUNX1 or PU.1.
“Tet2 binds and governs site-specific DNA demethylation upon being recruited to the chromatin by DNA-binding TF, such as RUNX1 (51) or PU.1 (34)”
From PU.1-Dependent Enhancer Inhibition Separates <i>Tet2</i> -Deficient Hematopoiesis from Malignant Transformation (2022) · cites this paper as [34]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400 · see citing works
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072 · see citing works
Heinz, S., Benner, C., Spann, N., Bertolino, E., Lin, Y. C., Laslo, P., Cheng, J. X., Murre, C., Singh, H., & Glass, C. K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.004 · Cited by 13,382 · see citing works
deepTools2: a next generation web server for deep-sequencing data analysis
Ramírez, F., Ryan, D. P., Grüning, B., Bhardwaj, V., Kilpert, F., Richter, A. S., Heyne, S., Dündar, F., & Manke, T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw257 · Cited by 8,096 · see citing works
Buenrostro, J. D., Giresi, P. G., Zaba, L. C., Chang, H. Y., & Greenleaf, W. J. (2013) · Nature Methods · doi:10.1038/nmeth.2688 · Cited by 6,422 · see citing works
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
Self-citationHistone H3K27ac separates active from poised enhancers and predicts developmental state
Creyghton, M. P., Cheng, A. W., Welstead, G. G., Kooistra, T., Carey, B. W., Steine, E. J., Hanna, J., Lodato, M. A., Frampton, G. M., Sharp, P. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016071107 · Cited by 4,302 · 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 accessible chromatin landscape of the human genome
Thurman, R. E., Rynes, E., Humbert, R., Vierstra, J., Maurano, M. T., Haugen, E., Sheffield, N. C., Stergachis, A. B., Wang, H., Vernot, B., et al. (2012) · Nature · doi:10.1038/nature11232 · Cited by 2,679 · see citing works
Genomic DNA methylation: the mark and its mediators.
Klose, R. J., & Bird, A. P. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.12.008 · Cited by 2,501 · see citing works
Function and information content of DNA methylation
Schübeler, D. (2015) · Nature · doi:10.1038/nature14192 · Cited by 2,060 · see citing works
Victora, G. D., & Nussenzweig, M. C. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075032 · Cited by 1,878 · see citing works
Charting a dynamic DNA methylation landscape of the human genome
Ziller, M. J., Gu, H., Müller, F., Donaghey, J., Tsai, L. T.-Y., Kohlbacher, O., De Jager, P. L., Rosen, E. D., Bennett, D. A., Bernstein, B. E., et al. (2013) · Nature · doi:10.1038/nature12433 · Cited by 1,357 · see citing works
Transcriptional enhancers: from properties to genome-wide predictions
Shlyueva, D., Stampfel, G., & Stark, A. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3682 · Cited by 1,356 · see citing works
Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
Ko, M., Huang, Y., Jankowska, A. M., Pape, U. J., Tahiliani, M., Bandukwala, H. S., An, J., Lamperti, E. D., Koh, K. P., Ganetzky, R. D., et al. (2010) · Nature · doi:10.1038/nature09586 · Cited by 1,294 · see citing works
Self-citationInsulator dysfunction and oncogene activation in IDH mutant gliomas
Flavahan, W. A., Drier, Y., Liau, B. B., Gillespie, S. M., Venteicher, A. S., Stemmer-Rachamimov, A. O., Suvà, M. L., & Bernstein, B. E. (2016) · Nature · doi:10.1038/nature16490 · Cited by 1,288 · cited 4× · see citing works
“Notably, consistent with a previous study (Benner et al., 2015), a fraction of the commonly accessible regions (especially those with the lowest ATAC-seq signals) corresponded to regions with significant CTCF binding in pro-B cells (Lin et al., 2010), suggesting these regions are potent insulators (Song et al., 2011).”
BackgroundInfluentialBSMAP: whole genome bisulfite sequence MAPping program
Xi, Y., & Li, W. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-232 · Cited by 1,216 · see citing works
The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes
Gu, T., Guo, F., Yang, H., Wu, H.-P., Xu, G., Liu, W., Xie, Z.-G., Shi, L., He, X., Jin, S., et al. (2011) · Nature · doi:10.1038/nature10443 · Cited by 1,144 · see citing works
Reversing DNA Methylation: Mechanisms, Genomics, and Biological Functions
Wu, H., & Zhang, Y. (2014) · Cell · doi:10.1016/j.cell.2013.12.019 · Cited by 1,065 · 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
MeCP2 binds to 5hmC enriched within active genes and accessible chromatin in the nervous system
Mellén, M., Ayata, P., Dewell, S., Kriaucionis, S., & Heintz, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.022 · Cited by 943 · see citing works
TETonic shift: biological roles of TET proteins in DNA demethylation and transcription
Pastor, W. A., Aravind, L., & Rao, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3589 · Cited by 897 · cited 8× · see citing works
“, 2013); subsequently, proteins of the TET dioxygenase family oxidise 5mC to 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC)(He et al., 2011; Ito et al., 2011; Pastor et al., 2013; Tahiliani et al., 2009).”
BackgroundInfluentialSelf-citationThe Transcription Factor NFAT Promotes Exhaustion of Activated CD8 + T Cells
Martinez, G. J., Pereira, R. M., Äijö, T., Kim, E. Y., Marangoni, F., Pipkin, M. E., Togher, S., Heissmeyer, V., Zhang, Y. C., Crotty, S., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.01.006 · Cited by 857 · cited 1× · see citing works
“To knockdown E2A and PU.1 in WT BCR-ABL transformed pre-B cells, cells were transduced overnight with lentivirus generated from pLKO.1 based shRNAs, including shScramble, shE2A-1, shE2A2, shPU.1–1, and shPU.1–2 similar to previously described (Martinez et al., 2015).”
