KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679

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

Histone demethylation by a family of JmjC domain-containing proteins

Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,244

The diverse functions of histone lysine methylation

Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,157

JmjC-domain-containing proteins and histone demethylation

Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290

Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases

Whetstine, J. R., Nottke, A. C., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiácovo, M. P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.028 · Cited by 1,075

p53 Activation by Knockdown Technologies

Robu, M. E., Larson, J. D., Nasevicius, A., Beiraghi, S., Brenner, C., Farber, S. A., & Ekker, S. C. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0030078 · Cited by 1,049

New nomenclature for chromatin-modifying enzymes

Allis, C. D., Berger, S. L., Cote, J., Dent, S., Jenuwien, T., Kouzarides, T., Pillus, L., Reinberg, D., Shi, Y., Shiekhattar, R., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.039 · Cited by 957

The key to development: interpreting the histone code?

Margueron, R., Trojer, P., & Reinberg, D. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.01.005 · Cited by 770

Follistatin, an antagonist of activin, is expressed in the Spemann organizer and displays direct neuralizing activity

Hemmati‐Brivanlou, A., Kelly, O., & Melton, D. A. (1994) · Cell · doi:10.1016/0092-8674(94)90320-4 · Cited by 761

PHF8/KDM7B: A Versatile Histone Demethylase and Epigenetic Modifier in Nervous System Disease and Cancers

Fan, T., Xie, J., Huang, G. C., Li, L., Zeng, X., & Tao, Q. (2024) · Epigenomes · doi:10.3390/epigenomes8030036 · Cited by 13

Lysine demethylase 7a regulates murine anterior-posterior development by modulating the transcription of Hox gene cluster

Higashijima, Y., Nagai, N., Yamamoto, M., Kitazawa, T., Kawamura, Y., Taguchi, A., Nakada, N., Nangaku, M., Furukawa, T., Aburatani, H., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01456-5 · Cited by 13

Expression profiles of histone lysine demethylases during cardiomyocyte differentiation of mouse embryonic stem cells

Tang, Y., Chen, Z., Hong, Y., Wu, Q., Lin, H., Chen, C. D., & Yang, H. (2014) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.40 · Cited by 13

Decreased expression of JHDMID in placenta is associated with preeclampsia through HLA-G

Shouling, L. U. O., Pei, J., Li, X., & Gu, W. (2018) · Journal of Human Hypertension · doi:10.1038/s41371-018-0062-1 · Cited by 13

Epigenetic regulation of stemness maintenance in the neurogenic niches

Montalbán-Loro, R. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i4.700 · Cited by 15

Lysine-specific demethylase 7A (KDM7A): A potential target for disease therapy

Li, C.-Y., Liu, Y., Tao, F., Chen, R.-Y., Shi, J.-J., Lu, J., Yang, G., & Chen, J. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115799 · Cited by 12

The histone demethylase PHF8 regulates astrocyte differentiation and function

Iacobucci, S., Padilla, N., Gabrielli, M., Navarro, C., Lombardi, M., Vicioso‐Mantis, M., Verderio, C., de la Cruz, X., & Martínez‐Balbás, M. A. (2021) · Development · doi:10.1242/dev.194951 · Cited by 12

KDM6A/UTX promotes spermatogenic gene expression across generations and is not required for male fertility

Walters, B. W., Rainsford, S. R., Heuer, R. A., Dias, N., Huang, X., de Rooij, D. G., & Lesch, B. J. (2023) · Biology of Reproduction · doi:10.1093/biolre/ioad141 · Cited by 13

Histone Demethylase Modulation: Epigenetic Strategy to Combat Cancer Progression

Srivastava, R., Singh, R., Jauhari, S., Lodhi, N., & Srivastava, R. (2023) · Epigenomes · doi:10.3390/epigenomes7020010 · Cited by 12

Leveraging genetic overlap between irritability and psychiatric disorders to identify genetic variants of major psychiatric disorders

Jung, K., Yoon, J., Ahn, Y., Kim, S., Shim, I., Ko, H., Jung, S., Kim, J., Kim, H. J., Lee, D. J., et al. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01005-0 · Cited by 11

