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 accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“KDM6A/B mediate the removal of the suppressive chromatin modification H3K27me3, which is associated with silenced genes26.”
From Epigenetic regulation of brain region-specific microglia clearance activity (2018) · cites this paper as [26]
In the citing paper
“Enrichment of mRNAs encoding the H3K27me3-specific demethylases, KDM6A/B26 in cbMg (Supplementary Fig. 5b, Supplementary Table 3) as well as the up-regulation of Kdm6a/b in microglia upon exposure to dying cells in vitro (Fig. 3c, Supplementary Fig. 10g) point to the possible role of PRC2/H3K27me3 in suppressing clearance-promoting genes in stMg.”
From Epigenetic regulation of brain region-specific microglia clearance activity (2018) · cites this paper as [26]
In the citing paper
“Among the genes that become rapidly induced in microglia upon exposure to apoptotic cells were the cbMg-enriched Kdm6a/b, which encode histone demethylases26 (Fig. 3c, Supplementary Fig. 10g).”
From Epigenetic regulation of brain region-specific microglia clearance activity (2018) · cites this paper as [26]
Citations
Cites
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
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-citationDe 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
Research works printed but not linked: 4
- Agger, 2007, Nature
- De Santa, 2007, Cell
- Lan, 2007, Nature
- Lee, 2007, Science
Cited by
Sorted by citations
Items 201–300 of 328
Taneja, G., Maity, S., Jiang, W., Moorthy, B., Coarfa, C., & Ghose, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-43248-w · Cited by 18
Cheng, M.-F., Lee, C.-H., Hsia, K.-T., Huang, G.-S., & Lee, H.-S. (2009) · PubMed · doi:10.14670/hh-24.1105 · Cited by 18
Zhang, M., Tang, C., Li, S., Jiang, X., Li, B., Chen, Y., Zheng, Q., Tang, Y., Zhu, X., Huang, L., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217939 · Cited by 17
Cheng, X., & Trievel, R. C. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00210 · Cited by 17
Bonello, G. B., Pham, M.-H., Begum, K., Sigala, J. A., Sataranatarajan, K., & Mummidi, S. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.0900643 · Cited by 18
Chi, Y., Stodola, T. J., de Assuncao, T. M., Leverence, E. N., Tripathi, S., Dsouza, N. R., Mathison, A., Basel, D., Volkman, B. F., Smith, B. C., et al. (2021) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-021-01692-w · Cited by 17
Epigenetic Heterogeneity of B-Cell Lymphoma: Chromatin Modifiers
Hopp, L., Nersisyan, L., Loeffler‐Wirth, H., Arakelyan, A., & Binder, H. (2015) · Genes · doi:10.3390/genes6041076 · Cited by 16
Generation of an anti-EpCAM antibody and epigenetic regulation of EpCAM in colorectal cancer
Liao, M., Kuo, M. Y., Lu, T., Wang, Y., & Wu, H. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.2876 · Cited by 15
Mapping the epigenome — impact for toxicology
Marlowe, J. L., Teo, S.-S., Chibout, S., Pognan, F., & Moggs, J. G. (2009) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-7643-8336-7_10 · Cited by 15
Chi, Y., Stodola, T. J., de Assuncao, T. M., Leverence, E. N., Smith, B. C., Volkman, B. F., Mathison, A., Lomberk, G. A., Zimmermann, M. T., & Urrutia, R. A. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.04.028 · Cited by 15
Phagocytic microglia in development: Are they what they eat?
