Cited by 1,290Epigenetics and DNA MethylationGenomics and Chromatin DynamicsCancer-related gene regulation

The DOI matches its Crossref record; 105 of the 106 references it cites were found in a registry or an index.

JmjC-domain-containing proteins and histone demethylation

Klose, Robert J., Kallin, Eric M., Zhang, Yi·2006·Nature Reviews Genetics

DOI 10.1038/nrg1945

Open this paper in CoChat — free account

Abstract

Histone methylation has important roles in regulating gene expression and forms part of the epigenetic memory system that regulates cell fate and identity. Enzymes that directly remove methyl marks from histones have recently been identified, revealing a new level of plasticity within this epigenetic modification system. Here we analyse the evolutionary relationship between Jumonji C (JmjC)-domain-containing proteins and discuss their cellular functions in relation to their potential enzymatic activities.

Integrity signals

Registry

Crossref · 10.1038/nrg1945

Cites

105 of 105 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, 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?

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

Show all 106 references

Sorted by citations

Items 901–1,000 of 1,000

LSD1 prevents aberrant heterochromatin formation in Neurospora crassa
Storck, W. K., Bicocca, V. T., Rountree, M. R., Honda, S., Ormsby, T., & Selker, E. U. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa724 · Cited by 9
Exploiting Drug-Induced Senescence in Transgenic Mouse Models
Kılıç, M., & Schmitt, C. A. (2008) · CRC Press eBooks · doi:10.3109/9781420020502-17 · Cited by 9
Epigenetic modification mechanism of histone demethylase KDM1A in regulating cardiomyocyte apoptosis after myocardial ischemia-reperfusion injury
He, L., Wang, Y., & Luo, J. (2022) · PeerJ · doi:10.7717/peerj.13823 · Cited by 8
Histone modifications in fat metabolism and obesity
Chu, D., Thi, Y.-V. N., & Chew, N. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.01.003 · Cited by 8
JmjC catalysed histone H2a N-methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships
Bonnici, J., Oueini, R., Salah, E., Johansson, C., Pires, E., Abboud, M. I., Dawber, R. S., Tumber, A., Rabe, P., Saraç, H., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-07183-5 · Cited by 8
Heterozygous Kmt2d loss diminishes enhancers to render medulloblastoma cells vulnerable to combinatory inhibition of LSD1 and OXPHOS
Dhar, S. S., Brown, C. J., Rizvi, A., Reed, L., Kotla, S., Zod, C., Abraham, J., Abe, J., Rajaram, V., Chen, K., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115619 · Cited by 8
Histone demethylation by JMJ family genes: insights into plant growth and adaptation
Theboral, J., Blessy, A., Krishnamoorthy, S., & Sridhar, A. (2025) · Plant Molecular Biology · doi:10.1007/s11103-025-01645-y · Cited by 8
Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins
Konduri, P. C., Wang, T., Salamat, N., & Li, Z. (2020) · Cells · doi:10.3390/cells9030773 · Cited by 8
KDM6A, a histone demethylase, regulates stress hematopoiesis and early B-cell differentiation
Huppertz, S., Senger, K., Brown, A., Leins, H., Eiwen, K., Mulaw, M. A., Geiger, H., & Becker, M. (2021) · Experimental Hematology · doi:10.1016/j.exphem.2021.06.001 · Cited by 8
The Lysine Demethylases KdmA and KdmB Differently Regulate Asexual Development, Stress Response, and Virulence in Aspergillus fumigatus
Choi, Y.-H., Lee, M.-W., & Shin, K.-S. (2022) · Journal of Fungi · doi:10.3390/jof8060590 · Cited by 8
Chromosome-level genome assemblies of two parasitoid biocontrol wasps reveal the parthenogenesis mechanism and an associated novel virus
Inwood, S. N., Skelly, J., Guhlin, J. G., Harrop, T. W. R., Goldson, S. L., & Dearden, P. K. (2023) · BMC Genomics · doi:10.1186/s12864-023-09538-4 · Cited by 8
The Effect of the Length of Histone H3K4me3 on Recognition by Reader Proteins
Pieters, B. J. G. E., Belle, R., & Mecinović, J. (2013) · ChemBioChem · doi:10.1002/cbic.201300525 · Cited by 8
Epigenetic control of the immune system: histone demethylation as a target for drug discovery
Lora, J. M., Wilson, D. M., Lee, K. C., & Larminie, C. G. C. (2010) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2010.10.001 · Cited by 8
