The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A–ARF locus in response to oncogene- and stress-induced senescence
Open accessAbstract
The tumor suppressor proteins p16 INK4A and p14 ARF, encoded by the INK4A–ARF locus, are key regulators of cellular senescence. The locus is epigenetically silenced by the repressive H3K27me3 mark in normally growing cells, but becomes activated in response to oncogenic stress. Here, we show that expression of the histone H3 Lys 27 (H3K27) demethylase JMJD3 is induced upon activation of the RAS–RAF signaling pathway. JMJD3 is recruited to the INK4A–ARF locus and contributes to the transcriptional activation of p16 INK4A in human diploid fibroblasts. Additionally, inhibition of Jmjd3 expression in mouse embryonic fibroblasts results in suppression of p16 Ink4a and p19 Arf expression and in their immortalization.
Overview
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
Verification
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?
The cited source says what the claim attributes to it.
In the citing paper
“For example, oncogene activation induces the expression of the histone 3 Lys27 (H3K27) demethylase, Jumonji domain-containing D3 (JMJD3), which removes the repressive H3K27 tri-methylation marks and thereby promotes p16 expression [19].”
From The role of cellular senescence and SASP in tumour microenvironment (2023) · cites this paper as [19]
In the citing paper
“During senescence, PRC delocalization from the CDKN2A locus, transcriptional downregulation of EZH2 [83], and recruitment of JMJD3 [84,85], a histone lysine demethylase that catalyzes H3K27 demethylation, lead to removal of the repressive H3K27me3 mark at the CDKN2A locus and facilitate p16 transcription.”
From Mechanisms and Regulation of Cellular Senescence (2021) · cites this paper as [84]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mutations in the p53 gene occur in diverse human tumour types
Nigro, J. M., Baker, S. J., Preisinger, A. C., Jessup, J. M., Hosteller, R., Cleary, K. R., Signer, S. H., Davidson, N. E., Baylin, S., Devilee, P., et al. (1989) · Nature · doi:10.1038/342705a0 · Cited by 2,730
Role of the INK4a Locus in Tumor Suppression and Cell Mortality
Serrano, M., Lee, H.-W., Chin, L., Cordon-Cardo, C., Beach, D., & DePinho, R. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81079-x · Cited by 1,585
Jacobs, J. J. L., Kieboom, K., Marino, S., DePinho, R. A., & van Lohuizen, M. (1999) · Nature · doi:10.1038/16476 · Cited by 1,580
Tumor Suppression at the Mouse INK4a Locus Mediated by the Alternative Reading Frame Product p19
Kamijo, T., Zindy, F., Roussel, M. F., Quelle, D. E., Downing, J. R., Ashmun, R. A., Grosveld, G., & Sherr, C. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80452-3 · Cited by 1,566
Reverse engineering of regulatory networks in human B cells
Basso, K., Margolin, A. A., Stolovitzky, G. A., Klein, U., Dalla‐Favera, R., & Califano, A. (2005) · Nature Genetics · doi:10.1038/ng1532 · Cited by 1,408
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
Self-citationOxygen sensitivity severely limits the replicative lifespan of murine fibroblasts
Parrinello, S., Samper, E., Krtolica, A., Goldstein, J., Melov, S., & Campisi, J. (2003) · Nature Cell Biology · doi:10.1038/ncb1024 · Cited by 1,116
The INK4a/ARF network in tumour suppression
Sherr, C. J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096061 · Cited by 1,003
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
Bracken, A. P., Kleine-Kohlbrecher, D., Dietrich, N., Pasini, D., Gargiulo, G., Beekman, C., Theilgaard-Mönch, K., Minucci, S., Porse, B. T., Marine, J.-C., et al. (2007) · Genes & Development · doi:10.1101/gad.415507 · Cited by 850
Self-citation
Cited by
Sorted by citations
The essence of senescence: Figure 1.