VanRyzin, J. W. (2021) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2021.100373 · Cited by 15
Epigenetic Pathways of Oncogenic Viruses: Therapeutic Promises
El‐Araby, A. M., Fouad, A. A., Hanbal, A. M., Abdelwahab, S. M. M., Qassem, O. M., & El‐Araby, M. E. (2016) · Archiv der Pharmazie · doi:10.1002/ardp.201500375 · Cited by 15
JMJD3 promotes esophageal squamous cell carcinoma pathogenesis through epigenetic regulation of MYC
Li, S., He, L., Chen, J., Zhou, J., Nie, R., Jin, X., Wang, X., Fu, J., Wang, F., & Xie, D. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00282-9 · Cited by 13
Small Molecule GSK-J1 Affects Differentiation of Specific Neuronal Subtypes in Developing Rat Retina
Raeisossadati, R., Móvio, M. I., Walter, L. T., Takada, S. H., Debbio, C. B. D., & Kihara, A. H. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1197-3 · Cited by 12
Tissue-Specific Tumour Suppressor and Oncogenic Activities of the Polycomb-like Protein MTF2
Ngubo, M., Moradi, F., Ito, C. Y., & Stanford, W. L. (2023) · Genes · doi:10.3390/genes14101879 · Cited by 12
Roy, S., Sinha, N., Huang, B., Cline-Fedewa, H. M., Gleicher, N., Wang, J., & Sen, A. (2022) · Endocrinology · doi:10.1210/endocr/bqac047 · Cited by 12
Adachi, N., Suzuki, S., Matsuoka, H., Fushimi, S., Ono, J., Ohta, K., Hirai, Y., Miki, T., & Koshimizu, H. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14310 · Cited by 12
Christensen, M. D., Nitiyanandan, R., Meraji, S., Daer, R., Godeshala, S., Goklany, S., Haynes, K. A., & Rege, K. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.06.030 · Cited by 12
Li, S., Jiang, L., He, Q., Wei, W., Wang, Y., Zhang, X., Liu, J., Chen, K., Chen, J., & Xie, D. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s225596 · Cited by 12
Emerging role of Jumonji domain-containing protein D3 in inflammatory diseases
Li, X., Chen, R.-Y., Shi, J., Li, C., Liu, Y.-J., Gao, C., Gao, M.-R., Zhang, S., Lu, J., Cao, J.-F., et al. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.100978 · Cited by 11
Ge, G., Zhang, P., Sui, P., Shi, C., Yang, H., Guo, Y., Rubalcava, I. P., Noor, A., Delma, C. R., Agosto-Peña, J., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci163964 · Cited by 10
Functions and Mechanism of Thyroid Hormone Receptor Action During Amphibian Development
Louis, E., Fu, L., Shi, Y., & Sachs, L. M. (2024) · Endocrinology · doi:10.1210/endocr/bqae137 · Cited by 10
Hong, Z., Li, H., Li, L., Wang, W., & Xu, T. (2016) · Cancer Biomarkers · doi:10.3233/cbm-160003 · Cited by 10
Nava, M., Dutta, P., Farias‐Eisner, R., Vadgama, J. V., & Wu, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-41672-6 · Cited by 10
Liu, Z., Zhang, H., Hu, Y., Liu, D., Li, L., Li, C., Wang, Q., Huo, J., Liu, H., Xie, N., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0546-8 · Cited by 10
DNA-sequence-specific erasers of epigenetic memory
Mozgová, I., & Köhler, C. (2016) · Nature Genetics · doi:10.1038/ng.3579 · Cited by 10
The Role of Methylation Modification in Neural Injury and Repair
Lv, S., Pan, Y., Zheng, T., Cao, Q., Yu, B., Zhou, F., & Wang, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115349 · Cited by 9
Nuclear architecture and gene silencing in olfactory sensory neurons
Armelin‐Correa, L., Nagai, M. H., Silva, A. G. L., & Malnic, B. (2014) · BioArchitecture · doi:10.4161/19490992.2014.982934 · Cited by 9
Rao, R. C., Chan, M. P., Andrews, C., & Kahana, A. (2018) · Cellular Oncology · doi:10.1007/s13402-018-0402-8 · Cited by 9
Transcriptional Control of Cell Fate Determination in Antigen-Experienced CD8 T CellsPreprint
Tsuda, S., & Pipkin, M. E. (2021) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a037945 · Cited by 10
McIntyre, T. I., Valdez, O., Kochhar, N. P., Davidson, B. R., Samad, B., Qiu, L., Hu, K. H., Combes, A. J., & Erlebacher, A. (2025) · Cell · doi:10.1016/j.cell.2024.12.019 · Cited by 8
Bhadhprasit, W., Sakuma, T., Kawasaki, Y., & Nemoto, N. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.035980 · Cited by 8
Imuta, H., Fujita, D., Oba, S., Kiyosue, A., Nishimatsu, H., Yudo, K., & Suzuki, E. (2020) · Heart and Vessels · doi:10.1007/s00380-020-01670-5 · Cited by 8
Panning, B. (2010) · Cell stem cell · doi:10.1016/j.stem.2009.12.013 · Cited by 7
Hasebe, T., Fujimoto, K., Buchholz, D. R., & Ishizuya‐Oka, A. (2020) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2020.113441 · Cited by 7
Graffmann, N., Brands, J., Görgens, A., Castro, S. V. D. C., Santourlidis, S., Reckert, A., Michele, I., Ritz‐Timme, S., Fischer, J., Adjaye, J., et al. (2015) · Stem Cells and Development · doi:10.1089/scd.2014.0435 · Cited by 6
KDM6B is a conserved activator at the top of the male sex determination pathway
Dupont, S. M., Garcia-Moreno, S. A., O’Neil, E. V., & Capel, B. (2025) · Development · doi:10.1242/dev.204724 · Cited by 6
Rack, S., Patel, K., Heathcote, E., Mistry, H. B., Betts, G. N. J., Harrington, K. J., & Metcalf, R. L. (2025) · Oral Oncology · doi:10.1016/j.oraloncology.2025.107229 · Cited by 6
An aging program at the systems level?