MethodSelf-citationGenome-wide mapping of 5-hydroxymethylcytosine in embryonic stem cells
Pastor, W. A., Pape, U. J., Huang, Y., Henderson, H. R., Lister, R., Ko, M., McLoughlin, E. M., Brudno, Y., Mahapatra, S., Kapranov, P., et al. (2011) · Nature · doi:10.1038/nature10102 · Cited by 804 · see citing works
Self-citationKoh, K. P., Yabuuchi, A., Rao, S., Huang, Y., Cunniff, K., Nardone, J., Laiho, A., Tahiliani, M., Sommer, C. A., Mostoslavsky, G., et al. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.01.008 · Cited by 776 · see citing works
Self-citationThe Behaviour of 5-Hydroxymethylcytosine in Bisulfite Sequencing
Huang, Y., Pastor, W., Shen, Y.-H., Tahiliani, M., Liu, D. R., & Rao, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008888 · Cited by 755 · see citing works
Self-citationPax5: the guardian of B cell identity and function
Cobaleda, C., Schebesta, A., Delogu, A., & Busslinger, M. (2007) · Nature Immunology · doi:10.1038/ni1454 · Cited by 697 · see citing works
Developmentally controlled and tissue-specific expression of unrearranged VH gene segments
Yancopoulos, G. D. (1985) · Cell · doi:10.1016/0092-8674(85)90141-2 · Cited by 696 · see citing works
Failure of B-cell differentiation in mice lacking the transcription factor EBF
Lin, H., & Grosschedl, R. (1995) · Nature · doi:10.1038/376263a0 · Cited by 692 · see citing works
Ghisletti, S., Barozzi, I., Mietton, F., Polletti, S., De Santa, F., Venturini, E., Gregory, L., Lonie, L., Chew, A., Wei, C.-L., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.02.008 · Cited by 666 · see citing works
Ko, M., Bandukwala, H. S., An, J., Lamperti, E. D., Thompson, E. C., Hastie, R., Tsangaratou, A., Rajewsky, K., Koralov, S. B., & Rao, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112317108 · Cited by 616 · see citing works
Self-citationTesting gene function early in the B cell lineage in mb1-cre mice
Hobeika, E., Thiemann, S., Storch, B., Jumaa, H., Nielsen, P. J., Pelanda, R., & Reth, M. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605944103 · Cited by 581 · see citing works
Survival of Resting Mature B Lymphocytes Depends on BCR Signaling via the Igα/β Heterodimer
Kraus, M., Alimzhanov, M. B., Rajewsky, N., & Rajewsky, K. (2004) · Cell · doi:10.1016/j.cell.2004.05.014 · Cited by 573 · see citing works
Genome-wide Profiling of 5-Formylcytosine Reveals Its Roles in Epigenetic Priming
Song, C., Szulwach, K. E., Dai, Q., Fu, Y., Mao, S.-Q., Lin, L., Street, C., Li, Y., Poidevin, M., Wu, H., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.001 · Cited by 545 · see citing works
Lin, Y. C., Jhunjhunwala, S., Benner, C. W., Heinz, S., Welinder, E., Månsson, R., Sigvardsson, M., Hagman, J. R., Espinoza, C. A., Dutkowski, J., et al. (2010) · Nature Immunology · doi:10.1038/ni.1891 · Cited by 502 · see citing works
Song, L., Zhang, Z., Grasfeder, L. L., Boyle, A. P., Giresi, P. G., Lee, B.-K., Sheffield, N. C., Gräf, S., Huss, M., Keefe, D., et al. (2011) · Genome Research · doi:10.1101/gr.121541.111 · Cited by 500 · see citing works
Genome-wide Analysis Reveals TET- and TDG-Dependent 5-Methylcytosine Oxidation Dynamics
Shen, L., Wu, H., Diep, D., Yamaguchi, S., D’Alessio, A. C., Fung, H.-L., Zhang, K., & Zhang, Y. (2013) · Cell · doi:10.1016/j.cell.2013.04.002 · Cited by 497 · see citing works
Mechanisms of Programmed DNA Lesions and Genomic Instability in the Immune System
Alt, F. W., Zhang, Y., Meng, F., Guo, C., & Schwer, B. (2013) · Cell · doi:10.1016/j.cell.2013.01.007 · Cited by 477 · see citing works
BS-Seeker2: a versatile aligning pipeline for bisulfite sequencing data
Guo, W., Fiziev, P. P., Yan, W., Cokus, S. J., Sun, X., Zhang, M. Q., Chen, P., & Pellegrini, M. A. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-774 · Cited by 422 · see citing works
Song, Q., Decato, B. E., Hong, E. E., Zhou, M., Fang, F., Qu, J., Garvin, T. H., Kessler, M. D., Zhou, J., & Smith, A. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081148 · Cited by 415 · 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
Self-citationMeCP2 binds to 5hmc enriched within active genes and accessible chromatin in the nervous system
Mellén, M., Ayata, P., Dewell, S. B., Kriaučionis, S., & Heintz, N. (2013) · Epigenetics & Chromatin · doi:10.1186/1756-8935-6-s1-p52 · Cited by 345 · see citing works
Clark, M. R., Mandal, M., Ochiai, K., & Singh, H. (2013) · Nature reviews. Immunology · doi:10.1038/nri3570 · Cited by 337 · see citing works
Hon, G. C., Song, C., Du, T., Jin, F., Selvaraj, S., Lee, A. Y., Yen, C., Ye, Z., Mao, S.-Q., Wang, B.-A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.026 · Cited by 332 · see citing works
Whole-genome fingerprint of the DNA methylome during human B cell differentiation
Kulis, M., Merkel, A., Heath, S. C., Queirós, A. C., Schuyler, R. P., Castellano, G., Beekman, R., Raineri, E., Esteve‐Codina, A., Clot, G., et al. (2015) · Nature Genetics · doi:10.1038/ng.3291 · Cited by 329 · see citing works
Lienhard, M., Grimm, C., Morkel, M., Herwig, R., & Chávez, L. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt650 · Cited by 328 · see citing works
Helix-loop-helix proteins and lymphocyte development
Murre, C. (2005) · Nature Immunology · doi:10.1038/ni1260 · Cited by 319 · see citing works
Hodges, E., Molaro, A., dos Santos, C. O., Thekkat, P. U., Song, Q., Uren, P. J., Park, J., Butler, J., Rafii, S., McCombie, W., et al. (2011) · Molecules and Cells · doi:10.1016/j.molcel.2011.08.026 · Cited by 304 · see citing works
WT1 Recruits TET2 to Regulate Its Target Gene Expression and Suppress Leukemia Cell Proliferation