Histone modifications controlling native and induced neural stem cell identity

Broccoli, V., Colasante, G., Sessa, A., & Rubio, A. (2015) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2015.08.003 · Cited by 11

Cross-Talk Between Histone Methyltransferases and Demethylases Regulate REST Transcription During Neurogenesis

Swaminathan, J., Maegawa, S., Shaik, S., Sharma, A., Bravo-Alegria, J. B., Guo, L. M., Xu, L., Harmanci, A. O., & Gopalakrishnan, V. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.855167 · Cited by 10

Histone demethylases in autophagy and inflammation

Ma, Y., Lv, W., Guo, Y. C., Yin, T., Bai, Y., Liu, Z., Chen, C., WenjuanYang, Feng, J., Qian, W., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-024-02006-w · Cited by 11

Basic Epigenetic Mechanisms

Davie, J., Sattarifard, H., Sudhakar, S. R. N., Roberts, C.-T., Beacon, T. H., Muker, I., Shahib, A. K., & Rastegar, M. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-75980-2_1 · Cited by 12

DNA methylation and histone modifications are essential for regulation of stem cell formation and differentiation in zebrafish development

Marchione, A. D., Thompson, Z., & Kathrein, K. L. (2021) · Briefings in Functional Genomics · doi:10.1093/bfgp/elab022 · Cited by 10

The Role of Histone Methylation and Methyltransferases in Gene Regulation

Cui, J. Y., Fu, Z. D., & Dempsey, J. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812433-8.00002-2 · Cited by 11

The Lysine Demethylase KDM7A Regulates Immediate Early Genes in Neurons

Wang, Y., Hong, Q., Xia, Y., Zhang, Z., & Wen, B. (2023) · Advanced Science · doi:10.1002/advs.202301367 · Cited by 8

Chromatin Modification in Zebrafish Development

Cayuso, J., Noël, E. S., & Ober, E. A. (2011) · Methods in cell biology · doi:10.1016/b978-0-12-374814-0.00022-7 · Cited by 9

Identification of novel TGF-β regulated genes with pro-migratory roles

Liu, Q., Borcherding, N. C., Shao, P., Cao, H., Zhang, W., & Qi, H. H. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165537 · Cited by 9

In Vitro Histone Demethylase Assays

Kokura, K., Sun, L., & Fang, J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2474-5_8 · Cited by 9

Regulation of histone H3 lysine 9 methylation in inflammation

Ren, X., Wang, R., Yu, X., Cai, B., & Guo, F. (2021) · All Life · doi:10.1080/26895293.2021.1931477 · 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

Epigenetic regulation of myogenesis by vitamin C

Takeuchi, S. Y., Dusadeemeelap, C., Kawamoto, T., Matsubara, T., Kokabu, S., & Addison, W. N. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31472 · Cited by 7

Prolonged Inhibition of the MEK1/2-ERK Signaling Axis Primes Interleukin-1 Beta Expression through Histone 3 Lysine 9 Demethylation in Murine Macrophages

Low, R., Ha, S.-D., Sleapnicov, N., Maneesh, P., & Kim, S. O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914428 · Cited by 7

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

The Histone Lysine Demethylase KDM7A Contributes to Reward Memory via Fscn1‐Induced Synaptic Plasticity in the Medial Prefrontal Cortex

Yang, Z., Yu, D., Gao, F., Zhou, D., Wu, Y., Yang, X., Chen, J., Yang, J., Shen, M., Zhang, Y.-X., et al. (2025) · Advanced Science · doi:10.1002/advs.202405352 · Cited by 7

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

vp1524, a Vibrio parahaemolyticus NAD +-dependent deacetylase, regulates host response during infection by induction of host histone deacetylation

Mishra, P., Beura, S., Sikder, S., Dhal, A. K., Vasudevan, M., Roy, M., Rakshit, J., Budhwar, R., Kundu, T. K., & Modak, R. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac027 · 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

Identification of family determining residues in J umonji‐C lysine demethylases: A sequence‐based, family wide classification

Slama, P. S. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24986 · Cited by 4

Histone demethylases regulate ferroptosis in metabolic dysfunction‐associated steatotic liver disease via epigenetic modification

Huang, W., Wu, W., Xiao, J., Bai, Y., Chen, C., Ou, H., Ma, Y., Que, X., Shan, S., Qu, L., et al. (2025) · FEBS Journal · doi:10.1111/febs.70351 · Cited by 3