Lysine demethylase 3a in craniofacial and neural development during Xenopus embryogenesis
Lee, H., Ismail, T., Kim, C., Kim, Y., Park, J., Kwon, O., Kang, B., Lee, D., Kwon, T., Park, T. J., et al. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.4024 · Cited by 8
Interplay of Circadian Rhythms and Light in the Regulation of Photosynthesis-Derived Metabolism
Jones, M. A. (2017) · Progress in botany · doi:10.1007/124_2017_2 · Cited by 8
PHF2 regulates sarcomeric gene transcription in myogenesis
Fukushima, T., Hasegawa, Y., Kuse, S., Fujioka, T., Nikawa, T., Masubuchi, S., & Sakakibara, I. (2024) · PLoS ONE · doi:10.1371/journal.pone.0301690 · Cited by 7
Targeting histone methylation and demethylation for non-alcoholic fatty liver disease
Du, Y., He, Z., Jin, S., Jin, G. Y., Wang, K., Yang, F., & Zhang, J. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107698 · Cited by 7
Interplay between epigenetics and metabolism controls cancer stem cell plasticity
Choi, J.-E., & Baek, I. (2024) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2024.1424163 · Cited by 7
An H3K9me2 demethylase encoded by Jumonji C domain-containing DT2 regulates drought tolerance in rice
Wang, X., Yu, Z., Xu, H. J., Chen, H., Lu, J., Li, X., Li, F., Chen, W., & Xu, Q. (2025) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiaf280 · Cited by 7
Evidence human FTO catalyses hydroxylation of N6-methyladenosine without direct formation of a demethylated product contrasting with ALKBH5/2/3 and bacterial AlkB
Kaur, S., Maheswaran, P., Kaur, S., Lai, Y., Salah, E., Zhang, D., Shishodia, S., Schofield, C. J., & Aik, W. S. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf813 · Cited by 7
To Erase or Not to Erase: Non-Canonical Catalytic Functions and Non-Catalytic Functions of Members of Histone Lysine Demethylase Families
Nisio, E. D., Manzini, V., Licursi, V., & Negri, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136900 · Cited by 7
Biosynthesis of the Unusual Epoxy Isonitrile-Containing Antibiotics Aerocyanidin and Amycomicin
Zheng, Z., Clardy, J., & Liu, H. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c06411 · Cited by 7
Genome-wide identification, evolution of histone lysine demethylases (KDM) genes and their expression during gonadal development in Nile tilapia
Qin, Z., Li, Z., Yang, S., Wang, F., Gao, T., Tao, W., Zhou, L., Wang, D., & Sun, L. (2021) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2021.110674 · Cited by 7
Site-specific Phosphorylation of Histone H3K36 Methyltransferase Set2p and Demethylase Jhd1p is Required for Stress Responses in Saccharomyces cerevisiae
Separovich, R. J., Wong, M. W. M., Bartolec, T. K., Hamey, J. J., & Wilkins, M. R. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167500 · Cited by 7
Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans
Chowdhury, R., Abboud, M. I., Wiley, J., Tumber, A., Markolovic, S., & Schofield, C. J. (2022) · Scientific Reports · doi:10.1038/s41598-022-10028-y · Cited by 7
Molecular characterization of the porcine JHDM1A gene associated with average daily gain: evaluation its role in skeletal muscle development and growth
Peng, Y., Fan, B., Han, X., Xu, X., Rothschild, M. F., Martine Yerle, B., & Liu, B. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0604-2 · Cited by 7
The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain
Pieters, B. J. G. E., Meulenbroeks, E., Belle, R., & Mecinović, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139205 · Cited by 7
Effect of sex differences in donor foetal fibroblast on the early development and DNA methylation status of buffalo (Bubalus bubalis) nuclear transfer embryos
Ruan, Z., Zhao, X., Li, Z., Qin, X., Shao, Q., Ruan, Q., Deng, Y., Jiang, J., Huang, B., Lu, F., et al. (2018) · Reproduction in Domestic Animals · doi:10.1111/rda.13286 · Cited by 7
Cellular Iron Deficiency Disrupts Thyroid Hormone Regulated Gene Expression in Developing Hippocampal Neurons
Monko, T. R., Tripp, E., Burr, S. E., Gunderson, K. N., Lanier, L. M., Georgieff, M., & Bastian, T. W. (2023) · Journal of Nutrition · doi:10.1016/j.tjnut.2023.11.007 · Cited by 6