Wang, Y., Xiao, M., Chen, X., Chen, L., Xu, Y., Lv, L., Wang, P., Yang, H., Ma, S., Lin, H., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.023 · Cited by 304 · see citing works
IRF-4,8 orchestrate the pre-B-to-B transition in lymphocyte developmentPreprint
Lu, R., Medina, K. L., Lancki, D. W., & Singh, H. (2003) · Genes & Development · doi:10.1101/gad.1104803 · Cited by 275 · see citing works
Connections between TET proteins and aberrant DNA modification in cancer
Huang, Y., & Rao, A. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.07.005 · Cited by 264 · see citing works
Self-citationMammalian cytosine methylation at a glance
Ooi, S. K. T., O’Donnell‐Luria, A., & Bestor, T. H. (2009) · Journal of Cell Science · doi:10.1242/jcs.015123 · Cited by 241 · see citing works
Notes on the role of dynamic DNA methylation in mammalian development
Bestor, T. H., Edwards, J. R., & Boulard, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415301111 · Cited by 238 · see citing works
TET1 is a tumor suppressor of hematopoietic malignancy
Cimmino, L., Dawlaty, M. M., Ndiaye‐Lobry, D., Yap, Y. S., Bakogianni, S., Yu, Y., Bhattacharyya, S., Shaknovich, R., Geng, H., Lobry, C., et al. (2015) · Nature Immunology · doi:10.1038/ni.3148 · Cited by 228 · see citing works
de la Rica, L., Rodríguez-Ubreva, J., García, M., Islam, A. B., Urquiza, J. M., Hernando, H., Christensen, J., Helin, K., Gómez-Vaquero, C., & Ballestar, E. (2013) · Genome Biology · doi:10.1186/gb-2013-14-9-r99 · Cited by 211 · see citing works
Acute loss of TET function results in aggressive myeloid cancer in mice
An, J., González‐Avalos, E., Chawla, A., Jeong, M., López-Moyado, I. F., Li, W., Goodell, M. A., Chávez, L., Ko, M., & Rao, A. (2015) · Nature Communications · doi:10.1038/ncomms10071 · Cited by 204 · see citing works
Self-citationTET proteins and 5‐methylcytosine oxidation in hematological cancers
Ko, M., An, J., Pastor, W. A., Koralov, S. B., Rajewsky, K., & Rao, A. (2014) · Immunological Reviews · doi:10.1111/imr.12239 · Cited by 197 · see citing works
Self-citationMeta-analysis of IDH-mutant cancers identifies EBF1 as an interaction partner for TET2
Guilhamon, P., Eskandarpour, M., Halai, D., Wilson, G. A., Feber, A., Teschendorff, A. E., Gómez, V., Hergovich, A., Tirabosco, R., Amary, F. M., et al. (2013) · Nature Communications · doi:10.1038/ncomms3166 · Cited by 169 · see citing works
Muljo, S. A., & Schlissel, M. S. (2002) · Nature Immunology · doi:10.1038/ni870 · Cited by 164 · see citing works
TET proteins regulate the lineage specification and TCR-mediated expansion of iNKT cells
Tsagaratou, A., González-Avalos, E., Rautio, S., Scott-Browne, J. P., Togher, S., Pastor, W. A., Rothenberg, E. V., Chavez, L., Lähdesmäki, H., & Rao, A. (2017) · Nature Immunology · doi:10.1038/ni.3630 · Cited by 154 · see citing works
Self-citationBossen, C., Murre, C. S., Chang, A. N., Mansson, R., Rodewald, H.-R., & Murre, C. (2015) · Nature Immunology · doi:10.1038/ni.3170 · Cited by 144 · see citing works
An active v-abl protein tyrosine kinase blocks immunoglobulin light-chain gene rearrangement.Preprint
Chen, Y. Y., Wang, L. C., Huang, M. S., & Rosenberg, N. E. (1994) · Genes & Development · doi:10.1101/gad.8.6.688 · Cited by 133 · see citing works
Boller, S., Ramamoorthy, S., Akbas, D., Nechanitzky, R., Burger, L., Murr, R., Schübeler, D., & Grosschedl, R. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.021 · Cited by 133 · see citing works
Kang, J., Lienhard, M., Pastor, W. A., Chawla, A., Novotny, M., Tsagaratou, A., Lasken, R. S., Thompson, E. C., Surani, M. A., Koralov, S. B., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510510112 · Cited by 126 · see citing works
Self-citationInlay, M. A., Alt, F. W., Baltimore, D., & Xu, Y. (2002) · Nature Immunology · doi:10.1038/ni790 · Cited by 119 · see citing works
The GLIB technique for genome-wide mapping of 5-hydroxymethylcytosine
Pastor, W. A., Huang, Y., Henderson, H. R., Agarwal, S., & Rao, A. (2012) · Nature Protocols · doi:10.1038/nprot.2012.104 · Cited by 98 · see citing works
Self-citationTranscription factors drive B cell development
Hagman, J. R., & Lukin, K. (2006) · Current Opinion in Immunology · doi:10.1016/j.coi.2006.01.007 · Cited by 98 · see citing works
IFN Regulatory Factor 4 and 8 Promote Ig Light Chain κ Locus Activation in Pre-B Cell Development
Ma, S., Turetsky, A., Trinh, L. X., & Lu, R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7898 · Cited by 95 · see citing works
The anti-CMS technique for genome-wide mapping of 5-hydroxymethylcytosine
Huang, Y., Pastor, W. A., Zepeda-Martínez, J. A., & Rao, A. (2012) · Nature Protocols · doi:10.1038/nprot.2012.103 · Cited by 95 · see citing works
Self-citationChromatin Topology and the Regulation of Antigen Receptor Assembly
Bossen, C., Månsson, R., & Murre, C. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075003 · Cited by 92 · see citing works
Klug, C. A., Gerety, S. J., Shah, P. C., Chen, Y. Y., Rice, N. R., Rosenberg, N. E., & Singh, H. (1994) · Genes & Development · doi:10.1101/gad.8.6.678 · Cited by 79 · see citing works
Benner, C. W., Isoda, T., & Murre, C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512995112 · Cited by 64 · see citing works
Transcription‐coupled eviction of histones H2A/H2B governs V(D)J recombination
Bevington, S. L., & Boyes, J. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.42 · Cited by 50 · see citing works
Histone reader BRWD1 targets and restricts recombination to the Igk locus