Han, J. J. (2012) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.21007 · Cited by 6
Early-Life Adversity and Suicide Risk: The Role of Epigenetics
Turecki, G. (2017) · Springer eBooks · doi:10.1007/978-3-319-47976-7_4 · Cited by 6
Post-Translational Modifications that Regulate Kinetochore Activity
Kotwaliwale, C. V., & Biggins, S. (2008) · Springer eBooks · doi:10.1007/978-0-387-69076-6_10 · Cited by 6
Tang, S., Wang, Q., Wang, Z., Cai, L., Pan, D., Li, J., Chen, Q., Zhou, Y. L., & Shen, Y. (2025) · The Journal of Pathology · doi:10.1002/path.6430 · Cited by 5
Pinton, G., Ferraro, A., Balma, M., & Moro, L. (2020) · Electromagnetic Biology and Medicine · doi:10.1080/15368378.2020.1737807 · Cited by 4
Hasebe, T., Fujimoto, K., & Ishizuya‐Oka, A. (2022) · Vitamins and hormones · doi:10.1016/bs.vh.2022.11.006 · Cited by 4
Novel histone modifications in microglia derived from a mouse model of chronic pain
Zhang, P., Guergues, J., Alleyne, A. R., Cirino, T. J., Nadeau, O. W., Figueroa, A. M., Stacy, H. M., Suzuki, T., McLaughlin, J. P., Stevens, S. M., et al. (2022) · PROTEOMICS · doi:10.1002/pmic.202100137 · Cited by 4
Kolev, H. M., Swisa, A., Manduchi, E., Lan, Y., Stine, R. R., Testa, G., & Kaestner, K. H. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.12.001 · Cited by 4
The KDM6B mutation: Phenotype and clinical characteristics—Report of a case
Pineda, I. I., & González, C. L. G. (2021) · Revista de Psiquiatría y Salud Mental · doi:10.1016/j.rpsm.2020.12.005 · Cited by 4
Inter-nucleosomal communication between histone modifications for nucleosome phasing
Chen, W., Liu, Y., Zhu, S., Chen, G., & Han, J. J. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006416 · Cited by 4
Luo, J., Yu, Y., & Song, J. (2011) · doi:10.1002/9781119949930.ch8 · Cited by 4
Karpenko, D. V., Петинати, Н. А., Дризе, Н. И., & Bigildeev, A. (2021) · Гематология и трансфузиология · doi:10.35754/0234-5730-2021-66-2-263-279 · Cited by 3
Integrating epigenetic marks for identification of transcriptionally active miRNAs
Xiao, Y., Liu, T., Zhao, H., Li, X., Guan, J., Xu, C., Ping, Y., Fan, H., Wang, L., Zhao, T., et al. (2014) · Genomics · doi:10.1016/j.ygeno.2014.07.003 · Cited by 3
Non-viral iPSCs: a safe way for therapy?