Unveiling the Molecular Landscape of Pancreatic Ductal Adenocarcinoma: Insights into the Role of the COMPASS-like Complex
Jamali, M., Barar, E., & Shi, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105069 · Cited by 6
Discovery and structural studies of histone demethylases
Peng, L., Li, X., Yang, H., Chen, H., Yue, Y., & Peng, S. (2025) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2025.1594400 · Cited by 6
KDM7 Demethylases: Regulation, Function and Therapeutic Targeting
Shao, P., Liu, Q., & Qi, H. H. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-38176-8_8 · Cited by 6
Construction of a high‐density linkage map and QTL detection for growth traits in South African abalone (Haliotis midae)
Tshilate, T. S., Ishengoma, E., & Rhode, C. (2024) · Animal Genetics · doi:10.1111/age.13462 · Cited by 6
Insights into The Function and Regulation of Jumonji C Lysine Demethylases as Hypoxic Responsive Enzymes
Chopra, A., Adhikary, H., Willmore, W. G., & Biggar, K. K. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203721666191231104225 · Cited by 7
Tudor domain of histone demethylase KDM4B is a reader of H4K20me3
Xiang, Y., Guo, J., Li, F., & Xiong, J. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa064 · Cited by 6
Elevated Expression of JMJD5 Protein Due to Decreased miR-3656 Levels Contributes to Cancer Stem Cell-Like Phenotypes under Overexpression of Cancer Upregulated Gene 2
Yawut, N., Cho, I.-R., Budluang, P., Kaowinn, S., Kaewpiboon, C., Jeon, B.-E., Kim, S., Kang, H. Y., Kang, M.-K., Koh, S. S., et al. (2022) · Biomolecules · doi:10.3390/biom12010122 · Cited by 6
Epigenetic Control of Muscle Stem Cells: Focus on Histone Lysine Demethylases
Cicciarello, D., Schaeffer, L., & Scionti, I. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.917771 · Cited by 6
A complete methyl-lysine binding aromatic cage constructed by two domains of PHF2
Horton, J. R., Zhou, J., Chen, Q., Zhang, X., Bedford, M. T., & Cheng, X. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102862 · Cited by 6
RNA or DNA? Revisiting the Chemical Nature of the Cenancestral Genome
Cottom-Salas, W., Becerra, A., & Lazcano, A. (2024) · Journal of Molecular Evolution · doi:10.1007/s00239-024-10194-9 · Cited by 7
Histone Modification and Breast Cancer
Luo, X., Guo, S., Guo, Y., & Zhang, C. (2011) · InTech eBooks · doi:10.5772/24308 · Cited by 6
The Histone Demethylase Activity of Rph1 is Not Essential for Its Role in the Transcriptional Response to Nutrient Signaling
Nordberg, N., Olsson, I., Carlsson, M. J. L., Hu, G., Westholm, J. O., & Ronne, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095078 · Cited by 6
The C-Module-Binding Factor Supports Amplification of TRE5-A Retrotransposons in the Dictyostelium discoideum Genome
Bilzer, A., Dölz, H., Reinhardt, A., Schmith, A., Siol, O., & Winckler, T. (2010) · Eukaryotic Cell · doi:10.1128/ec.00205-10 · Cited by 6
Genetic Screen for Genes Involved in Chk2 Signaling in Drosophila
Park, S.-K., & Song, Y. (2008) · Molecules and Cells · doi:10.1016/s1016-8478(23)14007-6 · Cited by 6
Current advances of targeting epigenetic modifications in neuroendocrine prostate cancer
Cheng, W., & Wang, H. (2021) · Tzu Chi Medical Journal · doi:10.4103/tcmj.tcmj_220_20 · Cited by 6
The emerging roles for histone demethylases in the modulation of signaling pathways
Stefano, L. D., & Dyson, N. J. (2012) · BioMolecular Concepts · doi:10.1515/bmc-2012-0031 · Cited by 6
Mina: a Th2 response regulator meets TGFβ
Pillai, M. R., Lian, S., & Bix, M. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.09.005 · Cited by 6
Involvement of epigenetic modifiers in the pathogenesis of testicular dysgenesis and germ cell cancer
Lawaetz, A. C., & Almstrup, K. (2015) · BioMolecular Concepts · doi:10.1515/bmc-2015-0006 · Cited by 6
LSD1/KDM1A Maintains Genome-wide Homeostasis of Transcriptional EnhancersPreprint
Agarwal, S., Garay, P. M., Porter, R. S., Brookes, E., Murata-Nakamura, Y., Macfarlan, T. S., Ren, B., & Iwase, S. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/146357 · Cited by 6
Dynamics of transcription-dependent H3K36me3 marking by the SETD2:IWS1:SPT6 ternary complexPreprint