Mandal, M., Hamel, K. M., Maienschein‐Cline, M., Tanaka, A., Teng, G., Tuteja, J. H., Bunker, J. J., Bahroos, N., Eppig, J. J., Schatz, D. G., et al. (2015) · Nature Immunology · doi:10.1038/ni.3249 · Cited by 45 · see citing works
BSeQC: quality control of bisulfite sequencing experiments
Lin, X., Sun, D., Rodriguez, B. A. T., Zhao, Q. C., Sun, H., Zhang, Y., & Li, W. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt548 · Cited by 45 · see citing works
Differentiation of B Lymphocytes From Hematopoietic Stem Cells
Vieira, P., & Cumano, A. (2004) · Humana Press eBooks · doi:10.1385/1-59259-796-3:067 · Cited by 42 · see citing works
V(D)J recombination is not activated by demethylation of the kappa locus
Cherry, S. R., Beard, C., Jaenisch, R., & Baltimore, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.150218497 · Cited by 40 · see citing works
Epigenetic Regulation of Monoallelic Rearrangement (Allelic Exclusion) of Antigen Receptor Genes
Levin-Klein, R., & Bergman, Y. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00625 · Cited by 31 · see citing works
The Igκ Gene Enhancers, E3′ and Ed, Are Essential for Triggering Transcription
Zhou, X., Xiang, Y., & Garrard, W. T. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1002665 · Cited by 25 · see citing works
Manoharan, A., Roure, C. D., Rolink, A. G., & Matthias, P. (2015) · European Journal of Immunology · doi:10.1002/eji.201445035 · Cited by 21 · see citing works
O-GlcNAcylation and 5-Methylcytosine Oxidation: An Unexpected Association between OGT and TETs
Balasubramani, A., & Rao, A. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.006 · Cited by 15 · see citing works
Self-citationQuantification of Jκ signal end breaks in developing B cells by blunt-end linker ligation and qPCR
Curry, J. D., Li, L., & Schlissel, M. S. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.10.003 · Cited by 5 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
TET-mediated active DNA demethylation: mechanism, function and beyond
Wu, X., & Zhang, Y. (2017) · Nature Reviews Genetics · doi:10.1038/nrg.2017.33 · Cited by 1,661 · see citing works
NR4A transcription factors limit CAR T cell function in solid tumours
Chen, J., López-Moyado, I. F., Seo, H., Lio, C.-W. J., Hempleman, L. J., Sekiya, T., Yoshimura, A., Scott-Browne, J. P., & Rao, A. (2019) · Nature · doi:10.1038/s41586-019-0985-x · Cited by 874 · see citing works
Self-citationTET (Ten-eleven translocation) family proteins: structure, biological functions and applications
Zhang, X., Zhang, Y., Wang, C., & Wang, X. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01537-x · Cited by 286 · see citing works
Vitamin C and immune cell function in inflammation and cancer
Ang, A., Pullar, J. M., Currie, M. J., & Vissers, M. C. M. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180169 · Cited by 191 · see citing works
Enhancer DNA methylation: implications for gene regulation
Angeloni, A., & Bogdanović, O. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190030 · Cited by 176 · see citing works
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 172 · see citing works
Self-citationLoss of TET2 and TET3 in regulatory T cells unleashes effector function
Yue, X., Lio, C. J., Samaniego‐Castruita, D., Li, X., & Rao, A. (2019) · Nature Communications · doi:10.1038/s41467-019-09541-y · Cited by 156 · see citing works
Self-citationDysregulation of the TET family of epigenetic regulators in lymphoid and myeloid malignancies
Lio, C. J., Yuita, H., & Rao, A. (2019) · Blood · doi:10.1182/blood.2019791475 · Cited by 146 · see citing works
Self-citationHelix–loop–helix proteins and the advent of cellular diversity: 30 years of discoveryPreprint
Murre, C. (2019) · Genes & Development · doi:10.1101/gad.320663.118 · Cited by 143 · see citing works
TET Enzymes and 5hmC in Adaptive and Innate Immune Systems
Lio, C. J., & Rao, A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00210 · Cited by 139 · see citing works
Self-citationParadoxical association of TET loss of function with genome-wide DNA hypomethylation
López-Moyado, I. F., Tsagaratou, A., Yuita, H., Seo, H., Delatte, B., Heinz, S., Benner, C. W., & Rao, A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903059116 · Cited by 125 · see citing works
Self-citationConnections Between Metabolism and Epigenetics in Programming Cellular Differentiation
Chisolm, D. A., & Weinmann, A. S. (2018) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042617-053127 · Cited by 129 · see citing works
B cell activation and plasma cell differentiation are inhibited by de novo DNA methylation
Barwick, B. G., Scharer, C. D., Martinez, R. J., Price, M. J., Wein, A. N., Haines, R. R., Bally, A. P. R., Kohlmeier, J. E., & Boss, J. M. (2018) · Nature Communications · doi:10.1038/s41467-018-04234-4 · Cited by 121 · see citing works
TET Enzymes in the Immune System: From DNA Demethylation to Immunotherapy, Inflammation, and Cancer
López-Moyado, I. F., Ko, M., Hogan, P. G., & Rao, A. (2024) · Annual Review of Immunology · doi:10.1146/annurev-immunol-080223-044610 · Cited by 116 · see citing works
Self-citationTet2 and Tet3 in B cells are required to repress CD86 and prevent autoimmunity
Tanaka, S., Ise, W., Inoue, T., Ito, A., Ono, C., Shima, Y., Sakakibara, S., Nakayama, M., Fujii, K., Miura, I., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0700-y · Cited by 96 · see citing works
Lio, C. J., Shukla, V., Samaniego‐Castruita, D., González‐Avalos, E., Chakraborty, A., Yue, X., Schatz, D. G., Ay, F., & Rao, A. (2019) · Science Immunology · doi:10.1126/sciimmunol.aau7523 · Cited by 96 · see citing works
