Cited by 328Epigenetics and DNA MethylationGenomics and Chromatin DynamicsCancer-related gene regulation

The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.

H3K27 Demethylases, at Long Last

Open access

Swigut, Tomek, Wysocka, Joanna·2007·Cell

DOI 10.1016/j.cell.2007.09.026

Open this paper in CoChat — free account Open PDF

Abstract

Methylation of lysine 27 on histone H3 (H3K27me) by the Polycomb complex (PRC2) proteins is associated with gene silencing in many developmental processes. A cluster of recent papers (Agger et al., 2007; De Santa et al., 2007; Lan et al., 2007; Lee et al., 2007) identify the JmjC-domain proteins UTX and JMJD3 as H3K27-specific demethylases that remove this methyl mark, enabling the activation of genes involved in animal body patterning and the inflammatory response.

Integrity signals

Registry

Crossref · 10.1016/j.cell.2007.09.026

Cites

18 of 18 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
Generation of germline-competent induced pluripotent stem cells
Okita, K., Ichisaka, T., & Yamanaka, S. (2007) · Nature · doi:10.1038/nature05934 · Cited by 4,438
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
In vitro reprogramming of fibroblasts into a pluripotent ES-cell-like state
Wernig, M., Meissner, A., Foreman, R. K., Brambrink, T., Ku, M., Hochedlinger, K., Bernstein, B., & Jaenisch, R. (2007) · Nature · doi:10.1038/nature05944 · Cited by 2,732
The Mammalian Epigenome
Bernstein, B. E., Meissner, A., & Lander, E. S. (2007) · Cell · doi:10.1016/j.cell.2007.01.033 · Cited by 2,086
Genome Regulation by Polycomb and Trithorax Proteins
Schuettengruber, B., Chourrout, D., Vervoort, M., Leblanc, B., & Cavalli, G. (2007) · Cell · doi:10.1016/j.cell.2007.02.009 · Cited by 1,418
UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
Agger, K., Cloos, P. A., Christensen, J. F., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Canaani, E., Salcini, A. E., & Helin, K. (2007) · Nature · doi:10.1038/nature06145 · Cited by 1,392
Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
Ruthenburg, A. J., Allis, C. D., & Wysocka, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.014 · Cited by 1,147
Self-citation
The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., & Natoli, G. (2007) · Cell · doi:10.1016/j.cell.2007.08.019 · Cited by 965
Regulation of histone methylation by demethylimination and demethylation
Klose, R. J., & Zhang, Y. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2143 · Cited by 922