Čermáková, K., Smith, E. A., Veverka, V., & Hodges, H. C. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/636084 · Cited by 8
Altered costimulatory signals and hypoxia support chromatin landscapes limiting the functional potential of exhausted T cells in cancerPreprint
Ford, B. R., Rittenhouse, N., Scharping, N. E., Vignali, P., Frisch, A. T., Peralta, R. M., Delgoffe, G. M., & Poholek, A. C. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.11.451947 · Cited by 6
JMJD3-mediated senescence is required to overcome stress-induced hematopoietic defects
Nakata, Y., Ueda, T., Sera, Y., Koizumi, M., Imamura, K., Kanai, A., Ikeda, K., Yamasaki, N., Nagamachi, A., Kobatake, K., et al. (2025) · EMBO Reports · doi:10.1038/s44319-025-00502-9 · Cited by 5
Mitochondrial Genetics in Cardiovascular Health and Disease: A Scientific Statement From the American Heart Association
Fetterman, J. L., Chinnery, P. F., McClellan, R., Wallace, D. C., Suomalainen, A., Ojala, T. H., Lewis, S. C., & Ballinger, S. W. (2025) · Circulation · doi:10.1161/cir.0000000000001393 · Cited by 7
Covalent inhibitors meet epigenetics: New opportunities
Feng, Q., Yu, L., Li, L., & Zhang, Q. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116951 · Cited by 5
JMJD1C forms condensate to facilitate a RUNX1-dependent gene expression program shared by multiple types of AML cells
Chen, Q., Wang, S., Zhang, J., Xie, M., Lu, B., He, J., Zhen, Z. P., Li, J., Zhu, J., Li, R., et al. (2024) · Protein & Cell · doi:10.1093/procel/pwae059 · Cited by 5
Biochemical investigations using mass spectrometry to monitor JMJD6-catalysed hydroxylation of multi-lysine containing bromodomain-derived substrates
Corner, T. P., Salah, E., Tumber, A., Brewitz, L., & Schofield, C. J. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00311j · Cited by 6
JMJ720 regulates flowering time in rice via H3K9 demethylation of Hd1
Li, X., Zhu, J., Tian, X., Liu, Y., Wei, J., Hong, Z., Jin, X., Chen, C., Wang, Z., Tang, J., et al. (2025) · Plant Biotechnology Journal · doi:10.1111/pbi.70206 · Cited by 5
Discovery of Histone Demethylase Inhibitors
Hauser, A., Roatsch, M., Schulz‐Fincke, J., Robaa, D., Sippl, W., & Jung, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801080-8.00018-1 · Cited by 6
Unprogrammed epigenetic variation mediated by stochastic formation of ectopic heterochromatin
Sorida, M., & Murakami, Y. (2019) · Current Genetics · doi:10.1007/s00294-019-01031-4 · Cited by 5
Genome-wide Characterization of the JmjC Domain-Containing Histone Demethylase Gene Family Reveals GhJMJ24 and GhJMJ49 Involving in Somatic Embryogenesis Process in Cotton
Li, Y., Zhu, S., Yao, J., Fang, S., Li, T., Li, B., Wang, X., Wang, M., Wu, L., Pan, J., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.888983 · Cited by 5
Self-citation
Lysine Demethylation in Pathogenesis
Cao, J. P., & Yan, Q. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-38176-8_1 · Cited by 5
Combined expression of JHDM1D/KDM7A gene and long non-coding RNA RP11-363E7.4 as a biomarker for urothelial cancer prognosis
da Silva, G. N., Pereira, I. O. A., Lima, A. P. B., Almeida, T. C., Sávio, A. L. V., Costa, R. P., Leite, K. R. M., & Salvadori, D. M. F. (2024) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2023-0265 · Cited by 5
Mechanism of JmjC-containing protein Hairless in the regulation of vitamin D receptor function
Mi, Y., Zhang, Y., & Shen, Y. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.09.015 · Cited by 5
Self-citation
Identification of novel JMJD2A inhibitor scaffold using shape and electrostatic similarity search combined with docking method and MM-GBSA approach
Feng, T., Chen, W., Li, D., Lin, H., Liu, F., Bao, Q., Lei, Y., Zhang, X., Xu, X., Guo, X., et al. (2015) · RSC Advances · doi:10.1039/c5ra11896d · Cited by 5
Nutrition, Histone Epigenetic Marks, and Disease
Zempleni, J., Liu, D., & Xue, J. (2013) · Epigenetics and human health · doi:10.1007/978-3-642-36827-1_9 · Cited by 5
Escape from Mitotic Arrest: An Unexpected Connection Between Microtubule Dynamics and Epigenetic Regulation of Centromeric Chromatin in Schizosaccharomyces pombe
George, A. A., & Walworth, N. C. (2015) · Genetics · doi:10.1534/genetics.115.181792 · Cited by 5