Self-citationLi, R., Cauchy, P., Ramamoorthy, S., Boller, S., Chavez, L., & Grosschedl, R. (2018) · Genes & Development · doi:10.1101/gad.309583.117 · Cited by 86 · see citing works
Impact of constitutional TET2 haploinsufficiency on molecular and clinical phenotype in humans
Kaasinen, E., Kuismin, O., Rajamäki, K., Ristolainen, H., Aavikko, M., Kondelin, J., Saarinen, S., Berta, D. G., Katainen, R., Hirvonen, E. A. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09198-7 · Cited by 92 · see citing works
Tet2 at the interface between cancer and immunity
Jiang, S. (2020) · Communications Biology · doi:10.1038/s42003-020-01391-5 · Cited by 89 · see citing works
Barnett, K. R., Decato, B. E., Scott, T. J., Hansen, T. J., Chen, B., Attalla, J., Smith, A. D., & Hodges, E. C. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.004 · Cited by 84 · see citing works
The Role of Host Cell DNA Methylation in the Immune Response to Bacterial Infection
Qin, W., Scicluna, B. P., & van der Poll, T. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.696280 · Cited by 85 · see citing works
Shukla, V., Samaniego‐Castruita, D., Dong, Z., González‐Avalos, E., Yan, Q., Sarma, K., & Rao, A. (2021) · Nature Immunology · doi:10.1038/s41590-021-01087-w · Cited by 88 · see citing works
Self-citationFang, S.-H., Li, J., Xiao, Y., Lee, M., Guo, L., Han, W., Li, T., Hill, M. C., Hong, T.-T., Mo, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12325-z · Cited by 70 · see citing works
TET methylcytosine oxidases: new insights from a decade of research
Lio, C. J., Yue, X., López-Moyado, I. F., Tahiliani, M., Aravind, L., & Rao, A. (2020) · Journal of Biosciences · doi:10.1007/s12038-019-9973-4 · Cited by 78 · see citing works
Self-citationTET Methylcytosine Oxidases in T Cell and B Cell Development and Function
Tsagaratou, A., Lio, C. J., Yue, X., & Rao, A. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00220 · Cited by 71 · see citing works
Self-citationRoles of TET and TDG in DNA demethylation in proliferating and non-proliferating immune cells
Onodera, A., González‐Avalos, E., Lio, C. J., Georges, R. O., Bellacosa, A., Nakayama, T., & Rao, A. (2021) · Genome biology · doi:10.1186/s13059-021-02384-1 · Cited by 72 · see citing works
Self-citationSeritrakul, P., & Gross, J. M. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006987 · Cited by 72 · see citing works
Li, J., Wu, X.-W., Zhou, Y.-B., Lee, M., Guo, L., Han, W., Mo, W., Cao, W., Sun, D.-Q., Xie, R., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky063 · Cited by 67 · see citing works
Transcriptional determination and functional specificity of myeloid cells: making sense of diversity
Monticelli, S., & Natoli, G. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.51 · Cited by 62 · see citing works
Nakatsukasa, H., Oda, M., Yin, J., Chikuma, S., Ito, M., Iizuka-Koga, M., Someya, K., Kitagawa, Y., Ohkura, N., Sakaguchi, S., et al. (2019) · International Immunology · doi:10.1093/intimm/dxz008 · Cited by 64 · see citing works
Vitamin D receptor, STAT3, and TET2 cooperate to establish tolerogenesis
Català‐Moll, F., Ferreté-Bonastre, A. G., Godoy‐Tena, G., Morante-Palacios, O., Ciudad, L., Barberà, L., Fondelli, F., Martínez-Cáceres, E. M., Rodríguez‐Ubreva, J., Li, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110244 · Cited by 61 · see citing works
Molecular regulation of peripheral B cells and their progeny in immunityPreprint
Boothby, M. R., Hodges, E. C., & Thomas, J. W. (2019) · Genes & Development · doi:10.1101/gad.320192.118 · Cited by 65 · see citing works
Qi, T., Sun, M., Zhang, C., Chen, P., Xiao, C., & Chang, X. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108452 · Cited by 62 · see citing works
Self-citationTET-Mediated Epigenetic Regulation in Immune Cell Development and Disease
Tsiouplis, N. J., Bailey, D. W., Chiou, L. F., Wissink, F. J., & Tsagaratou, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.623948 · Cited by 59 · see citing works
Miyazaki, K., Watanabe, H., Yoshikawa, G., Chen, K., Hidaka, R., Aitani, Y., Osawa, K., Takeda, R., Ochi, Y., Tani‐ichi, S., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abb1455 · Cited by 61 · see citing works
Li, X., Wu, C., Shen, Y., Wang, K., Tang, L., Zhou, M., Yang, M., Pan, T., Liu, X., & Xu, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001265 · Cited by 61 · see citing works
Schoeler, K., Aufschnaiter, A., Messner, S., Derudder, E., Herzog, S., Villunger, A., Rajewsky, K., & Labi, V. (2019) · FEBS Journal · doi:10.1111/febs.14934 · Cited by 56 · see citing works
Stoyanova, E. I., Riad, M. H., Rao, A., & Heintz, N. (2021) · eLife · doi:10.7554/elife.66973 · Cited by 55 · see citing works
Self-citationRosikiewicz, W., Chen, X., Domínguez, P. M., Ghamlouch, H., Aoufouchi, S., Bernard, O., Melnick, A. M., & Li, S. (2020) · Science Advances · doi:10.1126/sciadv.aay5872 · Cited by 54 · see citing works
B-cell tumor development in Tet2-deficient mice
Mouly, E., Ghamlouch, H., Della-Valle, V., Scourzic, L., Quivoron, C., Roos‐Weil, D., Pawlikowska, P., Saada, V., Diop, M. K., Lopez, C. K., et al. (2018) · Blood Advances · doi:10.1182/bloodadvances.2017014118 · Cited by 52 · see citing works
Tet2 Inactivation Enhances the Antitumor Activity of Tumor-Infiltrating Lymphocytes
Lee, M., Li, J., Li, J., Fang, S., Zhang, J., Vo, A. T. T., Han, W., Zeng, H., Isgandarova, S., Martinez-Moczygemba, M., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3213 · Cited by 47 · see citing works
Self-citationDefining B Cell Chromatin: Lessons from EBF1.