Volatile Organic Compounds of some Antagonists against Lasiodiplodia theobromae, a Pathogen of Coconut

Sudha, A., Rajesh, M., Kumar, M. S., Vijayakumar, M., & Sumathi, E. (2021) · International Journal of Agriculture and Biology · doi:10.17957/ijab/15.1889 · Cited by 3

Kdm7a expression is spatiotemporally regulated in developing Xenopus laevis embryos, and its overexpression influences late retinal development

Martini, D., Digregorio, M., Voto, I. A. P., Morabito, G., Degl’Innocenti, A., Giudetti, G., Giannaccini, M., & Andreazzoli, M. (2023) · Developmental Dynamics · doi:10.1002/dvdy.670 · Cited by 3

The silent guardian: unraveling the roles of H3K9me3 in genome maintenance

Li, Z., & Zhang, Z. (2024) · Genome Instability & Disease · doi:10.1007/s42764-024-00131-x · Cited by 3

Histone and DNA Methylome in Neurodegenerative, Neuropsychiatric and Neurodevelopmental Disorders

Rani, H., & Mahadevan, V. (2019) · RNA technologies · doi:10.1007/978-3-030-14792-1_4 · Cited by 3

HAUSP Is a Key Epigenetic Regulator of the Chromatin Effector Proteins

Abdullah, O., & Alhosin, M. (2021) · Genes · doi:10.3390/genes13010042 · Cited by 3

The H3K27 Histone Demethylase Kdm6b (Jmjd3) is Induced by Neuronal Activity and Contributes to Neuronal Survival and Differentiation

Wijayatunge, R. (2012) · DukeSpace (Duke University) · Cited by 2

Loss of epe1+ extends chronological lifespan in Schizosaccharomyces pombe

Basu, S., Xu, Y., & Vo, T. V. (2025) · PubMed Central · doi:10.17912/micropub.biology.001507 · Cited by 1

Genomic landscapes of natural selection in great apes

Huang, X., Chen, S., Han, S., & Kuhlwilm, M. (2026) · Genome biology · doi:10.1186/s13059-026-04247-z · Cited by 1

Extreme-phenotype genome-wide association study of growth traits in golden pompano (Trachinotus blochii) and implications for genomic selection

Bu, S., Zheng, D., 冉春丽, Sun, J., Shen, H., & Luo, J. (2026) · Aquaculture Reports · doi:10.1016/j.aqrep.2026.103659 · Cited by 1

The Histone Demethylase PHF8 and Neural Development*

Guo, X., Shen, Y., Bei, L. I. U., Chang, Y., & Duan, X. (2011) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2010.00390 · Cited by 1

Histone demethylases JHDM1D, PHF2 and PHF8 expression pattern in granulosa cells obtained from patients undergoing IVF procedure during short-term IVC

Bryl, R., Stefańska, K., Chermuła, B., Stelmach, B., Pieńkowski, W., Kulus, J., Perek, J., Wieczorkiewicz, M., Wąsiatycz, G., Ratajczak, K., et al. (2021) · Medical Journal of Cell Biology · doi:10.2478/acb-2021-0001 · Cited by 1

Epigenetics in Brain Development and Disease

Radford, E. J., Ferguson‐Smith, A. C., & Ferrón, S. R. (2017) · Wiley eBooks · doi:10.1002/9781118540770.ch14 · Cited by 1

Quiescence induces epigenetic changes in bovine fibroblasts and improves their reprogramming into cloned embryos

Kallingappa, P. K. (2013) · Research Commons (University of Waikato)

Targeting Non-Acetylation Histone Erasers

Lu, F., & Zhang, H. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782628484-00168

Development and Evaluation of Chemical Probes for the Study of Histone Demethylases

Marholz, L. J. (2015) · CU Scholar (University of Colorado Boulder)

Epigenetics

Pepin, J. T., Cárdenas, H., Nephew, K. P., & Matei, D. E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803741-6.00003-3

[The Role of Histone Demethylase in Osteogenic and Chondrogenic Differentiation of Mesenchymal Stem Cells: A Literature Review].