Flagged first, then by citations

Show all 18 references

Research works printed but not linked: 4

Agger, 2007, Nature
De Santa, 2007, Cell
Lan, 2007, Nature
Lee, 2007, Science

Sorted by citations

The Polycomb complex PRC2 and its mark in life
Margueron, R., & Reinberg, D. (2011) · Nature · doi:10.1038/nature09784 · Cited by 3,347
Modification of Enhancer Chromatin: What, How, and Why?
Calo, E., & Wysocka, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.038 · Cited by 1,457
Self-citation
De Novo Gene Disruptions in Children on the Autistic Spectrum
Iossifov, I., Ronemus, M., Levy, D., Wang, Z., Hakker, I., Rosenbaum, J., Yamrom, B., Lee, Y.-H., Narzisi, G., Leotta, A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.04.009 · Cited by 1,446
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,476
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,039
Regulation of epithelial-mesenchymal transition through epigenetic and post-translational modifications
Serrano-Gomez, S. J., Maziveyi, M., & Alahari, S. K. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0502-x · Cited by 817
The Adult Ventricular–Subventricular Zone (V-SVZ) and Olfactory Bulb (OB) Neurogenesis
Lim, D. A., & Alvarez-Buylla, A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018820 · Cited by 571
Epigenetic regulation of brain region-specific microglia clearance activity
Ayata, P., Badimon, A., Strasburger, H. J., Duff, M. K., Montgomery, S. E., Loh, Y.-H. E., Ebert, A., Pimenova, A. A., Ramirez, B. R., Chan, A. T., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0192-3 · Cited by 460
Recruitment of Polycomb group complexes and their role in the dynamic regulation of cell fate choice
Schuettengruber, B., & Cavalli, G. (2009) · Development · doi:10.1242/dev.033902 · Cited by 443
Chromatin remodelling factor Mll1 is essential for neurogenesis from postnatal neural stem cells
Lim, D. A., Huang, Y.-C., Swigut, T., Mirick, A. L., García‐Verdugo, J. M., Wysocka, J., Ernst, P., & Álvarez-Buylla, A. (2009) · Nature · doi:10.1038/nature07726 · Cited by 390
Self-citation
SRSF2 mutations in 275 cases with chronic myelomonocytic leukemia (CMML)
Meggendorfer, M., Roller, A., Haferlach, T., Eder, C., Dicker, F., Grossmann, V., Kohlmann, A., Alpermann, T., Yoshida, K., Ogawa, S., et al. (2012) · Blood · doi:10.1182/blood-2012-01-404863 · Cited by 309
The role of histone modifications: from neurodevelopment to neurodiseases
Park, J., Lee, K., Kim, K., & Yi, S.-J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01078-9 · Cited by 333
The Polycomb Group Protein Regulatory Network
Mozgová, I., & Hennig, L. (2015) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043014-115627 · Cited by 317
Polycomb complexes and epigenetic states
Schwartz, Y. B., & Pirrotta, V. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.002 · Cited by 302
Diversity of Polycomb group complexes in plants: same rules, different players?
Hennig, L., & Derkacheva, M. (2009) · Trends in Genetics · doi:10.1016/j.tig.2009.07.002 · Cited by 272
Targeting TGF-β signaling for the treatment of fibrosis
Györfi, A., Matei, A., & Distler, J. H. W. (2018) · Matrix Biology · doi:10.1016/j.matbio.2017.12.016 · Cited by 283
Control of differentiation in a self-renewing mammalian tissue by the histone demethylase JMJD3Preprint
Sen, G. L., Webster, D. E., Barragan, D. I., Chang, H. Y., & Khavari, P. A. (2008) · Genes & Development · doi:10.1101/gad.1673508 · Cited by 268
Histone demethylase UTX-1 regulates C. elegans life span by targeting the insulin/IGF-1 signaling pathway
Jin, C., Li, J., Green, C. D., Yu, X., Tang, X., Han, D., Xian, B., Wang, D., Huang, X., Cao, X., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.001 · Cited by 258
Biochemical mechanisms of gene regulation by polycomb group protein complexes
Müller, J., & Verrijzer, C. P. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.03.001 · Cited by 262
A UTX-MLL4-p300 Transcriptional Regulatory Network Coordinately Shapes Active Enhancer Landscapes for Eliciting Transcription
Wang, S., Tang, Z., Chen, C.-W. D., Shimada, M., Koche, R. P., Wang, L.-H., Nakadai, T., Chramiec, A. G., Krivtsov, A. V., Armstrong, S. A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.028 · Cited by 249
Hypoxia induces a novel signature of chromatin modifications and global repression of transcription
Johnson, A. B., Denko, N., & Barton, M. C. (2008) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2008.01.001 · Cited by 250
Comparative Analysis of JmjC Domain‐containing Proteins Reveals the Potential Histone Demethylases in Arabidopsis and Rice