Kuilman, T., Michaloglou, C., Mooi, W. J., & Peeper, D. S. (2010) · Genes & Development · doi:10.1101/gad.1971610 · Cited by 2,038
Mechanisms of Cellular Senescence: Cell Cycle Arrest and Senescence Associated Secretory Phenotype
Kumari, R., & Jat, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.645593 · Cited by 1,622
Senescence and aging: Causes, consequences, and therapeutic avenues
McHugh, D., & Gil, J. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201708092 · Cited by 1,233
Mechanisms and functions of cellular senescence
Herranz, N., & Gil, J. (2018) · Journal of Clinical Investigation · doi:10.1172/jci95148 · Cited by 1,232
Satoh, T., Takeuchi, O., Vandenbon, A., Yasuda, K., Tanaka, Y., Kumagai, Y., Miyake, T., Matsushita, K., Okazaki, T., Saitoh, T., et al. (2010) · Nature Immunology · doi:10.1038/ni.1920 · Cited by 1,156
Covalent histone modifications — miswritten, misinterpreted and mis-erased in human cancers
Chi, P., Allis, C. D., & Wang, G. G. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2876 · Cited by 1,131
Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials
Cheng, Y., He, C., Wang, M., Ma, X., Mo, F., Yang, S., Han, J., & Wei, X. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0095-0 · Cited by 1,097
ROS, Cell Senescence, and Novel Molecular Mechanisms in Aging and Age‐Related Diseases
Davalli, P., Mitic, T., Caporali, A., Lauriola, A., & D’Arca, D. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3565127 · Cited by 1,059
Kotake, Y., Nakagawa, T., Kitagawa, K., Suzuki, S., Liu, N., Kitagawa, M., & Xiong, Y. (2011) · Oncogene · doi:10.1038/onc.2010.568 · Cited by 1,001
Molecular mechanisms and potential functions of histone demethylases
Kooistra, S. M., & Helin, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3327 · Cited by 913
Self-citationCellular senescence and its effector programs
Salama, R., Sadaie, M., Hoare, M., & Narita, M. (2014) · Genes & Development · doi:10.1101/gad.235184.113 · Cited by 855
Polycomb Group Proteins: Multi-Faceted Regulators of Somatic Stem Cells and Cancer
Sauvageau, M., & Sauvageau, G. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.08.002 · Cited by 586
Reversal of Histone Methylation: Biochemical and Molecular Mechanisms of Histone Demethylases
Mosammaparast, N., & Shi, Y. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103946 · Cited by 607
Adaptive Chromatin Remodeling Drives Glioblastoma Stem Cell Plasticity and Drug Tolerance
Liau, B. B., Sievers, C., Donohue, L. K., Gillespie, S. M., Flavahan, W. A., Miller, T. E., Venteicher, A. S., Hebert, C. H., Carey, C. D., Rodig, S. J., et al. (2017) · Cell stem cell · doi:10.1016/j.stem.2016.11.003 · Cited by 535
Aging, Rejuvenation, and Epigenetic Reprogramming: Resetting the Aging Clock
Rando, T. A., & Chang, H. Y. (2012) · Cell · doi:10.1016/j.cell.2012.01.003 · Cited by 520
Histone lysine demethylases as targets for anticancer therapy
Højfeldt, J. W., Agger, K., & Helin, K. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4154 · Cited by 470
Self-citationMechanisms and Regulation of Cellular Senescence
Roger, L., Tomas, F., & Gire, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313173 · Cited by 395
Histone demethylases in development and disease
Pedersen, M. T., & Helin, K. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.08.011 · Cited by 389
Self-citationThe epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
Bao, H., Cao, J., Chen, M., Min, C., Chen, W., Chen, X., Chen, Y., Chen, Y., Chen, Y., Chen, Z., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2305-0 · Cited by 402
Contrasting roles of histone 3 lysine 27 demethylases in acute lymphoblastic leukaemia
Ntziachristos, P., Tsirigos, A., Welstead, G. G., Trimarchi, T., Bakogianni, S., Xu, L., Loizou, E., Holmfeldt, L., Strikoudis, A., King, B., et al. (2014) · Nature · doi:10.1038/nature13605 · Cited by 377
Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS
Barradas, M., Anderton, E., Acosta, J. C., Li, S., Banito, A., Rodriguez-Niedenführ, M., Maertens, G., Banck, M., Zhou, M.-M., Walsh, M. J., et al. (2009) · Genes & Development · doi:10.1101/gad.511109 · Cited by 352