Boller, S., Li, R., & Grosschedl, R. (2018) · Trends in Genetics · doi:10.1016/j.tig.2017.12.014 · Cited by 44 · see citing works
Reprogramming of DNA methylation at NEUROD2-bound sequences during cortical neuron differentiation
Hahn, M. A., Jin, S., Li, A. X., Liu, J., Huang, Z., Wu, X., Kim, B.-W., Johnson, J. S., Bilbao, A.-D. V., Tao, S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax0080 · Cited by 46 · see citing works
Decoding the role of TET family dioxygenases in lineage specification
Wu, X., Li, G., & Xie, R. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0228-7 · Cited by 43 · see citing works
The Role of Inflammation in the Initiation and Progression of Myeloid Neoplasms
Balandrán, J. C., Lasry, A., & Aifantis, I. (2023) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-22-0176 · Cited by 41 · see citing works
Whole-genome analysis of TET dioxygenase function in regulatory T cells
Yue, X., Samaniego‐Castruita, D., González‐Avalos, E., Li, X., Barwick, B. G., & Rao, A. (2021) · EMBO Reports · doi:10.15252/embr.202152716 · Cited by 40 · see citing works
Self-citation5-Hydroxymethylcytosine (5hmC), or How to Identify Your Favorite Cell
Ecsedi, S., Rodríguez‐Aguilera, J. R., & Hernández‐Vargas, H. (2018) · Epigenomes · doi:10.3390/epigenomes2010003 · Cited by 37 · see citing works
TET2 facilitates PPARγ agonist–mediated gene regulation and insulin sensitization in adipocytes
Bian, F., Ma, X., Villivalam, S. D., You, D., Choy, L. R., Paladugu, A., Fung, S., & Kang, S. (2018) · Metabolism · doi:10.1016/j.metabol.2018.08.006 · Cited by 37 · see citing works
Hepatic TET3 contributes to type-2 diabetes by inducing the HNF4α fetal isoform
Li, D., Cao, T., Sun, X., Jin, S., Xie, D., Huang, X., Yang, X., Carmichael, G., Taylor, H. S., Diano, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14185-z · Cited by 38 · see citing works
Dimitri, A. J., Baxter, A. E., Chen, G. M., Hopkins, C. R., Rouin, G. T., Huang, H., Kong, W., Holliday, C., Wiebking, V., Bartoszek, R. L., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp9371 · Cited by 37 · see citing works
Active DNA demethylation—The epigenetic gatekeeper of development, immunity, and cancer
Prasad, R. M., Yen, T. J., & Bellacosa, A. (2020) · Advanced Genetics · doi:10.1002/ggn2.10033 · Cited by 37 · see citing works
Epigenetic remodeling by vitamin C potentiates plasma cell differentiation
Chen, H.-Y., Almonte-Loya, A., Lay, F.-Y., Hsu, M., Johnson, E. C., González‐Avalos, E., Yin, J., Bruno, R. S., Ma, Q., Ghoneim, H. E., et al. (2022) · eLife · doi:10.7554/elife.73754 · Cited by 35 · see citing works
Self-citationCharting the dynamic epigenome during B-cell development
Martín-Subero, J. I., & Oakes, C. C. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.08.008 · Cited by 35 · see citing works
Circles of Life: linking metabolic and epigenetic cycles to immunity
Lio, C. J., & Huang, S. C. (2020) · Immunology · doi:10.1111/imm.13207 · Cited by 34 · see citing works
Self-citationRecent Advances in Lupus B Cell Biology: PI3K, IFNγ, and Chromatin
Bacalao, M. A., & Satterthwaite, A. B. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.615673 · Cited by 33 · see citing works
Mahajan, V. S., Mattoo, H., Sun, N., Viswanadham, V., Yuen, G. J., Allard‐Chamard, H., Ahmad, M., Murphy, S. J. H., Cariappa, A., Tuncay, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22458-9 · Cited by 33 · see citing works
Jiao, J., Jin, Y., Zheng, M., Zhang, H., Yuan, M., Lv, Z., Odhiambo, W. O., Yu, X., Zhang, P., Li, C., et al. (2018) · Clinical & Experimental Immunology · doi:10.1111/cei.13227 · Cited by 32 · see citing works
Peng, V., Xing, X., Bando, J. K., Tršan, T., Luccia, B. D., Collins, P. L., Li, D., Wang, W.-L., Lee, H. J., Oltz, E. M., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01164-8 · Cited by 32 · see citing works
The Role of Ten-Eleven Translocation Proteins in Inflammation
Gerecke, C., Rodrigues, C. E., Homann, T., & Kleuser, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.861351 · Cited by 36 · see citing works
The Pleiotropy of PAX5 Gene Products and Function
Nasrabadi, P. N., Martin, D., Gharib, E., & Robichaud, G. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710095 · Cited by 32 · see citing works
Epigenomic Modifications Mediating Antibody Maturation
Sheppard, E. C., Morrish, R. B., Dillon, M. J., Leyland, R., & Chahwan, R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00355 · Cited by 30 · see citing works
TET proteins in natural and induced differentiation
Scott-Browne, J. P., Lio, C. J., & Rao, A. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.07.011 · Cited by 31 · see citing works
Self-citationRole of TET dioxygenases in the regulation of both normal and pathological hematopoiesis
Joshi, K., Zhang, L., Breslin, P., Kini, A. R., & Zhang, J. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02496-x · Cited by 30 · see citing works
Self-citationMYC Regulation of D2HGDH and L2HGDH Influences the Epigenome and Epitranscriptome
