The DOI matches its Crossref record; 24 of the 25 references it cites were found in a registry or an index.
KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
Open accessAbstract
Methylation of histone H3 Lys 9 and Lys 27 (H3K9 and H3K27) is associated with transcriptional silencing. Here we show that KDM7, a JmjC domain-containing protein, catalyzes demethylation of both mono- or dimethylated H3K9 and H3K27. Inhibition of KDM7 orthologs in zebrafish resulted in developmental brain defects. KDM7 interacts with the follistatin gene locus, and KDM7 depletion in mammalian neuronal cells suppressed follistatin gene transcription in association with increased levels of dimethylated H3K9 and H3K27. Our findings identify KDM7 as a dual demethylase for H3K9 and H3K27 that functions as an eraser of silencing marks on chromatin during brain development.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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
“KDM7A (encoding Lysine Demethylase 7A), which plays a central role in the nervous system and midbrain development (Horton et al., 2010; Qi et al., 2010; Tsukada et al., 2010).”
From Genomic Relationships, Novel Loci, and Pleiotropic Mechanisms across Eight Psychiatric Disorders (2019) · cites this paper as Tsukada et al., 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Self-citationThe 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
Hemmati‐Brivanlou, A., Kelly, O., & Melton, D. A. (1994) · Cell · doi:10.1016/0092-8674(94)90320-4 · Cited by 761
Dynamic Regulation of Histone Lysine Methylation by Demethylases
Shi, Y., & Whetstine, J. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.010 · Cited by 720
Iwase, S., Lan, F., Bayliss, P. E., de la Torre-Ubieta, L., Huarte, M., Qi, H. H., Whetstine, J. R., Bonni, A., Roberts, T. M., & Shi, Y. (2007) · Cell · doi:10.1016/j.cell.2007.02.017 · Cited by 712
Erasing the methyl mark: histone demethylases at the center of cellular differentiation and diseasePreprint
Cloos, P. A., Christensen, J., Agger, K., & Helin, K. (2008) · Genes & Development · doi:10.1101/gad.1652908 · Cited by 679
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
Klose, R. J., Yamane, K., Bae, Y., Zhang, D., Erdjument‐Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006) · Nature · doi:10.1038/nature04853 · Cited by 648
An epigenetic road map for histone lysine methylation
Lachner, M., O’Sullivan, R. J., & Jenuwein, T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00493 · Cited by 641
Bannister, A. J., Schneider, R., & Kouzarides, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00798-5 · Cited by 560
Mechanisms involved in the regulation of histone lysine demethylases
Lan, F., Nottke, A. C., & Shi, Y. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.004 · Cited by 241
Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate
Laumonnier, F., Holbert, S., Ronce, N., Faravelli, F., Lenzner, S., Schwartz, C. E., Lespinasse, J., Esch, H. V., Lacombe, D., Goizet, C., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2004.029439 · Cited by 218
HuC:Kaede, a useful tool to label neural morphologies in networks in vivo
Sato, T., Takahoko, M., & Okamoto, H. (2006) · genesis · doi:10.1002/gene.20196 · Cited by 158
Regulation of ovarian function by the TGF-β superfamily and follistatin
Lin, S., Morrison, Phillips, D., & de Kretser, D. (2003) · Reproduction · doi:10.1530/rep.0.1260133 · Cited by 117
Abidi, F., Miano, M. G., Murray, J., & Schwartz, C. (2007) · Clinical Genetics · doi:10.1111/j.1399-0004.2007.00817.x · Cited by 103
Koivisto, A. M., Ala‐Mello, S., Lemmelä, S. M., Komu, H., Rautio, J., & Järvelä, I. E. (2007) · Clinical Genetics · doi:10.1111/j.1399-0004.2007.00836.x · Cited by 85
Zhu, C. C., Boone, J. Q., Jensen, P. A., Hanna, S., Podemski, L., LOCKE, J. L., Doe, C. Q., & O’Connor, M. B. (2008) · Development · doi:10.1242/dev.010876 · Cited by 77
PHF2, a novel PHD finger gene located on human Chromosome 9q22
Hasenpusch‐Theil, K., Chadwick, B. P., Theil, T., Heath, S. K., Wilkinson, D. G., & Frischauf, A. (1999) · Mammalian Genome · doi:10.1007/s003359900989 · Cited by 33
Flagged first, then by citations
1 of the 25 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Genomic Relationships, Novel Loci, and Pleiotropic Mechanisms across Eight Psychiatric Disorders
Lee, P. H., Anttila, V., Won, H., Feng, Y.-C. A., Rosenthal, J., Zhu, Z., Tucker-Drob, E. M., Nivard, M. G., Grotzinger, A. D., Posthuma, D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.11.020 · Cited by 1,381
“The brain Hi-C data indicated interaction of the associated region with the promoters of two nearby genes:BRAF, which contributes to theMAP kinase signal transduction pathway and plays a role in postsynaptic responses of hippocampal neurons (Grantyn and Grantyn, 1973), and KDM7A (encoding Lysine Demethylase 7A), which…”
BackgroundMolecular mechanisms and potential functions of histone demethylases
Kooistra, S. M., & Helin, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3327 · Cited by 913
2-Oxoglutarate-Dependent Oxygenases
Islam, M. S., Leissing, T. M., Chowdhury, R., Hopkinson, R. J., & Schofield, C. J. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044724 · Cited by 472
Histone demethylases in development and disease
Pedersen, M. T., & Helin, K. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.08.011 · Cited by 389
Miller, S. A., Mohn, S. E., & Weinmann, A. S. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.028 · Cited by 373
Metadata
- Authors
- Tsukada, Y.-I., Ishitani, T., & Nakayama, K. I.
- Affiliations
- Kyushu University (JP)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-03-01
- Volume
- 24
- Issue
- 5
- Pages
- 432-437
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2827838
- OpenAlex
- W2116387269
- Cited by
- 158
- References
- 25
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 7 · 2023: 15 · 2022: 6 · 2021: 15 · 2020: 7 · 2019: 11 · 2018: 7 · 2017: 11 · 2016: 5 · 2015: 14 · 2014: 16 · 2013: 3 · 2012: 13
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (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
- histone demethylase, H3K9 demethylation, H3K27 demethylation, JmjC domain, brain development, transcriptional silencing, follistatin, zebrafish, neurons, histone methylation
- MeSH terms
- Animals, Brain, Cells, Cultured, Embryo, Nonmammalian, Histones, Neurons, Zebrafish, Gene Expression Regulation, Developmental, Zebrafish Proteins, Follistatin, Mice, Jumonji Domain-Containing Histone Demethylases
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