Molecular mechanisms of transcriptional and chromatin remodeling around embryonic genome activation
Bogliotti, Y. S., & Ross, P. J. (2015) · Animal Reproduction · Cited by 5
Adventures in Defining Roles of Oxygenases in the Regulation of Protein Biosynthesis
Walport, L. J., & Schofield, C. J. (2018) · The Chemical Record · doi:10.1002/tcr.201800056 · Cited by 5
Mining histone methyltransferases and demethylases from whole genome sequence
Gulati, P., Kohli, S., Narang, A., & Brahmachari, V. (2020) · Journal of Biosciences · doi:10.1007/s12038-019-9982-3 · Cited by 5
Biological function and regulation of histone 4 lysine 20 methylation in DNA damage response
Kohi, S. M., Feng, T., Tian, Y., & Zhu, W. (2022) · Genome Instability & Disease · doi:10.1007/s42764-022-00063-4 · Cited by 6
Design, Synthesis and Characterization of Covalent KDM5 Inhibitors
Vázquez-Rodríguez, S., Wright, M., Rogers, C. M., Cribbs, A. P., Velupillai, S., Philpott, M., Lee, H., Dunford, J. E., Huber, K., Robers, M. B., et al. (2018) · Angewandte Chemie · doi:10.1002/ange.201810179 · Cited by 5
Is JmjC Oxygenase Catalysis Limited to Demethylation?
Hopkinson, R. J., Walport, L. J., Münzel, M., Rose, N. R., Smart, T. J., Kawamura, A., Claridge, T. D. W., & Schofield, C. J. (2013) · Angewandte Chemie · doi:10.1002/ange.201303282 · Cited by 5
KDM4 Demethylases: Structure, Function, and Inhibitors
Jiang, Y., Liu, L., & Yang, Z.-Q. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-38176-8_5 · Cited by 6
Overexpression of dJmj differentially affects intestinal stem cells and differentiated enterocytes
Suong, D. N. A., Shimaji, K., Pyo, J.-H., Park, J., Yoshida, H., Yoo, M., & Yamaguchi, M. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.10.017 · Cited by 5
In Vitro Enzyme Assays for JmjC‐Domain‐Containing Lysine Histone Demethylases (JmjC‐KDMs)
Tarhonskaya, H., Tumber, A., Kawamura, A., & Schofield, C. J. (2018) · Current Protocols in Pharmacology · doi:10.1002/cpph.34 · Cited by 5
Identification of Two Novel Mutations in KDM3A Regulatory Gene in Iranian Infertile Males
Hojati, Z., Soleimanpour, E., Javadirad, S.-M., & Nasr‐Esfahani, M. H. (2019) · PubMed Central · doi:10.29252/.23.3.220 · Cited by 5
HOXD3 Up-regulating KDM5C Promotes Malignant Progression of Diffuse Large B-Cell Lymphoma by Decreasing p53 Expression
Cui, Y., Lv, C., Wen, Y., Zhao, D., Yu, Y., Qiu, H., & Wang, C. (2021) · Balkan Medical Journal · doi:10.5152/balkanmedj.2021.21068 · Cited by 5
Conserved Gene Regulatory Function of the Carboxy-Terminal Domain of Dictyostelid C-Module-Binding Factor
Schmith, A., Groth, M., Ratka, J., Gatz, S., Spaller, T., Siol, O., Glöckner, G., & Winckler, T. (2013) · Eukaryotic Cell · doi:10.1128/ec.00329-12 · Cited by 5
Novel Potent Inhibitors of the Histone Demethylase Kdm1A (Lsd1), Orally Active in a Murine Promyelocitic Leukemia Model
Trifiró, P., Cappa, A., Brambillasca, S., Botrugno, O. A., Cera, M. R., Zuffo, R. D., Dessanti, P., Meroni, G., Thaler, F., Villa, M., et al. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0003 · Cited by 5
Two‐domain analysis of JmjN‐JmjC and PHD‐JmjC lysine demethylases: Detecting an inter‐domain evolutionary stress
Slama, P. S. (2017) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25394 · Cited by 5
Inhibiting the Jumonji Family: A Potential New Clinical Approach to Targeting Aberrant Epigenetic Mechanisms
Martínez, E. D., & Gazdar, A. F. (2016) · Epigenomics · doi:10.2217/epi.15.115 · Cited by 5
A new role for IDH1 in the control of ovarian cancer cells metabolism and senescence
Sonego, M., & Baldassarre, G. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2020.02.62 · Cited by 5
The role of Kabuki Syndrome genes KMT2D and KDM6A in development: Analysis in Human sequencing data and compared to mice and zebrafishPreprint
Sen, R., Lencer, E. S., Geiger, E. A., Jones, K. L., Shaikh, T. H., & Artinger, K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.03.024646 · Cited by 5
Advances in combination therapy for the treatment of estrogen receptor positive breast cancer
Liu, L., Zhao, Z., Zou, F., Lu, Y., & Lu, Y. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.111451 · Cited by 4