Sui, H., & Zhang, T. (2021) · PubMed Central · doi:10.12182/20210560202

KDM6A/UTX promotes spermatogenic gene expression across generations but is dispensable for male fertilityPreprint

Walters, B. W., Rainsford, S. R., Dias, N., Huang, X., de Rooij, D. G., & Lesch, B. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.27.513976

Histone Demethylases

Kales, S. C., & Simeonov, A. M. (2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837674916-00383

Drug Discovery for Chromatin Readers, Writers, Erasers, Remodelers and Epitranscriptomic Targets

(2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837674916-part3

Additional file 1 of Glutamate regulates gliosis of BMSCs to promote ENS regeneration through α-KG and H3K9/H3K27 demethylation

Fan, M., Shi, H., Yao, H., Wang, W., Zhang, Y., Jiang, C., & Lin, R. (2022) · Figshare · doi:10.6084/m9.figshare.20098517

Additional file 2 of Glutamate regulates gliosis of BMSCs to promote ENS regeneration through α-KG and H3K9/H3K27 demethylation

Fan, M., Shi, H., Yao, H., Wang, W., Zhang, Y., Jiang, C., & Lin, R. (2022) · Figshare · doi:10.6084/m9.figshare.20098520

Epigenetic landscape of normal and malignant lympho-hematopoiesis : interplays between chromatin signature and tissue specific gene expression

Pękowska, A. (2011) · theses.fr (ABES) · doi:10.70675/dd2d7d5ezf8abz4452z9c93zdcd5d852abf1

Genome-wide identification and expression analysis of lysine-specific demethylase (KDM) genes in the echiuran worm Urechis unicinctus and the association of Jumonji domain containing 6 (Jmjd6) with antioxidant defense

Yang, Z., Wu, M., & Mao, Q. (2026) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2026.111288

Neuronal activity-regulated histone demethylase KDM7A controls hippocampal gene expression and behavior

Paraíso‐Luna, J., Niñerola, S., Scandaglia, M., López-Gómez, M. C., Martín-González, A., & Barco, Á. (2026) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2026.102957

BindingDB Entry 50020995: Exploring the potential of histone demethylase inhibition in multi-therapeutic approaches for cancer treatment.

BindingDB (2025) · UC San Diego · doi:10.7270/q2x35322

BindingDB Entry 50034383: Lysine demethylases inhibitors.

BindingDB (2012) · UC San Diego · doi:10.7270/q2d50nfr

BindingDB Entry 50046119: Identification of Jumonji AT-Rich Interactive Domain 1A Inhibitors and Their Effect on Cancer Cells.

BindingDB (2016) · UC San Diego · doi:10.7270/q2v69mc7

BindingDB Entry 50043384: Identification of the KDM2/7 histone lysine demethylase subfamily inhibitor and its antiproliferative activity.

BindingDB (2014) · UC San Diego · doi:10.7270/q2sb475v

Coordinated regulation of active and repressive histone methylations by a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans

Hanqing, Lin, L., Yiqin, Wang, Yanru, Feng, Tian, T., Pu, P., ̆, Y., yu, Y., et al. (2010) · Cell Research

KDM2B is a histone H3K79 demethylase and induces transcriptional repression via sirtuin‐1‐mediated chromatin silencing

Kang, J., Kim, J., Kim, K., Park, J. W., Cho, H., Hahm, J. Y., Chae, Y., Kim, D., Kook, H. Y., Rhee, S., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800242r · Cited by 103

The histone lysine demethylase KDM7A is required for normal development and first cell lineage specification in porcine embryos

Rissi, V. B., Glanzner, W. G., de Macedo, M. P., Gutierrez, K., Baldassarre, H., Gonçalves, P. B. D., & Bordignon, V. (2019) · Epigenetics · doi:10.1080/15592294.2019.1633864 · Cited by 18

Lysine-specific demethylase 7A (KDM7A): A potential target for disease therapy

Li, C.-Y., Liu, Y., Tao, F., Chen, R.-Y., Shi, J.-J., Lu, J., Yang, G., & Chen, J. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115799 · Cited by 12

Histone demethylases in neurodevelopment and neurodegenerative diseases

Wang, H., Guo, B., & Guo, X. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2023.2276656 · Cited by 13