Lu, F., Li, G., Cui, X., Liu, C., Wang, X., & Cao, X. (2008) · Journal of Integrative Plant Biology · doi:10.1111/j.1744-7909.2008.00692.x · Cited by 247
Polycomb Group Proteins Set the Stage for Early Lineage Commitment
Surface, L. E., Thornton, S. R., & Boyer, L. A. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.08.004 · Cited by 241
The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and HYPB/Setd2-mediated histone H3K36 methylationPreprint
Yoh, S. M., Lucas, J., & Jones, K. A. (2008) · Genes & Development · doi:10.1101/gad.1720008 · Cited by 258
UTX regulates mesoderm differentiation of embryonic stem cells independent of H3K27 demethylase activity
Wang, C., Lee, J., Cho, Y., Xiao, Y., Jin, Q., Liu, C., & Ge, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204166109 · Cited by 219
Dynamic protein methylation in chromatin biology
Ng, S. S., Yue, W. W., Oppermann, U. C. T., & Klose, R. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8303-z · Cited by 250
Polycomb repressive complex 2 (PRC2) silences genes responsible for neurodegeneration
von Schimmelmann, M., Feinberg, P. A., Sullivan, J. M., Ku, S. M., Badimon, A., Duff, M. K., Wang, Z., Lachmann, A., Dewell, S., Ma'ayan, A., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4360 · Cited by 225
X-linked H3K27me3 demethylase Utx is required for embryonic development in a sex-specific manner
Welstead, G. G., Creyghton, M. P., Bilodeau, S., Cheng, A. W., Markoulaki, S., Young, R. A., & Jaenisch, R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210787109 · Cited by 194
Chromatin Regulatory Mechanisms in Pluripotency
Lessard, J. A., & Crabtree, G. R. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-051809-102012 · Cited by 185
Structurally Designed trans-2-Phenylcyclopropylamine Derivatives Potently Inhibit Histone Demethylase LSD1/KDM1,,
Mimasu, S., Umezawa, N., Sato, S., Higuchi, T., Umehara, T., & Yokoyama, S. (2010) · Biochemistry · doi:10.1021/bi100299r · Cited by 179
KDM6B/JMJD3 Histone Demethylase Is Induced by Vitamin D and Modulates Its Effects in Colon Cancer Cells
Pereira, F., Barbáchano, A., Silva, J., Bonilla, F., Campbell, M. J., Muñoz, A., & Larriba, M. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr399 · Cited by 177
Histone Demethylase KDM6B Promotes Epithelial-Mesenchymal Transition
Ramadoss, S., Chen, X., & Wang, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424903 · Cited by 171
Unraveling Epigenetic Regulation in Embryonic Stem Cells
Bibikova, M. V., Laurent, L. C., Ren, B., Loring, J. F., & Fan, J. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.01.005 · Cited by 171
A cultured affair: HSV latency and reactivation in neurons
Wilson, A. C., & Mohr, I. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.08.005 · Cited by 174
UTX Mutations in Human Cancer
Wang, L., & Shilatifard, A. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.001 · Cited by 165
Repression of BMI1 in normal and leukemic human CD34+ cells impairs self-renewal and induces apoptosis
Rizo, A., Olthof, S. G. M., Han, L., Vellenga, E., de Haan, G., & Schuringa, J. J. (2009) · Blood · doi:10.1182/blood-2009-03-209734 · Cited by 170
Mitochondrial regulation of epigenetics and its role in human diseases
Minocherhomji, S., Tollefsbol, T. O., & Singh, K. K. (2012) · Epigenetics · doi:10.4161/epi.19547 · Cited by 151
TPO-Induced Metabolic Reprogramming Drives Liver Metastasis of Colorectal Cancer CD110+ Tumor-Initiating Cells
Wu, Z., Wei, D., Gao, W., Xu, Y., Hu, Z., Ma, Z., Gao, C., Zhu, X., & Li, Q. (2015) · Cell Stem Cell · doi:10.1016/j.stem.2015.05.016 · Cited by 149
JMJD3 as an epigenetic regulator in development and disease
Burchfield, J. S., Li, Q., Wang, H. Y., & Wang, R. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.07.006 · Cited by 160
Direct activation of human and mouse Oct4 genes using engineered TALE and Cas9 transcription factors
Hu, J., Lei, Y., Wong, W.-K., Liu, S., Lee, K.-C., He, X., You, W., Zhou, R., Guo, J., Chen, X., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku109 · Cited by 145
Proteomic analysis of blastema formation in regenerating axolotl limbs
Rao, N., Jhamb, D., Milner, D. J., Li, B., Song, F., Wang, M., Voss, S. R., Palakal, M. J., King, M. W., Saranjami, B., et al. (2009) · BMC Biology · doi:10.1186/1741-7007-7-83 · Cited by 139
Genistein downregulates onco-miR-1260b and upregulates sFRP1 and Smad4 via demethylation and histone modification in prostate cancer cells
Hirata, H., Hinoda, Y., Shahryari, V., Deng, G., Tanaka, Y., Tabatabai, Z. L., & Dahiya, R. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.48 · Cited by 141
Drosophila Kismet Regulates Histone H3 Lysine 27 Methylation and Early Elongation by RNA Polymerase II