Zhang, W., Guan, D., Qu, J., Zhang, W., & Liu, G. (2012) · Protein & Cell · doi:10.1007/s13238-012-2804-0 · Cited by 3
The KDM6B mutation: Phenotype and clinical characteristics—Report of a case
Pineda, I. I., & González, C. L. G. (2022) · Revista de Psiquiatría y Salud Mental (English Edition) · doi:10.1016/j.rpsmen.2022.06.005 · Cited by 3
Epigenetic Regulation of Neural Crest Cells
Strobl‐Mazzulla, P. H., & Bronner-Fraser, M. E. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-401730-6.00005-3 · Cited by 3
Methods of Epigenome Editing for Probing the Function of Genomic Imprinting
Rienecker, K. D. A., Hill, M., & Isles, A. R. (2016) · Epigenomics · doi:10.2217/epi-2016-0073 · Cited by 3
Structural landscape of H3K27me3 recognition by protein domains and their potential for inhibition
Rosas, R., Baracaldo-Lancheros, L. F., Dykhuizen, E. C., & Musselman, C. A. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111344 · Cited by 2
Epigenetic Regulation of Pluripotency by Polycomb Group Proteins
Breiling, A. (2014) · Epigenetics and human health · doi:10.1007/978-3-642-31974-7_6 · Cited by 2
CCL17 Blockade by CCL17mAb/GSK-J4 Ameliorates Hyperalgesia in a Rat Model of Postoperative Pain
Zhang, Z., Zhang, T., Zhang, Y., & Liang, Y. (2023) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b22-00463 · Cited by 2
Wu, Q., Yu, C., Yu, F., Guo, Y., Sheng, Y., Li, L., Li, Y., Zhang, Y., Hu, C., Wang, J., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci173403 · Cited by 2
Impact of the Early-Life Environment on the Epigenome and Behavioral Development
Labonté, B., & Turecki, G. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8078-5_8 · Cited by 2
Finnegan, E. J., & Dennis, E. S. (2008) · Plant Signaling & Behavior · doi:10.4161/psb.3.6.5439 · Cited by 2
Epigenetics of Suicidal Behaviour
Turecki, G. (2015) · Advances in biological psychiatry · doi:10.1159/000434738 · Cited by 2
System Review about Function Role of ESCC Driver Gene KDM6A by Network Biology Approach
Ran, J., Li, H., & Li, H. (2016) · The Scientific World JOURNAL · doi:10.1155/2016/1970904 · Cited by 2
Histone modifications in aging: Research progress
Jia, M., & Pu, M. (2019) · Scientia Sinica Vitae · doi:10.1360/ssv-2019-0106 · Cited by 1
Acetylation and Methylation in Asthma, COPD, and Lung Cancer
Zwinderman, M. R. H., Cao, F., & Dekker, F. J. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_81 · Cited by 2
Epigenetic regulation of dental pulp stem cells and its potential in regenerative endodontics
Liu, Y., Gan, L., Cui, D., Yu, S.-H., Pan, Y., Zheng, L., & Wan, M. (2021) · World Journal of Stem Cells · doi:10.4252/wjsc.v13.i11.1650 · Cited by 2
Specific low frequency electromagnetic fields induce epigenetic and functional changes in U937 cellsPreprint
Pinton, G., Ferraro, A., Balma, M., & Moro, L. (2018) · arXiv (Cornell University) · doi:10.48550/arxiv.1810.06255 · Cited by 2
Wang, Q., Yuan, D., Lu, Y., Wang, X., Zheng, H., Li, L., Chen, S., & He, X. (2025) · Advanced Science · doi:10.1002/advs.202503420 · Cited by 1
Metabolic oxidoreductases: central regulators of the epigenetic landscapes in stemness
Lee, H., Roe, J., & Youn, H. (2026) · Experimental & Molecular Medicine · doi:10.1038/s12276-026-01687-2 · Cited by 2
Herndon, C. A., Snell, J., & Fromm, L. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0227-7 · Cited by 1
Chromatin Remodeling and Androgen Receptor-Mediated Transcription
Li, J., Khalid, O. S., Frenkel, B., & Coetzee, G. A. (2009) · Springer eBooks · doi:10.1007/978-0-387-69179-4_18 · Cited by 1
Research progress in modification of histone lysine methylation and congenital heart defect
Sheng, W., & Ma, D. (2010) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2010.00650 · Cited by 1
The role of polyhomeotic in polycomb group-mediatedregulation of the tumour suppressor P16INK4A
