The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
JMJD6 Is a Histone Arginine Demethylase
Abstract
Arginine methylation occurs on a number of proteins involved in a variety of cellular functions. Histone tails are known to be mono- and dimethylated on multiple arginine residues where they influence chromatin remodeling and gene expression. To date, no enzyme has been shown to reverse these regulatory modifications. We demonstrate that the Jumonji domain–containing 6 protein (JMJD6) is a JmjC-containing iron- and 2-oxoglutarate–dependent dioxygenase that demethylates histone H3 at arginine 2 (H3R2) and histone H4 at arginine 3 (H4R3) in both biochemical and cell-based assays. These findings may help explain the many developmental defects observed in the JMJD6 –/– knockout mice.
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Cites
The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
Nash, T. (1953) · Biochemical Journal · doi:10.1042/bj0550416 · Cited by 4,371
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument-Bromage, H., Warren, M. E., Borchers, C. H., Tempst, P., & Zhang, Y. (2006) · Nature · doi:10.1038/nature04433 · Cited by 2,163
Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550
Self-citationA receptor for phosphatidylserine-specific clearance of apoptotic cells
Fadok, V. A., Bratton, D. L., Rose, D. M., Pearson, A., Ezekewitz, R. A. B., & Henson, P. M. (2000) · Nature · doi:10.1038/35011084 · Cited by 1,491
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., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiacovo, M., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.028 · Cited by 1,040
Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination
Wang, Y., Wysocka, J., Sayegh, J., Lee, Y.-H., Perlin, J. R., Leonelli, L., Sonbuchner, L. S., McDonald, C. H., Cook, R. G., Dou, Y., et al. (2004) · Science · doi:10.1126/science.1101400 · Cited by 1,010
Histone Deimination Antagonizes Arginine Methylation
Cuthbert, G. L., Daujat, S., Snowden, A. W., Erdjument-Bromage, H., Hagiwara, T., Yamada, M., Schneider, R., Gregory, P. D., Tempst, P., Bannister, A. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.08.020 · Cited by 839
Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y.-M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200273200 · Cited by 719
Iwase, S., Lan, F., Bayliss, P., 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 692
Cited by
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials
Cheng, Y., He, C., Wang, M., Ma, X., Mo, F., Yang, S., Han, J., & Wei, X. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0095-0 · Cited by 1,097
Protein arginine methyltransferases and cancer
Yang, Y., & Bedford, M. T. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3409 · Cited by 1,083
Rahman, S., Sowa, M. E., Ottinger, M., Smith, J. A., Shi, Y., Harper, J. W., & Howley, P. M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01341-10 · Cited by 532
Metadata
- Authors
- Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K.
- Venue
- Science
- Published
- 2007-10-19
- Volume
- 318
- Issue
- 5849
- Pages
- 444-447
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2081204899
- Cited by
- 745
- References
- 28
- FWCI
- 15.45
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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