Srinivasan, S., Dorighi, K. M., & Tamkun, J. W. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000217 · Cited by 134
Histone Methylation Regulator PTIP Is Required for PPARγ and C/EBPα Expression and Adipogenesis
Cho, Y.-W., Hong, S., Jin, Q., Wang, L., Lee, J., Gavrilova, O., & Ge, K. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.05.010 · Cited by 136
X and Y Chromosome Complement Influence Adiposity and Metabolism in Mice
Chen, X., McClusky, R., Itoh, Y., Reue, K., & Arnold, A. P. (2013) · Endocrinology · doi:10.1210/en.2012-2098 · Cited by 133
Epithelial Cell Adhesion Molecule Regulation Is Associated with the Maintenance of the Undifferentiated Phenotype of Human Embryonic Stem Cells
Lu, T., Lu, R., Liao, M., Yu, J., Chung, C.-H., Kao, C.-F., & Wu, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.077081 · Cited by 136
Histone H3K27 methyltransferase EZH2 and demethylase JMJD3 regulate hepatic stellate cells activation and liver fibrosis
Jiang, Y., Xiang, C., Zhong, F., Zhang, Y., Wang, L., Zhao, Y., Wang, J., Ding, C., Li, J., He, F., et al. (2020) · Theranostics · doi:10.7150/thno.46360 · Cited by 124
JMJD3 in the regulation of human diseases
Zhang, X., Liu, L., Yuan, X., Wei, Y., & Wei, X. (2019) · Protein & Cell · doi:10.1007/s13238-019-0653-9 · Cited by 123
An Epigenetic Role of Mitochondria in Cancer
Liu, Y., Chen, C., Wang, X., Sun, Y., Zhang, J., Chen, J., & Shi, Y. (2022) · Cells · doi:10.3390/cells11162518 · Cited by 131
A histone demethylase is necessary for regeneration in zebrafish
Stewart, S., Tsun, Z.-Y., & Belmonte, J. C. I. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904132106 · Cited by 127
Interpretation of Developmental Signaling at Chromatin: The Polycomb Perspective
Sawarkar, R., & Paro, R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.012 · Cited by 119
Histone H1 Variants Are Differentially Expressed and Incorporated into Chromatin during Differentiation and Reprogramming to Pluripotency
Terme, J.-M., Sesé, B., Millán-Ariño, L., Mayor, R., Belmonte, J. C. I., Barrero, M. J., & Jordan, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.281923 · Cited by 117
Dynamics of histone H3 lysine 27 trimethylation in plant development
Zheng, B., & Chen, X. (2011) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2011.01.001 · Cited by 114
Molecular mechanisms of maternal cannabis and cigarette use on human neurodevelopment
Morris, C. V., DiNieri, J. A., Szutorisz, H., & Hurd, Y. L. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07884.x · Cited by 113
Epigenetic Control of the Invasion-promoting MT1-MMP/MMP-2/TIMP-2 Axis in Cancer Cells
Chernov, A. V., Sounni, N. E., Remacle, A. G., & Strongin, A. Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900273200 · Cited by 108
Evidence for Alteration of EZH2, BMI1, and KDM6A and Epigenetic Reprogramming in Human Papillomavirus Type 16 E6/E7-Expressing Keratinocytes
Hyland, P. L., McDade, S. S., McCloskey, R., Dickson, G. J., Arthur, K., McCance, D. J., & Patel, D. (2011) · Journal of Virology · doi:10.1128/jvi.00160-11 · Cited by 112
EZH2: Not EZHY (Easy) to Deal
Deb, G., Singh, A. K., & Gupta, S. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0546 · Cited by 110
Histone deacetylase inhibition accelerates the early events of stem cell differentiation: transcriptomic and epigenetic analysis
Karantzali, E., Schulz, H., Hummel, O., Hübner, N., Hatzopoulos, A., & Kretsovali, A. (2008) · Genome biology · doi:10.1186/gb-2008-9-4-r65 · Cited by 107
Phosphorylation of H3S10 Blocks the Access of H3K9 by Specific Antibodies and Histone Methyltransferase
Duan, Q., Chen, H., Costa, M., & Dai, W. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803312200 · Cited by 103
A Simple Calixarene Recognizes Post‐translationally Methylated Lysine
Beshara, C. S., Jones, C. E., Daze, K. D., Lilgert, B. J., & Hof, F. A. (2009) · ChemBioChem · doi:10.1002/cbic.200900633 · Cited by 97
Epigenetic regulation of drug metabolism and transport
Peng, L., & Zhong, X. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.01.007 · Cited by 96
The C. elegans H3K27 Demethylase UTX-1 Is Essential for Normal Development, Independent of Its Enzymatic Activity
Vandamme, J., Lettier, G., Sidoli, S., Schiavi, E. D., Jensen, O. N., & Salcini, A. E. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002647 · Cited by 94
Histone H3K27 Demethylase JMJD3 in Cooperation with NF-κB Regulates Keratinocyte Wound Healing
Na, J., Lee, K., Na, W., Shin, J.-Y., Lee, M.-J., Yune, T. Y., Lee, H., Jung, H.-S., Kim, W., & Ju, B. (2016) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2015.11.029 · Cited by 96
