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The FBXL10/KDM2B Scaffolding Protein Associates with Novel Polycomb Repressive Complex-1 to Regulate Adipogenesis

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NOF1 Encodes an Arabidopsis Protein Involved in the Control of rRNA Expression

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Reversible histone methylation regulates brain gene expression and behavior

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H3K9 Demethylation-Induced R-Loop Accumulation Is Linked to Disorganized Nucleoli

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KDM2B is involved in the epigenetic regulation of TGF-β-induced epithelial–mesenchymal transition in lung and pancreatic cancer cell lines

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Inhibition of microRNA let‐7b expression by KDM2B promotes cancer progression by targeting EZH2 in ovarian cancer

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The Histone Demethylase FBXL10 Regulates the Proliferation of Spermatogonia and Ensures Long-Term Sustainable Spermatogenesis in Mice1

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H3K27me3 in Diffuse Midline Glioma and Epithelial Ovarian Cancer: Opposing Epigenetic Changes Leading to the Same Poor Outcomes

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RIPK3 deficiency blocks R-2-hydroxyglutarate–induced necroptosis in IDH-mutated AML cells

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ARABIDILLO proteins have a novel and conserved domain structure important for the regulation of their stability

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FBXL10 promotes ERRα protein stability and proliferation of breast cancer cells by enhancing the mono-ubiquitylation of ERRα

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Transcriptional regulation of INK4/ARF locus by cis and trans mechanisms

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Biology and targeting of the Jumonji-domain histone demethylase family in childhood neoplasia: a preclinical overview

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Remodeling and destabilization of chromosome 1 pericentromeric heterochromatin by SSX proteins

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JHDM1B expression regulates ribosome biogenesis and cancer cell growth in a p53 dependent manner

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Abnormal X chromosome inactivation and sex-specific gene dysregulation after ablation of FBXL10

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Nucleolar localization signal and histone methylation reader function is required for SPIN1 to promote rRNA gene expression

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CxxC-ZF Domain Is Needed for KDM2A to Demethylate Histone in rDNA Promoter in Response to Starvation

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DNA replication initiator Cdc6 also regulates ribosomal DNA transcription initiation

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Structural Basis for the Recognition of Non-methylated DNA by the CXXC Domain

Liu, K., & Min, J. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.09.025 · Cited by 20

JmjC‐domain containing histone demethylase 1B‐mediated p15Ink4b suppression promotes the proliferation of leukemic progenitor cells through modulation of cell cycle progression in acute myeloid leukemia

Nakamura, S., Tan, L., Nagata, Y., Takemura, T., Asahina, A., Yokota, D., Yagyu, T., Shibata, K., Fujisawa, S., & Ohnishi, K. (2011) · Molecular Carcinogenesis · doi:10.1002/mc.20878 · Cited by 18

A developmental genetic analysis of the lysine demethylase KDM2 mutations in Drosophila melanogaster

Zheng, Y., Hsu, F.-N., Xu, W., Xie, X.-J., Ren, X., Gao, X., Ni, J., & Ji, J. (2014) · Mechanisms of Development · doi:10.1016/j.mod.2014.06.003 · Cited by 18

Epigenetic Control and Cancer: The Potential of Histone Demethylases as Therapeutic Targets

Lizcano, F., & García, J. (2012) · Pharmaceuticals · doi:10.3390/ph5090963 · Cited by 17

Epigenetic Metalloenzymes

Blanquart, C., Linot, C., Cartron, P., Tomaselli, D., Mai, A., & Bertrand, P. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180706105903 · Cited by 17

Argininosuccinate lyase drives activation of mutant TERT promoter in glioblastomas

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Oocyte-Specific Knockout of Histone Lysine Demethylase KDM2a Compromises Fertility by Blocking the Development of Follicles and Oocytes

Xiong, X., Zhang, X., Yang, M., Zhu, Y., Yu, H., Fei, X., Mastuda, F., Lan, D., Xiong, Y., Fu, W., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231912008 · Cited by 14

KDM2B-Rearranged Soft Tissue Sarcomas Expand the Concept of BCOR-Associated Sarcoma

Motoi, T., Hirata, M., Kukita, Y., Satomi, K., Tamura, H., Adachi, S., Matsushita, Y., Horiguchi, S., Hishima, T., Ikegami, M., et al. (2023) · Modern Pathology · doi:10.1016/j.modpat.2023.100317 · Cited by 14

Exploring the potential of histone demethylase inhibition in multi-therapeutic approaches for cancer treatment