Histone Demethylases KDM4B and KDM6B Promotes Osteogenic Differentiation of Human MSCs
Ye, L., Fan, Z., Yu, B., Chang, J., Hezaimi, K. A., Zhou, X., Park, N.-H., & Wang, C. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.04.009 · Cited by 335
Healing and Hurting: Molecular Mechanisms, Functions, and Pathologies of Cellular Senescence
Adams, P. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.021 · Cited by 326
McLaughlin-Drubin, M. E., Crum, C. P., & Münger, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009933108 · Cited by 337
Inhibitors of Protein Methyltransferases and Demethylases
Kanıskan, H. Ü., Martini, M. L., & Jin, J. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00801 · Cited by 327
A Kinase-Independent Function of CDK6 Links the Cell Cycle to Tumor Angiogenesis
Kollmann, K., Heller, G., Schneckenleithner, C., Warsch, W., Scheicher, R., Ott, R. G., Schäfer, M., Fajmann, S., Schlederer, M., Schiefer, A.-I., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.07.012 · Cited by 313
UTX and UTY Demonstrate Histone Demethylase-Independent Function in Mouse Embryonic Development
Shpargel, K. B., Sengoku, T., Yokoyama, S., & Magnuson, T. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002964 · Cited by 320
Chandra, T., Kirschner, K., Thuret, J.-Y., Pope, B. D., Ryba, T., Newman, S., Ahmed, K., Samarajiwa, S. A., Salama, R., Carroll, T., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.010 · Cited by 308
Füllgrabe, J., Kavanagh, E. T., & Joseph, B. (2011) · Oncogene · doi:10.1038/onc.2011.121 · Cited by 322
Epigenetic mechanisms in tumorigenesis, tumor cell heterogeneity and drug resistance
Wilting, R. H., & Dannenberg, J. (2012) · Drug Resistance Updates · doi:10.1016/j.drup.2012.01.008 · Cited by 309
The Molecular Balancing Act of p16INK4a in Cancer and Aging
LaPak, K. M., & Burd, C. E. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0350 · Cited by 304
Oncogene-induced senescence: the bright and dark side of the response
Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.07.013 · Cited by 257
Throwing the cancer switch: reciprocal roles of polycomb and trithorax proteins
Mills, A. A. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2931 · Cited by 256
Kim, J., Sharma, A., Dhar, S. S., Lee, S.-H., Gu, B., Chan, C., Lin, H., & Lee, M. G. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-1896 · Cited by 249
Hypoxia promotes stem cell phenotypes and poor prognosis through epigenetic regulation of DICER
van den Beucken, T., Koch, E., Chu, K., Rupaimoole, R., Prickaerts, P., Adriaens, M. E., Voncken, J. W., Harris, A. L., Buffa, F. M., Haider, S. A., et al. (2014) · Nature Communications · doi:10.1038/ncomms6203 · Cited by 229
Chang, S., Yim, S., & Park, H. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0230-6 · Cited by 228
Oxidative Stress and Epigenetic Regulation in Ageing and Age-Related Diseases
Cencioni, C., Spallotta, F., Martelli, F., Valente, S., Mai, A., Zeiher, A. M., & Gaetano, C. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140917643 · Cited by 227
Monti, S., Chapuy, B., Takeyama, K., Rodig, S. J., Hao, Y., Yeda, K. T., Inguilizian, H., Mermel, C. H., Currie, T., Doǧan, A., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.07.014 · Cited by 215
Epigenetic regulation of the INK4b-ARF-INK4a locus: In sickness and in health
Popov, N., & Gil, J. (2010) · Epigenetics · doi:10.4161/epi.5.8.12996 · Cited by 202
Bone Aging, Cellular Senescence, and Osteoporosis
Pignolo, R. J., Law, S. F., & Chandra, A. (2021) · JBMR Plus · doi:10.1002/jbm4.10488 · Cited by 217
Cellular Senescence in Postmitotic Cells: Beyond Growth Arrest
Sapieha, P., & Mallette, F. A. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.03.003 · Cited by 193
Targeting Histone Demethylases: A New Avenue for the Fight against Cancer
Rotili, D., & Mai, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417976 · Cited by 201
Targeting histone lysine methylation in cancer
McGrath, J. P., & Trojer, P. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.002 · Cited by 190
The ARF tumor suppressor: Structure, functions and status in cancer
Ozenne, P., Eymin, B., Brambilla, E. M., & Gazzéri, S. (2010) · International Journal of Cancer · doi:10.1002/ijc.25511 · Cited by 189