H3K27 demethylation by JMJD3 at a poised enhancer of anti‐apoptotic gene BCL2 determines ERα ligand dependency
Svotelis, A., Bianco, S., Madore, J., Huppé, G., Nordell-Markovits, A., Mes‐Masson, A., & Gévry, N. Y. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.284 · Cited by 98
Mechanisms of thyroid hormone receptor action during development: Lessons from amphibian studies
Grimaldi, A. G., Buisine, N., Miller, T. C. R., Shi, Y., & Sachs, L. M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.04.020 · Cited by 95
Polycomb gene expression and histone H3 lysine 27 trimethylation changes during bovine preimplantation development
Ross, P. J., Ragina, N. P., Rodríguez, R. M. A., Iager, A. E., Siripattarapravat, K., Lopez-Corrales, N. L., & Cibelli, J. B. (2008) · Reproduction · doi:10.1530/rep-08-0045 · Cited by 92
Inhibited expression of hematopoietic progenitor kinase 1 associated with loss of jumonji domain containing 3 promoter binding contributes to autoimmunity in systemic lupus erythematosus
Zhang, Q., Long, H., Liao, J., Zhao, M., Liang, G., Wu, X., Zhang, P., Ding, S., Luo, S., & Lu, Q. (2011) · Journal of Autoimmunity · doi:10.1016/j.jaut.2011.09.006 · Cited by 90
Epigenetic regulation in neural crest development
Hu, N., Strobl‐Mazzulla, P. H., & Bronner-Fraser, M. E. (2014) · Developmental Biology · doi:10.1016/j.ydbio.2014.09.034 · Cited by 95
Hypoxia increases genome-wide bivalent epigenetic marking by specific gain of H3K27me3
Prickaerts, P., Adriaens, M. E., van den Beucken, T., Koch, E., Dubois, L. J., Dahlmans, V. E. H., Gits, C. M. M., Evelo, C. T., Chan‐Seng‐Yue, M., Wouters, B. G., et al. (2016) · Epigenetics & Chromatin · doi:10.1186/s13072-016-0086-0 · Cited by 91
Emerging Roles of JmjC Domain-Containing Proteins
Accari, S. L., & Fisher, P. R. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.003 · Cited by 87
A new role for histone demethylases in the maintenance of plant genome integrity
Antúnez-Sánchez, J., Naish, M., Ramirez-Prado, J. S., Ohno, S., Huang, Y., Dawson, A., Opassathian, K., Manza-Mianza, D., Ariel, F., Raynaud, C., et al. (2020) · eLife · doi:10.7554/elife.58533 · Cited by 82
Proteomic Analysis of Mouse Oocytes Reveals 28 Candidate Factors of the “Reprogrammome”
Pfeiffer, M. J., Siatkowski, M., Paudel, Y., Balbach, S. T., Baeumer, N., Crosetto, N., Drexler, H. C. A., Fuellen, G., & Boiani, M. (2011) · Journal of Proteome Research · doi:10.1021/pr100706k · Cited by 84
Expression and significance of histone H3K27 demethylases in renal cell carcinoma
Shen, Y., Guo, X., Wang, Y., Qiu, W., Chang, Y., Zhang, A., & Duan, X. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-470 · Cited by 86
Cystathionine-γ-lyase ameliorates the histone demethylase JMJD3-mediated autoimmune response in rheumatoid arthritis
Wu, W., Qin, M., Jia, W., Huang, Z., Li, Z., Yang, D., Huang, M., Xiao, C., Long, F., Mao, J., et al. (2018) · Cellular and Molecular Immunology · doi:10.1038/s41423-018-0037-8 · Cited by 80
Breast Cancer Cells Induce Stromal Fibroblasts to Secrete ADAMTS1 for Cancer Invasion through an Epigenetic Change
Tyan, S., Hsu, C.-H., Peng, K.-L., Chen, C.-C., Kuo, W., Lee, E. Y.-H. P., Shew, J., Chang, K., Juan, L., & Lee, W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035128 · Cited by 80
Immune mechanisms in cerebral ischemic tolerance
García‐Bonilla, L., Benakis, C., Moore, J. M. R., Iadecola, C., & Anrather, J. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00044 · Cited by 86
Dynamic Patterns of Histone Methylation Are Associated with Ontogenic Expression of the Cyp3a Genes during Mouse Liver Maturation
Li, Y., Cui, Y., Hart, S. N., Klaassen, C. D., & Zhong, X. (2009) · Molecular Pharmacology · doi:10.1124/mol.108.052993 · Cited by 79
SUZ12 Promotes Human Epithelial Ovarian Cancer by Suppressing Apoptosis via Silencing HRK
Li, H., Cai, Q. K., Wu, H. G., Vathipadiekal, V., Dobbin, Z. C., Li, T., Xiang, H., Landen, C. N., Birrer, M. J., Sánchez‐Beato, M., et al. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0335 · Cited by 80
Yin Yang 1 Regulates the Expression of Snail through a Distal Enhancer
Palmer, M. B., Majumder, P., Cooper, J. C., Yoon, H., Wade, P. A., & Boss, J. M. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0229 · Cited by 75
The role and prospect of JMJD3 in stem cells and cancer
Yin, X., Yang, S., Zhang, M., & Yue, Y. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109384 · Cited by 70
Stretching the limits: Stem cells in regeneration science
Stocum, D. L., & Zupanc, G. K. H. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21774 · Cited by 70