Lysine demethylases 6 A and 6B as epigenetic regulators in therapeutic resistance of cancer
Yang, L., Li, H., Zhao, Y., Qian, Z., Luo, G., Chen, X., & Yang, X. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-02010-y · Cited by 5
The JmjC domain-containing histone demethylase ZmJMJ703 orchestrates salt stress adaptation in maize
Wang, S., Jiang, L., Zhai, T., Qu, K., Liu, X., Di, Z., Chen, Y., Lu, X., Li, X., Zhang, J., et al. (2025) · Journal of Plant Physiology · doi:10.1016/j.jplph.2025.154677 · Cited by 4
Metabolic support of trained immune responses in myeloid cells
Jarit-Cabanillas, A., Dunphy, G., Virga, F., den Bossche, J. V., & Sancho, D. (2026) · eLife · doi:10.7554/elife.108814 · Cited by 4
Activity Guided Azide-methyllysine Photo-trapping for Substrate Profiling of Lysine Demethylases
Kuwik, J., Hinkelman, K., Waldman, M., Stepler, K. E., Wagner, S., Arora, S., Chernenkoff, S., Cabalteja, C. C., Sidoli, S., Robinson, R. A. S., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c07299 · Cited by 4
Kdm4d mutant mice show impaired sperm motility and subfertility
Zhuoran, X. U., FUJIMOTO, Y., SAKAMOTO, M., Ito, D., Ikawa, M., & Ishiuchi, T. (2024) · Journal of Reproduction and Development · doi:10.1262/jrd.2024-039 · Cited by 4
JmjC domain-containing histone demethylase gene family in Chinese cabbage: Genome-wide identification and expressional profiling
Yin, F., Hu, Y., Cao, X., Xiao, X., Zhang, M., Xiang, Y., Wang, L., Yao, Y., Sui, M., & Shi, W. (2024) · PLoS ONE · doi:10.1371/journal.pone.0312798 · Cited by 4
Identification of Two Distinct Stereoselective Lysine 5‐Hydroxylases by Genome Mining Based on Alazopeptin Biosynthetic Enzymes
Kawai, S., Moriga, K., Nirdnoy, W., Hara, R., Ogawa, J., Katsuyama, Y., & Ohnishi, Y. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202404790 · Cited by 4
Designing Epigenome Editors: Considerations of Biochemical and Locus Specificities
Sen, D., & Keung, A. J. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7774-1_3 · Cited by 4
The Pliable Genome: Epigenomics of Norway Spruce
Yakovlev, I., Viejo, M. D., & Fossdal, C. G. (2020) · Compendium of plant genomes · doi:10.1007/978-3-030-21001-4_5 · Cited by 4
Jumonji family histone demethylases in Epinephelus coioides gonad
Zhang, J., Yu, Z., Zhang, W., Shi, H., Tao, M., Chen, J., Liu, Y., Zhao, M., Li, S., Zhang, Y., et al. (2021) · Reproduction and Breeding · doi:10.1016/j.repbre.2021.02.002 · Cited by 4
Self-citation
Molecular Cloning and Expression Responses of Jarid2b to High-Temperature Treatment in Nile Tilapia (Oreochromis niloticus)
Zhou, M., Yao, Z., Zhao, M., Fang, Q., Ji, X. S., Chen, H., & Zhao, Y. (2022) · Genes · doi:10.3390/genes13101719 · Cited by 4
Genome-wide identification and expression analysis of JmjC domain-containing gene family related to abiotic stress and photoperiodic treatments in Mung bean (Vignaradiata L.)
Li, M., Ding, D., Zhang, Y., Liu, J., Cai, D., Cao, L., Chen, J., & Yang, S. (2023) · Ciência Rural · doi:10.1590/0103-8478cr20220241 · Cited by 4
Self-citation
JMJD6 functions as an oncogene and is associated with poor prognosis in esophageal squamous cell carcinoma
Liu, H., Jiang, M., Ma, F., Qin, J., Zhou, X., Xu, L., Yan, X., & Jiang, T. (2023) · BMC Cancer · doi:10.1186/s12885-023-11171-z · Cited by 4
Prohexadione, a plant growth regulator, inhibits histone lysine demethylases and modulates epigenetics
Vavilala, D. T., Reddy, S., Sachchidanand, Prakash, S., Ponnaluri, V. K. C., Kumar, A., & Mukherji, M. (2014) · Toxicology Reports · doi:10.1016/j.toxrep.2014.10.026 · Cited by 4
Clinical Epigenetics of Lung Cancer
Langevin, S. M., & Kelsey, K. T. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-800802-7.00005-8 · Cited by 4
Hairless regulates p53 target genes to exert tumor suppressive functions in glioblastoma
Brook, L., Palade, P., Maatough, A., Whitfield, G. K., Emeterio, L. S., Hsieh, D., & Hsieh, J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27408 · Cited by 4
Silencing and anti-silencing mechanisms that shape the epigenome in plants
Inagaki, S. (2021) · Genes & Genetic Systems · doi:10.1266/ggs.21-00041 · Cited by 4