Qiu, Z., Lin, A., Jiang, S., Elkashef, S. M., Myers, J., Srikantan, S., Sasi, B. K., Cao, J. Z., Godley, L. A., Rakheja, D., et al. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.02.002 · Cited by 30 · see citing works
Miyazaki, K., & Miyazaki, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.659761 · Cited by 29 · see citing works
Macrophage migration inhibitory factor is overproduced through EGR1 in TET2low resting monocytes
Pronier, E., Imanci, A., Selimoglu‐Buet, D., Badaoui, B., Itzykson, R., Roger, T., Jego, C., Naimo, A., Francillette, M., Breckler, M., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03057-w · Cited by 31 · see citing works
Byun, S., Lee, C. H., Jeong, H., Kim, H., Kwon, H. M., Park, S. H., Myung, K., An, J., & Ko, M. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205626119 · Cited by 31 · see citing works
Fujii, K., Tanaka, S., Hasegawa, T., Narazaki, M., Kumanogoh, A., Koseki, H., Kurosaki, T., & Ise, W. (2020) · International Immunology · doi:10.1093/intimm/dxaa042 · Cited by 28 · see citing works
Gregoricchio, S., Polit, L., Esposito, M., Berthelet, J., Delestré, L., Evanno, E., Diop, M., Gallais, I., Aleth, H., Poplineau, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac613 · Cited by 27 · see citing works
TET1 and 5-Hydroxymethylation Preserve the Stem Cell State of Mouse Trophoblast
Senner, C. E., Chrysanthou, S., Burge, S., Lin, H., Branco, M. R., & Hemberger, M. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.04.009 · Cited by 27 · see citing works
Role of Tet2 in Regulating Adaptive and Innate Immunity
Li, J., Li, L., Sun, X., Deng, T., Huang, G., Li, X., Xie, Z., & Zhou, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.665897 · Cited by 26 · see citing works
Dissecting TET2 Regulatory Networks in Blood Differentiation and Cancer
Lazarenkov, A., & Sardina, J. L. (2022) · Cancers · doi:10.3390/cancers14030830 · Cited by 25 · see citing works
Maher, N., Maiellaro, F., Ghanej, J., Rasi, S., Moia, R., & Gaïdano, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178132 · Cited by 25 · see citing works
Ascorbic Acid Promotes KIR Demethylation during Early NK Cell Differentiation
Wu, C., Zhang, B., Kim, H., Anderson, S. K., Miller, J. S., & Cichocki, F. M. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000212 · Cited by 24 · see citing works
TET2 mutation as prototypic clonal hematopoiesis lesion
Guarnera, L., & Jha, B. K. (2024) · Seminars in Hematology · doi:10.1053/j.seminhematol.2024.01.013 · Cited by 24 · see citing works
Engineered Split-TET2 Enzyme for Inducible Epigenetic Remodeling
Lee, M., Li, J., Liang, Y., Ma, G., Zhang, J., He, L., Liu, Y., Li, Q., Li, M., Sun, D., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b01459 · Cited by 23 · see citing works
Self-citationEpigenetic Alterations in Inborn Errors of Immunity
Romano, R., Cillo, F., Moracas, C., Pignata, L., Nannola, C., Toriello, E., Rosa, A. D., Cirillo, E., Coppola, E., Giardino, G., et al. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11051261 · Cited by 23 · see citing works
Aivalioti, M. M., Bartholdy, B. A., Pradhan, K., Bhagat, T. D., Zintiridou, A., Jeong, J. J., Thiruthuvanathan, V. J., Pujato, M., Paranjpe, A., Zhang, C., et al. (2022) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-21-0226 · Cited by 22 · see citing works
Tet Proteins Regulate Neutrophil Granulation in Zebrafish through Demethylation of socs3b mRNA
Banks, K. M., Lan, Y., & Evans, T. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108632 · Cited by 21 · see citing works
Muscle injury causes long-term changes in stem-cell DNA methylation
Michaeli, T. F., Sabag, O., Fok, R., Azria, B., Monin, J., Nevo, Y., Gielchinsky, Y., Berman, B. P., Cedar, H., & Bergman, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2212306119 · Cited by 23 · see citing works
Guerin, L. N., Scott, T. J., Yap, J. A., Johansson, A., Puddu, F., Charlesworth, T., Yang, Y., Simmons, A. J., Lau, K. S., Ihrie, R. A., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115680 · Cited by 19 · see citing works
Noncoding RNA transcription at enhancers and genome folding in cancer
Isoda, T., Morio, T., & Takagi, M. (2019) · Cancer Science · doi:10.1111/cas.14107 · Cited by 19 · see citing works
Active DNA demethylation of developmental cis -regulatory regions predates vertebrate origins
Skvortsova, K., Bertrand, S., Voronov, D., Duckett, P. E., Ross, S. E., Magri, M. S., Maeso, I., Weatheritt, R. J., Gómez-Skármeta, J. L., Arnone, M. I., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn2258 · Cited by 18 · see citing works
Yuita, H., López-Moyado, I. F., Jeong, H., Cheng, A. X., Scott-Browne, J. P., An, J., Nakayama, T., Onodera, A., Ko, M., & Rao, A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214824120 · Cited by 18 · see citing works
Self-citationNovel Discoveries in Immune Dysregulation in Inborn Errors of Immunity