de Breed, L. A. (2010) · UCL Discovery (University College London) · Cited by 1
JMJD3 and vascular injury: the Emperor's new clothes
Mongelli, A., & Gaetano, C. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy249 · Cited by 1
Swigut, T., & Wysocka, J. (2009) · Cell · doi:10.1016/j.cell.2009.04.008 · Cited by 1
Self-citationKim, H., Lebeau, B., Papadopoli, D. J., Jovanović, P., Russo, M. D. S. T., Avizonis, D. Z., Morita, M., Afzali, F., Ursini‐Siegel, J., Postovit, L.-M. M., et al. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4631549 · Cited by 1
Peeters, J. G. C., Silveria, S. L., Özdemir, M., Ramachandran, S., & DuPage, M. J. P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.05.588284 · Cited by 1
Epigenetic Role of PTIP in Mouse Spermatogenesis
Liu, C. (2015)
Identification and Functional Characterization of Polycomb Group Complexes in Drosophila
Lagarou, A. (2009) · EUR Research Repository (Erasmus University Rotterdam)
Einfluss epigenetischer Mechanismen auf das Verhalten der Honigbiene
Hättig, J. (2009) · Publications of the UdS (Saarland University) · doi:10.22028/d291-22575
The role of CYP33 in MLL mediated gene repression
Poppen, S. D. (2012) · Loyola eCommons (Loyola University of Chicago)
Histone Methyltransferases (GLP, G9a, SETDB1) and H3K9me2; Regulation in Psychiatric Disorders
Chase, K. A. (2012) · Figshare
Early life programming of adult Leydig cell function
Kilcoyne, K. R., Smith, L. B., Jobling, M. S., McKinnell, C., Macpherson, S., van, D. D. S., De, G. K., Verhoeven, G., Anderson, R. A., & Sharpe, R. M. (2014) · Reproduction Abstracts · doi:10.1530/repabs.1.p175
Role of histone methylation in paternal transmission of epigenetic information
Brykczynska, U. (2010) · edoc (University of Basel) · doi:10.5451/unibas-005404718
Organic codes and their identification : is the histone code a true organic code
Kühn, S. (2014) · SUNScholar (Stellenbosch University)
Labonté, B., & Turecki, G. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139519502.034
A SMARCB1 gén genetikai és epigenetikai vizsgálata epithelioid sarcomában
Papp, G. (2015) · Semmelweis University Repository (Semmelweis University) · doi:10.14753/se.2015.1692
Research: Mediators and Moderators
Koslow, S. H., Ruiz, P., & Nemeroff, C. B. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139519502.033
Engineering and Delivery of Synthetic Chromatin Effectors
Tekel, S. J. (2019)
Solary, É. (2017) · Springer eBooks · doi:10.1007/978-3-662-46875-3_7137
Solary, É. (2012) · Springer eBooks · doi:10.1007/978-3-642-27841-9_7137-3
KDM6B Promotes ESCC Cell Proliferation and Metastasis by Facilitating C/EBPβ TranscriptionPreprint
qin, M., han, F., Wu, J., Gao, F., Li, Y., Yan, D.-X., He, X., Long, Y., tang, X., Ren, D.-L., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-140744/v1
McLaughlin-Drubin, M. E. (2014) · Springer eBooks · doi:10.1007/978-3-642-27841-9_7177-3
McLaughlin-Drubin, M. E. (2017) · Springer eBooks · doi:10.1007/978-3-662-46875-3_7177
Blelloch, R. H. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727824409.793549700
Data from EZH2: Not EZHY (Easy) to Deal
Deb, G., Singh, A. K., & Gupta, S. (2023) · doi:10.1158/1541-7786.c.6539991.v1
JMJD3 Exerts Oncorepressor Activity in Acute Promyelocytic Leukemia by Promoting PU.1 Expression
Wang, M., Yu, S., Xiao, M., & Chen, J. (2023) · Molecular Biology · doi:10.1134/s0026893323040179
JMJD3 Exerts Oncorepressor Activity in Acute Promyelocytic Leukemia by Promoting PU.1 Expression
Wang, M.-X., Yu, S.-H., Xiao, M., & Chen, J. (2023) · Molecular Biology · doi:10.31857/s0026898423040213
Metadata
- Authors
- Swigut, T., & Wysocka, J.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Wysocka, Joanna
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-10
- Volume
- 131
- Issue
- 1
- Pages
- 29-32
- ISSN
- 0092-8674 (ISSN-L)
- 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