Authors: Klose, R. J., Kallin, E. M., & Zhang, Y.
Affiliations: University of North Carolina at Chapel Hill (US)
Corresponding author: Zhang, Yi
ORCID: Klose, Robert J.
Zhang, Yi
Venue: Nature Reviews Genetics
Publisher: Springer Science and Business Media LLC
Published: 2006-09
Volume: 7
Issue: 9
Pages: 715-727
ISSN: 1471-0056 (ISSN-L)
1471-0064
DOI: 10.1038/nrg1945
OpenAlex: W1982409009
Cited by: 1,290
References: 106
Citations by year: 2026: 40 · 2025: 47 · 2024: 53 · 2023: 69 · 2022: 57 · 2021: 83 · 2020: 64 · 2019: 73 · 2018: 84 · 2017: 58 · 2016: 66 · 2015: 83 · 2014: 80 · 2013: 57 · 2012: 68
FWCI: 4.01
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Genetics (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: Jumonji C domain, histone demethylation, histone methylation, chromatin modification, epigenetic inheritance, protein evolution, gene expression regulation
MeSH terms: Histone Methyltransferases, Amino Acid Sequence, Animals, Gene Expression Regulation, Histones, Humans, Molecular Sequence Data, Nuclear Proteins, Oxidoreductases, N-Demethylating, Phylogeny, Histone-Lysine N-Methyltransferase, Protein Methyltransferases, Transcription, Genetic, Sequence Alignment, Protein Structure, Tertiary, Amino Acid Motifs, Epigenesis, Genetic

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

JmjC-domain-containing proteins and histone demethylation

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