Ren, A., Yin, W., Miller, H. E., Westerberg, L. S., Candotti, F., Park, C.-S., Lee, P. P. W., Gong, Q., Chen, Y., & Liu, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.725587 · Cited by 18 · see citing works
Epigenetic marks or not? The discovery of novel DNA modifications in eukaryotes
Meng, W., Wang, Z., Zhang, Y., Hou, Y., & Xue, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.106791 · Cited by 17 · see citing works
Guo, L., Hong, T., Lee, Y., Hu, X., Pan, G., Zhao, R., Yang, Y., Yang, J., Cai, X., Rivera, L., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01496-7 · Cited by 17 · see citing works
Epigenetics of the antibody and autoantibody response
Moroney, J. B., Chupp, D. P., Xu, Z., Zan, H., & Casali, P. (2020) · Current Opinion in Immunology · doi:10.1016/j.coi.2020.09.004 · Cited by 17 · see citing works
Tsagaratou, A. (2021) · Immunological Reviews · doi:10.1111/imr.12940 · Cited by 16 · see citing works
Äijö, T., Theofilatos, D., Cheng, M., Smith, M. D., Xiong, Y., Baldwin, A. S., & Tsagaratou, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940995 · Cited by 16 · see citing works
Genome-wide characterization of cytosine-specific 5-hydroxymethylation in normal breast tissue
Wilkins, O. M., Johnson, K. C., Houseman, E. A., King, J. E., Marsit, C. J., & Christensen, B. C. (2019) · Epigenetics · doi:10.1080/15592294.2019.1695332 · Cited by 15 · see citing works
Micro but mighty—Micronutrients in the epigenetic regulation of adaptive immune responses*
Chen, H., Hsu, M., & Lio, C. J. (2021) · Immunological Reviews · doi:10.1111/imr.13045 · Cited by 17 · see citing works
Self-citationThe HDAC7–TET2 epigenetic axis is essential during early B lymphocyte development
Azagra, A., Meler, A., de Barrios, O., Tomás-Daza, L., Collazo, O., Monterde, B., Obiols, M., Rovirosa, L., Vila-Casadesús, M., Cabrera-Pasadas, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac619 · Cited by 13 · see citing works
L’hématopoïèse clonale : un concept émergent à la croisée des spécialités
Danlos, F., Papo, M., & Micol, J. (2019) · La Revue de Médecine Interne · doi:10.1016/j.revmed.2019.05.005 · Cited by 14 · see citing works
Predicting gene expression state and prioritizing putative enhancers using 5hmC signal
González-Avalos, E., Onodera, A., Samaniego-Castruita, D., Rao, A., & Ay, F. (2024) · Genome Biology · doi:10.1186/s13059-024-03273-z · Cited by 13 · see citing works
Self-citationHidaka, R., Miyazaki, K., & Miyazaki, M. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.890056 · Cited by 13 · see citing works
Plasma cell generation during T-cell-dependent immune responses
Ise, W., & Kurosaki, T. (2021) · International Immunology · doi:10.1093/intimm/dxab071 · Cited by 12 · see citing works
Maity, J., Majumder, S., Pal, R., Saha, B., & Mukhopadhyay, P. K. (2023) · BioEssays · doi:10.1002/bies.202300035 · Cited by 14 · see citing works
Epigenetic regulation of inflammation by CxxC domain‐containing proteins*
Onodera, A., Kiuchi, M., Kokubo, K., & Nakayama, T. (2021) · Immunological Reviews · doi:10.1111/imr.13056 · Cited by 12 · see citing works
TET2 Regulates 5-Hydroxymethylcytosine Signature and CD4+ T-Cell Balance in Allergic Rhinitis
Tan, L., Fu, L., Zheng, L., Fan, W., Tan, H., Tao, Z., & Xu, Y. (2022) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2022.14.2.254 · Cited by 11 · see citing works
- Authors
- Lio, C.-W., Zhang, J., González-Avalos, E., Hogan, P. G., Chang, X., & Rao, A.
- Affiliations
- Division of Signaling and Gene Expression, San Diego, United States
- Shanghai Jiao Tong University (CN)
- University of California San Diego (US)
- Corresponding author
- Chang, Xing
- Rao, Anjana
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2016-11-21
- Volume
- 5
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC5142813
- OpenAlex
- W2552742463
- Cited by
- 170
- References
- 83
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 14 · 2023: 14 · 2022: 25 · 2021: 22 · 2020: 24 · 2019: 22 · 2018: 21 · 2017: 8
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Cancer Research Institute (Irvington Postdoctoral Fellowship)
- Ministry of Science and Technology of the People's Republic of China (2014CB943600)
- National Institutes of Health (AI44432, CA151535)
- Leukemia and Lymphoma Society (6187-12)
- 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 › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Keywords
- TET2, TET3, B cell development, IRF4, germline transcription, DNA demethylation, 5-methylcytosine oxidation, CpG methylation, E2A, PU.1, transcription factor cooperation, bone marrow
- MeSH terms
- Interferon Regulatory Factor-4, Animals, B-Lymphocytes, Cell Differentiation, Chromatin, DNA, DNA-Binding Proteins, Gene Expression Regulation, Proto-Oncogene Proteins, Transcription, Genetic, 5-Methylcytosine, Dioxygenases, Interferon Regulatory Factors, Mice, Gene Knockout Techniques
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 ›
Are you an author, or do you see a problem with this page? Request a review