de Groote, M. L., Verschure, P. J., & Rots, M. G. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks863 · Cited by 180
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
Senescence in Wound Repair: Emerging Strategies to Target Chronic Healing Wounds
Wilkinson, H. N., & Hardman, M. J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00773 · Cited by 173
Real-time in vivo imaging of p16Ink4a reveals cross talk with p53
Yamakoshi, K., Takahashi, A., Hirota, F., Nakayama, R., Ishimaru, N., Kubo, Y., Mann, D. J., Ohmura, M., Hirao, A., Saya, H., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200904105 · Cited by 172
Tumor suppressor p16 INK4A is necessary for survival of cervical carcinoma cell lines
McLaughlin-Drubin, M. E., Park, D., & Münger, K. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310432110 · Cited by 173
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
Epigenetic aberrations during oncogenesis
Hatziapostolou, M., & Iliopoulos, D. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0624-z · Cited by 173
A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype
Serra, R. W., Fang, M., Park, S. M., Hutchinson, L., & Green, M. R. (2014) · eLife · doi:10.7554/elife.02313 · Cited by 172
The Roles of Jumonji-Type Oxygenases in Human Disease
Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 167
DNA Methylation Is Crucial for the Early Development in the Oyster C. gigas
Rivière, G., Wu, G.-C., Fellous, A., Goux, D., Sourdaine, P., & Favrel, P. (2013) · Marine Biotechnology · doi:10.1007/s10126-013-9523-2 · Cited by 166
Kaelin, W. G. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010975 · Cited by 161
MLL1 is essential for the senescence-associated secretory phenotype
Capell, B. C., Drake, A. M., Zhu, J., Shah, P. P., Dou, Z., Dorsey, J., Simola, D. F., Donahue, G., Sammons, M., Rai, T. S., et al. (2016) · Genes & Development · doi:10.1101/gad.271882.115 · Cited by 156
Critical role of histone demethylase Jmjd3 in the regulation of CD4+ T-cell differentiation
Li, Q., Zou, J., Wang, M., Ding, X., Chepelev, I., Zhou, X., Zhao, W., Wei, G., Cui, J., Zhao, K., et al. (2014) · Nature Communications · doi:10.1038/ncomms6780 · Cited by 152
Zhao, W., Li, Q., Ayers, S. D., Gu, Y., Shi, Z. Q., Zhu, Q., Chen, Y., Wang, H. Y., & Wang, R. (2013) · Cell · doi:10.1016/j.cell.2013.02.006 · Cited by 153
Epigenetic regulation in cancer progression
Baxter, E., Windloch, K., Gannon, F., & Lee, J. S. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-45 · Cited by 159
The role of cellular senescence and SASP in tumour microenvironment
Takasugi, M., Yoshida, Y., Hara, E., & Ohtani, N. (2023) · The FEBS Journal · doi:10.1111/febs.16381 · Cited by 144
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
Salminen, A., Kaarniranta, K., Hiltunen, M. O., & Kauppinen, A. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1182-x · Cited by 148
Lysine Demethylases Inhibitors
Suzuki, T., & Miyata, N. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201048w · Cited by 146
Carragher, L. A. S., Snell, K. R., Giblett, S. M., Aldridge, V. S. S., Patel, B., Cook, S. J., Winton, D. J., Marais, R., & Pritchard, C. A. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000099 · Cited by 144
Anderton, J. A., Bose, S., Vockerodt, M., Vrzalikova, K., Wei, W., Kuo, M., Helin, K., Christensen, J. F., Rowe, M., Murray, P. G., et al. (2011) · Oncogene · doi:10.1038/onc.2010.579 · Cited by 144
Self-citationThe histone demethylase UTX enables RB-dependent cell fate controlPreprint
Wang, J. K., Tsai, M.-C., Poulin, G. B., Adler, A. S., Chen, S., Liu, H., Shi, Y., & Chang, H. Y. (2010) · Genes & Development · doi:10.1101/gad.1882610 · Cited by 152
Skalska, L., White, R. E., Franz, M., Ruhmann, M., & Allday, M. J. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000951 · Cited by 143
Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 145
A Comprehensive Review of Lysine-Specific Demethylase 1 and its Roles in Cancer
Hosseini, A., & Minucci, S. (2017) · Epigenomics · doi:10.2217/epi-2017-0022 · Cited by 139
Human papillomavirus E6 and E7: What remains?