Epigenetic regulation of matrix metalloproteinases and their collagen substrates in cancer
Chernov, A. V., & Strongin, A. Y. (2011) · bmc · doi:10.1515/bmc.2011.017 · Cited by 69
Ultrasensitive gene regulation by positive feedback loops in nucleosome modification
Sneppen, K., Micheelsen, M. A., & Dodd, I. B. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.21 · Cited by 69
Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes
Kim, D., Tang, Z., Shimada, M., Fierz, B., Houck-Loomis, B. R., Bar‐Dagan, M., Lee, S., Lee, S., Muir, T. W., Roeder, R. G., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00601-13 · Cited by 68
Therapeutic potential of inhibiting histone 3 lysine 27 demethylases: a review of the literature
Abu‐Hanna, J., Patel, J. A., Anastasakis, E., Cohen, R., Clapp, L. H., Loizidou, M., & Eddama, M. M. R. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01305-8 · Cited by 72
Epigenetic transcriptional repression of cellular genes by a viral SET protein
Mujtaba, S., Manzur, K. L., Gurnon, J. R., Kang, M., Etten, J. L. V., & Zhou, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1772 · Cited by 66
The Epigenetics of Suicide: Explaining the Biological Effects of Early Life Environmental Adversity
Labonté, B., & Turecki, G. (2010) · Archives of Suicide Research · doi:10.1080/13811118.2010.524025 · Cited by 75
Polycomb proteins in mammalian cell differentiation and plasticity
Prezioso, C., & Orlando, V. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.062 · Cited by 67
JMJD3 facilitates C/EBPβ-centered transcriptional program to exert oncorepressor activity in AML
Yu, S., Zhu, K.-Y., Chen, J., Liu, X.-Z., Xu, P., Zhang, W., Li, Y., Guo, H., & Zhu, J. (2018) · Nature Communications · doi:10.1038/s41467-018-05548-z · Cited by 63
The histone demethylase Jumonji domain-containing protein 3 (JMJD3) regulates fibroblast activation in systemic sclerosis
Bergmann, C., Brandt, A., Merlevede, B., Hallenberger, L., Dees, C., Wohlfahrt, T., Pötter, S., Zhang, Y., Chen, C.-W., Mallano, T., et al. (2018) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2017-211501 · Cited by 62
Molecular mechanism of Jmjd3‐mediated interleukin‐6 gene regulation in endothelial cells underlying spinal cord injury
Lee, K., Na, W., Lee, J. Y., Na, J., Cho, H., Wu, H., Yune, T. Y., Kim, W., & Ju, B. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07786.x · Cited by 62
Molecular basis for substrate recognition by lysine methyltransferases and demethylases
Rizzo, P. A. D., & Trievel, R. C. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.06.008 · Cited by 61
EED and KDM6B Coordinate the First Mammalian Cell Lineage Commitment To Ensure Embryo Implantation
Saha, B., Home, P., Ray, S. S., Larson, M. A., Paul, A., Rajendran, G., Behr, B. R., & Paul, S. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00069-13 · Cited by 60
KDM6B is an androgen regulated gene and plays oncogenic roles by demethylating H3K27me3 at cyclin D1 promoter in prostate cancer
Cao, Z., Shi, X., Tian, F., Yu, F., Wu, B. J., Mrđenović, S., Nian, X., Ji, J., Xu, H., Chen, K., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03354-4 · Cited by 60
UTX coordinates steroid hormone-mediated autophagy and cell death
Denton, D., Aung-Htut, M. T., Lorensuhewa, N., Nicolson, S., Zhu, W., Mills, K., Cakouros, D., Bergmann, A., & Kumar, S. (2013) · Nature Communications · doi:10.1038/ncomms3916 · Cited by 58
Specific Histone Lysine 4 Methylation Patterns Define TR-Binding Capacity and Differentiate Direct T3 Responses
Bilesimo, P., Jolivet, P., Alfama, G., Buisine, N., Mével, S. L., Havis, E., DEMENEIX, B. A., & Sachs, L. M. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0269 · Cited by 61
Methylation and demethylation activities of a C. elegans MLL-like complex attenuate RAS signalling
Fisher, K., Southall, S. M., Wilson, J. R., & Poulin, G. B. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.02.023 · Cited by 59
Epigenetic regulation of Nanog expression by Ezh2 in pluripotent stem cells
Villasante, A., Piazzolla, D., Li, H., Goméz-López, G., Djabali, M., & Serrano, M. (2011) · Cell Cycle · doi:10.4161/cc.10.9.15658 · Cited by 57
Female Bias in Rhox6 and 9 Regulation by the Histone Demethylase KDM6A
Berletch, J. B., Deng, X., Nguyen, D. K., & Distèche, C. M. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003489 · Cited by 57
ASXL2 promotes proliferation of breast cancer cells by linking ERα to histone methylation
Park, U.-H., Kang, M.-R., Kim, E.-J., Kwon, Y.-S., Hur, W., Yoon, S. K., Song, B.-J., Park, J. H., Hwang, J.-T., Jeong, J.-C., et al. (2015) · Oncogene · doi:10.1038/onc.2015.443 · Cited by 53