Li, D., Liang, H., Wei, Y., Xiao, H., Peng, X., & Pan, W. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115999 · Cited by 14

Histone Demethylases in Cancer

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Jumonji family histone demethylases in neural development

Fueyo, R., García, M. A., & Martínez‐Balbás, M. A. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1924-7 · Cited by 15

The Lysine Demethylase dKDM2 Is Non-essential for Viability, but Regulates Circadian Rhythms in Drosophila

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FBXL10 promotes EMT and metastasis of breast cancer cells via regulating the acetylation and transcriptional activity of SNAI1

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Histone Ubiquitylation Control of Gene Expression

Weake, V. M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8624-4_6 · Cited by 13

Epigenetic Regulation of Methylation in Determining the Fate of Dental Mesenchymal Stem Cells

Zhang, H., Fu, H. E., Fang, H., Deng, Q., Huang, H., Hou, D., Wang, M., Yao, Q., Si, Q., Chen, R., et al. (2022) · Stem Cells International · doi:10.1155/2022/5015856 · Cited by 13

Roles of F-box proteins in human digestive system tumors (Review)

Gong, J., Lv, L., & Huo, J. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2684 · Cited by 13

Histone H3K79 demethylation by KDM2B facilitates proper DNA replication through PCNA dissociation from chromatin

Kang, J., Park, J. W., Hahm, J. Y., Jung, H., & Seo, S. (2020) · Cell Proliferation · doi:10.1111/cpr.12920 · Cited by 13

Regulation of KDM2B and Brg1 on Inflammatory Response of Nasal Mucosa in CRSwNP

Liu, C. C., Sun, C., Zheng, X., Zhao, M., Kong, F., Xu, F., Chen, X. J., Wang, X., Zhang, M., & Xia, M. (2019) · Inflammation · doi:10.1007/s10753-019-01000-6 · Cited by 13

Modifying the maker: Oxygenases target ribosome biology

Zhuang, Q., Feng, T., & Coleman, M. L. (2015) · Translation · doi:10.1080/21690731.2015.1009331 · Cited by 12

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

Epstein-Barr Virus Nuclear Antigen 3C Inhibits Expression of COBLL1 and the ADAM28-ADAMDEC1 Locus via Interaction with the Histone Lysine Demethylase KDM2B

Gillman, A. C. T., Parker, G. A., Allday, M. J., & Bazot, Q. (2018) · Journal of Virology · doi:10.1128/jvi.01362-18 · Cited by 12

Current advances and future directions in targeting histone demethylases for cancer therapy

Shin, J.-H., Yoo, H.-B., & Roe, J. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100192 · Cited by 12

Epigenetic up-regulation of ribosome biogenesis and more aggressive phenotype triggered by the lack of the histone demethylase JHDM1B in mammary epithelial cells

Galbiati, A., Penzo, M., Bacalini, M. G., Onofrillo, C., Guerrieri, A. N., Garagnani, P., Franceschi, C., Treré, D., & Montanaro, L. (2017) · Oncotarget · doi:10.18632/oncotarget.16181 · Cited by 30

Abstract A15: Epigenetic up-regulation of ribosome biogenesis and more aggressive phenotype triggered by the lack of the histone demethylase JHDM1B in mammary epithelial cells

Galbiati, A., Penzo, M., Bacalini, M. G., Onofrillo, C., Guerrieri, A. N., Garagnani, P., Franceschi, C., Treré, D., & Montanaro, L. (2017) · Cancer Research · doi:10.1158/1538-7445.transcontrol16-a15

JHDM1B expression regulates ribosome biogenesis and cancer cell growth in a p53 dependent manner

Penzo, M., Casoli, L., Pollutri, D., Sicuro, L., Ceccarelli, C., Santini, D., Taffurelli, M., Govoni, M., Brina, D., Treré, D., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.29240 · Cited by 23

Abstract 5145: KDM2B expression regulates ribosome biogenesis and cancer cell growth in a p53-dependent manner

Penzo, M., Casoli, L., Sicuro, L., Galibiati, A., Pollutri, D., Govoni, M., Ceccarelli, C., Santini, D., Taffurelli, M., Treré, D., et al. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-5145

The histone demethylase JMJD2A/KDM4A links ribosomal RNA transcription to nutrients and growth factors availability

Salifou, K., Ray, S., Verrier, L., Aguirrebengoa, M., Trouche, D., Panov, K. I., & Vandromme, M. (2016) · Nature Communications · doi:10.1038/ncomms10174 · Cited by 46