Vats, A., Trejo-Cerro, Ó., Thomas, M., & Banks, L. (2021) · Tumour Virus Research · doi:10.1016/j.tvr.2021.200213 · Cited by 141
Chromatin remodeling in Cancer: A Gateway to regulate gene Transcription
Nair, S. S., & Kumar, R. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.005 · Cited by 139
Targets of Raf in tumorigenesis
Niault, T., & Baccarini, M. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp337 · Cited by 136
Pereira, F., Larriba, M. J., & Múñoz, A. (2012) · Endocrine Related Cancer · doi:10.1530/erc-11-0388 · Cited by 136
Maruo, S., Zhao, B., Johannsen, E., Kieff, E. D., Zou, J., & Takada, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019599108 · Cited by 130
Epigenetic regulation of aging stem cells
Pollina, E. A., & Brunet, A. (2011) · Oncogene · doi:10.1038/onc.2011.45 · Cited by 111
Epigenetic plasticity: A central regulator of epithelial-to-mesenchymal transition in cancer
Bedi, U., Mishra, V. K., Wasilewski, D., Scheel, C., & Johnsen, S. A. (2014) · Oncotarget · doi:10.18632/oncotarget.1875 · Cited by 131
Histone Demethylases and Their Roles in Cancer Epigenetics
D’Oto, A., Tian, Q., Davidoff, A. M., & Yang, J. (2016) · Journal of medical oncology and therapeutics · doi:10.35841/medical-oncology.1.2.34-40 · Cited by 127
Jung, J., Lee, S., Seo, M., Park, S., Kurtz, A., Kang, S., & Kang, K. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0242-9 · Cited by 127
Cancer associated human papillomaviruses
McLaughlin-Drubin, M. E., Meyers, J. M., & Münger, K. (2012) · Current Opinion in Virology · doi:10.1016/j.coviro.2012.05.004 · Cited by 124
Shpargel, K. B., Starmer, J., Yee, D., Pohlers, M., & Magnuson, T. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004507 · Cited by 127
Cell cycle progression in response to oxygen levels
Ortmann, B. M., Druker, J., & Rocha, S. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1645-9 · Cited by 131
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
Dahle, Ø., Kumar, A., & Kuehn, M. R. (2010) · Science Signaling · doi:10.1126/scisignal.2000841 · Cited by 120
A complex Polycomb issue: the two faces of EZH2 in cancerPreprint
Hock, H. R. (2012) · Genes & Development · doi:10.1101/gad.191163.112 · Cited by 124
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
The great unravelling: chromatin as a modulator of the aging process
O’Sullivan, R. J., & Karlseder, J. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.08.001 · Cited by 120
Oncogene-induced senescence: From biology to therapy
Zhu, H., Blake, S., Kusuma, F. K., Pearson, R. B., Kang, J., & Chan, K. T. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111229 · Cited by 116
Ohtani, K., Vlachojannis, G. J., Koyanagi, M., Boeckel, J., Urbich, C., Farcas, R., Bonig, H. B., Márquez, V. E., Zeiher, A. M., & Dimmeler, S. (2011) · Circulation Research · doi:10.1161/circresaha.111.247304 · Cited by 115
Cakouros, D., Isenmann, S., Cooper, L., Zannettino, A. C. W., Anderson, P. J., Glackin, C. A., & Gronthos, S. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06315-11 · Cited by 124
BIM promoter directly targeted by EBNA3C in polycomb-mediated repression by EBV
Paschos, K., Parker, G. A., Watanatanasup, E., White, R. E., & Allday, M. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks391 · Cited by 117