Authors: Swigut, T., & Wysocka, J.
Affiliations: Stanford Medicine (US)
Corresponding author: Wysocka, Joanna
ORCID: Swigut, Tomek
Wysocka, Joanna
Venue: Cell
Publisher: Elsevier BV
Published: 2007-10
Volume: 131
Issue: 1
Pages: 29-32
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2007.09.026
OpenAlex: W1971180847
Cited by: 327
References: 18
Citations by year: 2026: 7 · 2025: 10 · 2024: 15 · 2023: 11 · 2022: 19 · 2021: 21 · 2020: 15 · 2019: 18 · 2018: 17 · 2017: 12 · 2016: 17 · 2015: 20 · 2014: 19 · 2013: 18 · 2012: 26
FWCI: 8.21
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2116 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
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 › Molecular Biology › Cancer-related gene regulation
Keywords: H3K27 demethylase, H3K27 methylation, polycomb repressive complex 2, JmjC domain proteins, KDM6A, JMJD3, histone demethylation, gene silencing, gene activation, body patterning, inflammation
MeSH terms: Animals, Gene Expression Regulation, Immune System, Methylation, Oxidoreductases, N-Demethylating, Repressor Proteins, Homeodomain Proteins, Body Patterning, Gene Silencing, Epigenesis, Genetic, Jumonji Domain-Containing Histone Demethylases, Polycomb-Group Proteins

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

H3K27 Demethylases, at Long Last

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks