JmjC-domain-containing proteins and histone demethylation

MrBayes 3: Bayesian phylogenetic inference under mixed models

Ronquist, F., & Huelsenbeck, J. P. (2003) · Bioinformatics · doi:10.1093/bioinformatics/btg180 · Cited by 29,194

MRBAYES: Bayesian inference of phylogenetic trees.

Huelsenbeck, J. P., & Ronquist, F. (2001) · Bioinformatics · doi:10.1093/bioinformatics/17.8.754 · Cited by 21,937

The Pfam Protein Families Database

Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,075

MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment

Kumar, S. (2004) · Briefings in Bioinformatics · doi:10.1093/bib/5.2.150 · Cited by 11,674

Multiple sequence alignment with hierarchical clustering.

Corpet, F. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.22.10881 · Cited by 5,575

Multiple sequence alignment with the Clustal series of programs

Chenna, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg500 · Cited by 4,905

Histone demethylation mediated by the nuclear amine oxidase homolog LSD1

Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051

SMART, a simple modular architecture research tool: Identification of signaling domains

Schultz, J., Milpetz, F., Peer Bork, B., & Ponting, C. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5857 · Cited by 3,577

The Pfam protein families database

Bateman, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh121 · Cited by 3,127

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903

Epigenetic regulator Lid maintains germline stem cells through regulating JAK-STAT signaling pathway activity

Tarayrah, L., Li, Y., Gan, Q., & Chen, X. (2015) · Biology Open · doi:10.1242/bio.013961 · Cited by 31

Hydroxylation mediates chromatin demethylation

Tsukada, Y.-I. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs003 · Cited by 31

Metformin activates KDM2A to reduce rRNA transcription and cell proliferation by dual regulation of AMPK activity and intracellular succinate level

Tanaka, Y., Konishi, A., Obinata, H., & Tsuneoka, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-55075-0 · Cited by 31

Epigenetic Regulation of Wnt Signaling by Carboxamide-Substituted Benzhydryl Amines that Function as Histone Demethylase Inhibitors

Zhang, W., Sviripa, V. M., Xie, Y., Yu, T., Haney, M. G., Blackburn, J. S., Adeniran, C. A., Zhan, C., Watt, D. S., & Liu, C. (2020) · iScience · doi:10.1016/j.isci.2020.101795 · Cited by 30

Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells

Flora, P., Dalal, G., Cohen, I., & Ezhkova, E. (2021) · Genes · doi:10.3390/genes12101485 · Cited by 31

Disrupted Alpha-Ketoglutarate Homeostasis: Understanding Kidney Diseases from the View of Metabolism and Beyond

Guo, L.-J., Chen, S., Ou, L., Li, S., Ye, Z.-N., & Liu, J. (2022) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s369090 · Cited by 34

Reconstitution of Nucleosome Demethylation and Catalytic Properties of a Jumonji Histone Demethylase

Shiau, C., Trnka, M. J., Božičević, A., Torres, I. O., Al‐Sady, B., Burlingame, A. L., Narlikar, G. J., & Fujimori, D. G. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.03.008 · Cited by 30

Comparative integromics on JMJD1C gene encoding histone demethylase: Conserved POU5F1 binding site elucidating mechanism of JMJD1C expression in undifferentiated ES cells and diffuse-type gastric cancer

Katoh, M., & Katoh, M. (2007) · International Journal of Oncology · doi:10.3892/ijo.31.1.219 · Cited by 30

Structure of the JmjC-domain-containing protein JMJD5

Wang, H., Zhou, X., Wu, M., Wang, C., Zhang, X., Tao, Y., Chen, N., & Zang, J. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913016600 · Cited by 30

The expanding world of histone lysine demethylases

Metzger, E., & Schüle, R. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb0407-252 · Cited by 30

Protein and DNA Modifications: Evolutionary Imprints of Bacterial Biochemical Diversification and Geochemistry on the Provenance of Eukaryotic EpigeneticsPreprint

Aravind, L., Burroughs, A. M., Zhang, D., & Iyer, L. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016063 · Cited by 30

A novel form of JARID2 is required for differentiation in lineage‐committed cells

Al‐Raawi, D., Jones, R., Wijesinghe, S. N., Halsall, J. A., Petrić, M., Roberts, S., Hotchin, N. A., & Kanhere, A. (2018) · The EMBO Journal · doi:10.15252/embj.201798449 · Cited by 29

Vitamin C in Pneumonia and Sepsis

Carr, A. C. (2020) · CRC Press eBooks · doi:10.1201/9780429442025-7 · Cited by 31

Histone Modifications and Chondrocyte Fate: Regulation and Therapeutic Implications

Wan, C., Zhang, F., Yao, H., Li, H., & Tuan, R. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.626708 · Cited by 31

Genome-wide screens uncover KDM2B as a modifier of protein binding to heparan sulfate

Weiss, R. J., Spahn, P. N., Chiang, A. W. T., Liu, Q., Li, J., Hamill, K. M., Rother, S., Clausen, T. M., Hoeksema, M. A., Timm, B. M., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00776-9 · Cited by 28

Vitamin C, From Supplement to Treatment: A Re-Emerging Adjunct for Cancer Immunotherapy?

Kouakanou, L., Peters, C., Brown, C. E., Kabelitz, D., & Wang, L. D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.765906 · Cited by 31

Hairless Modulates Ligand-Dependent Activation of the Vitamin D Receptor-Retinoid X Receptor Heterodimer

Chuma, M., Endo‐Umeda, K., Shimba, S., Yamada, S., & Makishima, M. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.35.582 · Cited by 29

dLKR/SDH regulates hormone-mediated histone arginine methylation and transcription of cell death genes

Cakouros, D., Mills, K., Denton, D., Paterson, A., Daish, T., & Kumar, S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712169 · Cited by 29

HP1a Targets the Drosophila KDM4A Demethylase to a Subset of Heterochromatic Genes to Regulate H3K36me3 Levels

Lin, C., Paulson, A., Abmayr, S. M., & Workman, J. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039758 · Cited by 29

Regulatory Function of Histone Modifications in Controlling Rice Gene Expression and Plant Growth

Zhou, D., & Hu, Y. (2010) · Rice · doi:10.1007/s12284-010-9045-8 · Cited by 29

Mapping the Phosphorylation Pattern of Drosophila melanogaster RNA Polymerase II Carboxyl-Terminal Domain Using Ultraviolet Photodissociation Mass Spectrometry

Mayfield, J. E., Robinson, M., Cotham, V. C., Irani, S., Matthews, W. L., Ram, A., Gilmour, D. S., Cannon, J. R., Zhang, Y., & Brodbelt, J. S. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00729 · Cited by 28

Epigenetically Modified Bone Marrow Stromal Cells in Silk Scaffolds Promote Craniofacial Bone Repair and Wound Healing

Han, Q., Yang, P., Wu, Y., Meng, S., Sui, L., Zhang, L., Yu, L., Tang, Y., Jiang, H., Xuan, D., et al. (2015) · Tissue Engineering Part A · doi:10.1089/ten.tea.2014.0484 · Cited by 29

Histone lysine demethylases function as co-repressors of SWI/SNF remodeling activities during Drosophila wing development

Curtis, B. J., Zraly, C. B., Marenda, D. R., & Dingwall, A. K. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.12.001 · Cited by 28

Dissociation of the H3K36 demethylase Rph1 from chromatin mediates derepression of environmental stress-response genes under genotoxic stress inSaccharomyces cerevisiae

Liang, C., Wang, L., & Lo, W. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-11-0820 · Cited by 28

Hypoxia-mediated changes in bone marrow microenvironment in breast cancer dormancy

Ferrer, A. I., Roser, C. T., El-Far, M. H., Savanur, V. H., Eljarrah, A., Gergues, M., Kra, J., Etchegaray, J., & Rameshwar, P. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.05.026 · Cited by 30

Drug discovery of histone lysine demethylases (KDMs) inhibitors (progress from 2018 to present)

He, X., Zhang, H., Zhang, Y., Ye, Y., Wang, S., Bai, R., Xie, T., & Ye, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114143 · Cited by 28

CTCF and Its Multi-Partner Network for Chromatin Regulation

Moral‐Morales, A. D., Salgado-Albarrán, M., Sánchez-Pérez, Y., Wenke, N. K., Baumbach, J., & Soto‐Reyes, E. (2023) · Cells · doi:10.3390/cells12101357 · Cited by 30

Proteomic Identification and Analysis of Arginine-Methylated Proteins of Plasmodium falciparum at Asexual Blood Stages

Zeeshan, M., Kaur, I., Joy, J., Saini, E., Paul, G., Kaushik, A., Dabral, S., Mohmmed, A., Gupta, D. K., & Malhotra, P. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01052 · Cited by 28

JMJD5 (Jumonji Domain-containing 5) Associates with Spindle Microtubules and Is Required for Proper Mitosis

He, Z., Wu, J., Su, X., Zhang, Y., Pan, L., Wei, H., Fang, Q., Li, H., Wang, D.-L., & Sun, F.-L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.672642 · Cited by 27

JmjC domain proteins modulate circadian behaviors and sleep in Drosophila

Shalaby, N. A., Pinzón, J. H., Narayanan, A. S., Jin, E. J., Ritz, M. P., Dove, R., Wolfenberg, H., Rodan, A. R., Buszczak, M., & Rothenfluh, A. (2018) · Scientific Reports · doi:10.1038/s41598-017-18989-1 · Cited by 26

Epigenetic Regulation of Spermatogonial Stem Cell Homeostasis: From DNA Methylation to Histone Modification

Zhou, S., Feng, S., Qin, W., Wang, X., Tang, Y., & Yuan, S. (2020) · Stem Cell Reviews and Reports · doi:10.1007/s12015-020-10044-3 · Cited by 29

Fumonisin B1 Epigenetically Regulates PTEN Expression and Modulates DNA Damage Checkpoint Regulation in HepG2 Liver Cells

Arumugam, T., Ghazi, T., & Chuturgoon, A. A. (2020) · Toxins · doi:10.3390/toxins12100625 · Cited by 27

A glutamine ‘tug-of-war’: targets to manipulate glutamine metabolism for cancer immunotherapy

Pallett, L. J., Dimeloe, S., Sinclair, L. V., Byrne, A. J., & Schurich, A. (2021) · Immunotherapy Advances · doi:10.1093/immadv/ltab010 · Cited by 28

Dynamic changes of histone methylation in mammalian oocytes and early embryos

Bilmez, Y., Talibova, G., & Öztürk, S. (2021) · Histochemistry and Cell Biology · doi:10.1007/s00418-021-02036-2 · Cited by 27

Secondary Metabolite Gene Regulation in Mycotoxigenic Fusarium Species: A Focus on Chromatin

Atanasoff-Kardjalieff, A. K., & Studt, L. (2022) · Toxins · doi:10.3390/toxins14020096 · Cited by 27

How transcription factors program chromatin—Lessons from studies of the regulation of myeloid-specific genes

Bonifer, C., Hoogenkamp, M., Krysinska, H., & Tagoh, H. (2008) · Seminars in Immunology · doi:10.1016/j.smim.2008.05.001 · Cited by 27

Histone lysine demethylases in Drosophila melanogaster

Holowatyj, A., Yang, Z.-Q., & Pile, L. A. (2015) · Fly · doi:10.1080/19336934.2015.1074787 · Cited by 27

Epigenetic regulation of cardiac development and function by polycomb group and trithorax group proteins

Wang, Q. T. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23796 · Cited by 25

Depletion of Jmjd1c impairs adipogenesis in murine 3T3-L1 cells

Buerger, F., Müller, S., Ney, N., Weiner, J., Heiker, J. T., Kallendrusch, S., Kovacs, P. L., Schleinitz, D., Thiery, J., Stadler, S. C., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.05.011 · Cited by 27

Systematic genetic interaction studies identify histone demethylase Utx as potential target for ameliorating Huntington’s disease

Song, W., Zsindely, N., Faragó, A., Marsh, J., & Bodai, L. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx432 · Cited by 26

Regulation of ectopic heterochromatin-mediated epigenetic diversification by the JmjC family protein Epe1

Sorida, M., Hirauchi, T., Ishizaki, H., Kaito, W., Shimada, A., Mori, C., Chikashige, Y., Hiraoka, Y., Suzuki, Y., Ohkawa, Y., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008129 · Cited by 27

Evidence of a Demethylase-Independent Role for the H3K4-Specific Histone Demethylases in Aspergillus nidulans and Fusarium graminearum Secondary Metabolism

Bachleitner, S., Sørensen, J. L., Gacek‐Matthews, A., Sulyok, M., Studt, L., & Strauss, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01759 · Cited by 27

The Drosophila Huntington's disease gene ortholog dhtt influences chromatin regulation during development

Dietz, K. N., Stefano, L. D., Maher, R. C., Zhu, H., MacDonald, M. E., Gusella, J. F., & Walker, J. A. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu446 · Cited by 28

Epigenetics, infertility, and cancer: future directions

James, E. R., & Jenkins, T. G. (2018) · Fertility and Sterility · doi:10.1016/j.fertnstert.2017.11.006 · Cited by 25

The JMJD Family Histone Demethylases in Crosstalk Between Inflammation and Cancer

Yang, J., Hu, Y., Zhang, B., Liang, X., & Li, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.881396 · Cited by 26

Natural product myricetin is a pan-KDM4 inhibitor which with poly lactic-co-glycolic acid formulation effectively targets castration-resistant prostate cancer

Liu, J.-S., Fang, W.-K., Yang, S., Wu, M.-C., Chen, T.-J., Chen, C., Lin, T.-Y., Liu, K.-L., Wu, C.-M., Chen, Y., et al. (2022) · Journal of Biomedical Science · doi:10.1186/s12929-022-00812-3 · Cited by 26

Post-Translational Modifications of Histones in Vertebrate Neurogenesis

Mitrousis, N., Tropepe, V., & Hermanson, O. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00483 · Cited by 26

Utx loss causes myeloid transformation

Zheng, L., Xu, L., Xu, Q., Yu, L., Zhao, D., Chen, P., Wang, W., Wang, Y., Han, G., & Chen, C. D. (2018) · Leukemia · doi:10.1038/s41375-018-0011-6 · Cited by 26

Molecular architecture of the Jumonji C family histone demethylase KDM5B

Dorosz, J., Kristensen, L. H., Aduri, N. G., Mirza, O., Lousen, R., Bucciarelli, S., Mehta, V., Sellés‐Baiget, S., Solbak, S. M. Ø., Bach, A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40573-y · Cited by 26

The complexity of epigenetic diseases

Brazel, A. J., & Vernimmen, D. (2015) · The Journal of Pathology · doi:10.1002/path.4647 · Cited by 25

F‐box protein CFK1 interacts with and degrades de novo DNA methyltransferase in Arabidopsis

Chen, J., Liu, J., Jiang, J., Qian, S., Song, J., Kabara, R., Delo, I., Serino, G., Liu, F., Hua, Z., et al. (2020) · New Phytologist · doi:10.1111/nph.17103 · Cited by 24

Integrated Multiomic Analysis Reveals the High-Fat Diet Induced Activation of the MAPK Signaling and Inflammation Associated Metabolic Cascades via Histone Modification in Adipose Tissues

Wang, Z., Zhu, M., Wang, M., Gao, Y., Zhang, C., Liu, S., Qu, S., Liu, Z., & Zhang, C. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.650863 · Cited by 25

Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast

Separovich, R. J., & Wilkins, M. R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100939 · Cited by 29

Chemical Inhibitors Targeting the Histone Lysine Demethylase Families with Potential for Drug Discovery

Das, N. D., Niwa, H., & Umehara, T. (2023) · Epigenomes · doi:10.3390/epigenomes7010007 · Cited by 26

JARID2 coordinates with the NuRD complex to facilitate breast tumorigenesis through response to adipocyte‐derived leptin

Liu, W., Zeng, Y., Hao, X., Wang, X., Liu, J., Gao, T., Wang, M., Zhang, J., Huo, M., Hu, T., et al. (2023) · 癌症：英文版 · doi:10.1002/cac2.12479 · Cited by 24

High-Throughput Screening for Growth Inhibitors Using a Yeast Model of Familial Paraganglioma

Bancos, I., Bida, J. P., Tian, D., Bundrick, M., John, K., Holte, M. N., Her, Y. F., Evans, D. L., Saenz, D. T., Poeschla, E. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056827 · Cited by 25

Intersection of nuclear receptors and the proteasome on the epigenetic landscape

Kinyamu, H. K., Jefferson, W. N., & Archer, T. (2007) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20360 · Cited by 25

Genome Sequencing of the Behavior Manipulating Virus LbFV Reveals a Possible New Virus Family

Lepetit, D., Gillet, B., Hughes, S., Kraaijeveld, K., & Varaldi, J. (2016) · Genome Biology and Evolution · doi:10.1093/gbe/evw277 · Cited by 24

Crystal Structures of REF6 and Its Complex with DNA Reveal Diverse Recognition Mechanisms

Tian, Z., Li, X., Li, M., Wu, W., Zhang, M., Tang, C., Li, Z., Liu, Y., Chen, Z., Yang, M., et al. (2019) · Cell Discovery · doi:10.1038/s41421-020-0150-6 · Cited by 26

Nucleation and Propagation of Heterochromatin by the Histone Methyltransferase PRC2: Geometric Constraints and Impact of the Regulatory Subunit JARID2

Ge, E. J., Jani, K. S., Diehl, K. L., Müller, M. M., & Muir, T. W. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b02321 · Cited by 24

Early Life Stress- and Drug-Induced Histone Modifications Within the Ventral Tegmental Area

Shepard, R. D., & Nugent, F. S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.588476 · Cited by 25

EZH2 as a Potential Target for NAFLD Therapy

Lim, H. J., & Kim, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228617 · Cited by 24

The Role of 2-Oxoglutarate Dependent Dioxygenases in Gliomas and Glioblastomas: A Review of Epigenetic Reprogramming and Hypoxic Response

Crake, R., Burgess, E. R., Royds, J. A., Phillips, E., Vissers, M. C. M., & Dachs, G. U. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.619300 · Cited by 24

JMJD5 is a potential oncogene for colon carcinogenesis.

Zhang, R., Huang, Q., Li, Y., Song, Y., & Li, Y. (2015) · Europe PMC (PubMed Central) · Cited by 24

Ablation of Mina53 in Mice Reduces Allergic Response in the Airways

Mori, T., Okamoto, K., Tanaka, Y., Teye, K., Umata, T., Ohneda, K., Tokuyama, K., Okabe, M., & Tsuneoka, M. (2013) · Cell Structure and Function · doi:10.1247/csf.13006 · Cited by 24

Epigenetic methylations and their connections with metabolism

Chiacchiera, F., Piunti, A., & Pasini, D. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1293-5 · Cited by 25

Purification and assay protocols for obtaining highly active Jumonji C demethylases

Krishnan, S., Collazo, E., Ortiz-Tello, P. A., & Trievel, R. C. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.08.034 · Cited by 24

Epigenetics of Neurological Cancers

Fouse, S. D., & Costello, J. (2009) · Future Oncology · doi:10.2217/fon.09.132 · Cited by 25

Epigenetic Modification in Macrophages: A Promising Target for Tumor and Inflammation-associated Disease Therapy

Sun, P., Zhang, S., Maksim, S., Yao, Y., Liu, H., & Du, J. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190619143706 · Cited by 24

New discoveries of mdig in the epigenetic regulation of cancers

Zhang, Q., Thakur, C., Shi, J., Sun, J., Fu, Y. S., Stemmer, P. M., & Chen, F. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.013 · Cited by 24

Significant induction by drought of HvPKDM7-1, a gene encoding a jumonji-like histone demethylase homologue in barley (H. vulgare)

Papaefthimiou, D., & Tsaftaris, A. S. (2011) · Acta Physiologiae Plantarum · doi:10.1007/s11738-011-0915-5 · Cited by 24

Epigenetic Dysregulation in Cancer: Implications for Gene Expression and DNA Repair-Associated Pathways

Rembiałkowska, N., Rekiel, K., Urbanowicz, P., Mamala, M. B., Marczuk, K. M., Wojtaszek, M., Żywica, M., Radzevičiūtė-Valčiukė, E., Novickij, V., & Kulbacka, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136531 · Cited by 34

NO points to epigenetics in vascular development

Illi, B., Colussi, C., Rosati, J. D., Spallotta, F., Nanni, S., Farsetti, A., Capogrossi, M. C., & Gaetano, C. (2011) · Cardiovascular Research · doi:10.1093/cvr/cvr056 · Cited by 23

A JUMONJI Protein with E3 Ligase and Histone H3 Binding Activities Affects Transposon Silencing in Arabidopsis

Kabelitz, T., Brzezinka, K., Friedrich, T., Górka, M., Graf, A., Kappel, C., & Bäurle, I. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01688 · Cited by 22

Hypoxia and hypoxia mimetics differentially modulate histone post-translational modifications

Hsu, K., Wilkins, S. E., Hopkinson, R. J., Sekirnik, R., Flashman, E., Kawamura, A., McCullagh, J., Walport, L. J., & Schofield, C. J. (2020) · Epigenetics · doi:10.1080/15592294.2020.1786305 · Cited by 22

Mesenchymal Deletion of Histone Demethylase NO66 in Mice Promotes Bone Formation

Chen, Q., Sinha, K. M., Deng, J. M., Yasuda, H., Krahe, R., Behringer, R. R., & Crombrugghe, B. D. (2015) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2494 · Cited by 23

Advancing our understanding of functional genome organisation through studies in the fission yeast

Olsson, I., & Bjerling, P. (2010) · Current Genetics · doi:10.1007/s00294-010-0327-x · Cited by 23

Regulation of alternative macrophage activation by chromatin remodeling

Bowdridge, S. A. A., & Gause, W. C. (2010) · Nature Immunology · doi:10.1038/ni1010-879 · Cited by 23

Role of yeast JmjC-domain containing histone demethylases in actively transcribed regions

Kwon, D.-W., & Ahn, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.06.039 · Cited by 23

Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism

Chang, Y., Wu, J., Tong, X.-J., Zhou, J., & Ding, J. (2010) · Biochemical Journal · doi:10.1042/bj20101418 · Cited by 23

Inhibitors of both the N -methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases

Bonnici, J., Tumber, A., Kawamura, A., & Schofield, C. J. (2018) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2017.0071 · Cited by 23

Structural basis for binding of cyclic 2-oxoglutarate analogues to factor-inhibiting hypoxia-inducible factor

Conejo‐García, A., McDonough, M. A., Loenarz, C., McNeill, L. A., Hewitson, K. S., Ge, W., Liénard, B. M. R., Schofield, C. J., & Clifton, I. J. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.08.032 · Cited by 23

Epigenetic regulation in adult stem cells and cancers

Tarayrah, L., & Chen, X. (2013) · Cell & Bioscience · doi:10.1186/2045-3701-3-41 · Cited by 22

MoJMJ1, Encoding a Histone Demethylase Containing JmjC Domain, Is Required for Pathogenic Development of the Rice Blast Fungus, Magnaporthe oryzae

Huh, A., Dubey, A., Kim, S., Jeon, J., & Lee, Y. (2017) · The Plant Pathology Journal · doi:10.5423/ppj.oa.11.2016.0244 · Cited by 22

Defense Response to Pathogens Through Epigenetic Regulation in Rice

Hoang, T. V., Vo, K. T. X., Hong, W., Jung, K., & Jeon, J. (2018) · Journal of Plant Biology · doi:10.1007/s12374-017-0434-z · Cited by 22

Characterization and Stress Response of the JmjC Domain-Containing Histone Demethylase Gene Family in the Allotetraploid Cotton Species Gossypium hirsutum

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Chou, K. Y., Lee, J.-Y., Kim, K., Kim, E., Lee, H., & Ryu, H. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.02.037 · Cited by 24

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