Epigenetic Alterations in Human Papillomavirus-Associated Cancers
Soto, D. R., Song, C., & McLaughlin-Drubin, M. E. (2017) · Viruses · doi:10.3390/v9090248 · Cited by 116
G-tract RNA removes Polycomb repressive complex 2 from genes
Beltran-Nebot, M., Tavares, M., Justin, N., Khandelwal, G., Ambrose, J. C., Foster, B. M., Worlock, K. B., Tvardovskiy, A., Kunzelmann, S., Herrero, J., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0293-z · Cited by 109
Ene, C., Edwards, L., Riddick, G., Baysan, M. S., Woolard, K., Kotliarova, S. E., Lai, C., Belova, G. I., Cam, M. C., Walling, J., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051407 · Cited by 115
Genome-wide analysis reveals that Smad3 and JMJD3 HDM co-activate the neural developmental program
Estarás, C., Akizu, N., García, A., Beltrán, S., de la Cruz, X., & Martínez‐Balbás, M. A. (2012) · Development · doi:10.1242/dev.078345 · Cited by 115
Induced pluripotent stem cells and senescence: learning the biology to improve the technology
Banito, A., & Gil, J. (2010) · EMBO Reports · doi:10.1038/embor.2010.47 · Cited by 111
Epigenetic control of macrophage polarization
Takeuch, O., & Akira, S. (2011) · European Journal of Immunology · doi:10.1002/eji.201141792 · Cited by 110
Beyond transcription factors: how oncogenic signalling reshapes the epigenetic landscape
Liu, F., Wang, L., Perna, F., & Nimer, S. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.41 · Cited by 109
Molecular landscape of recurrent cervical cancer
Adiga, D., Eswaran, S., Pandey, D., Sharan, K., & Kabekkodu, S. P. (2020) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2020.103178 · Cited by 107
Metadata
- Authors
- Agger, K., Cloos, P. A. C., Rudkjær, L., Williams, K., Andersen, G., Christensen, J., & Helin, K.
- Affiliations
- University of Copenhagen (DK)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2009-05-15
- Volume
- 23
- Issue
- 10
- Pages
- 1171-1176
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2685535
- OpenAlex
- W1970592702
- Cited by
- 427
- References
- 26
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 13 · 2023: 13 · 2022: 10 · 2021: 24 · 2020: 23 · 2019: 22 · 2018: 23 · 2017: 21 · 2016: 33 · 2015: 23 · 2014: 36 · 2013: 36 · 2012: 48
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- Kræftens Bekæmpelse
- Sundhed og Sygdom, Det Frie Forskningsråd
- National Research Foundation
- Danmarks Grundforskningsfond
- Lundbeckfonden
- Novo Nordisk
- Harboefonden
- Novo Nordisk Fonden
- H. Lundbeck A/S
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- 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
- Keywords
- JMJD3, H3K27 demethylase, H3K27me3, INK4a/ARF locus, p16INK4a, p14ARF, cellular senescence, oncogene-induced senescence, stress-induced senescence, Ras/Raf signaling, histone demethylation, epigenetic silencing, transcriptional activation, cell immortalization, histone demethylase
- MeSH terms
- Animals, Cell Line, Fibroblasts, Gene Expression Regulation, Humans, Neoplasms, Oncogenes, Oxidoreductases, N-Demethylating, Stress, Physiological, Cellular Senescence, ras Proteins, Cyclin-Dependent Kinase Inhibitor p16, Genes, p16, raf Kinases, Proto-Oncogene Proteins B-raf, Cell Proliferation, Mice, Jumonji Domain-Containing Histone Demethylases
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