The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
H3K9 methyltransferase G9a and the related molecule GLP
Open accessAbstract
The discovery of Suv39h1, the first SET domain-containing histone lysine methyltransferase (HKMT), was reported in 2000. Since then, research on histone methylation has progressed rapidly. Among the identified HKMTs in mammals, G9a and GLP are the primary enzymes for mono- and dimethylation at Lys 9 of histone H3 (H3K9me1 and H3K9me2), and exist predominantly as a G9a–GLP heteromeric complex that appears to be a functional H3K9 methyltransferase in vivo. Recently, many important studies have reported that G9a and GLP play critical roles in various biological processes. The physiological relevance of G9a/GLP-mediated epigenetic gene regulation is discussed.
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Citations
Cites
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845 · cited 1×
“Genomewide analysis of different histone modifications suggests that the H3K9me2 mark is linked with transcriptional repression (Barski et al. 2007).”
BackgroundHistone 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
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Regulation of chromatin structure by site-specific histone H3 methyltransferases
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“Since the Su(var)3-9–Enhancer of zeste–Trithorax (SET) domain of Suv39h1/KMT1a was demonstrated to be the catalytic domain for lysine methylation (Rea et al. 2000), many SET domain-containing molecules have been found to be novel histone lysine methyltransferases (HKMTs) in various species,…”
BackgroundHistone 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
Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions
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UHRF1 Plays a Role in Maintaining DNA Methylation in Mammalian Cells
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The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA
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Self-citation
Cited by
DNA methylation pathways and their crosstalk with histone methylation
Du, J., Johnson, L. M., Jacobsen, S. E., & Patel, D. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4043 · Cited by 1,000
Single-Cell Dynamics of Genome-Nuclear Lamina Interactions
Kind, J., Pagie, L., Ortabozkoyun, H., Boyle, S., de Vries, S. S., Janssen, H., Amendola, M., Nolen, L. D., Bickmore, W. A., & van Steensel, B. (2013) · Cell · doi:10.1016/j.cell.2013.02.028 · Cited by 727
Epigenetic reprogramming in cancer
Suvà, M. L., Riggi, N., & Bernstein, B. E. (2013) · Science · doi:10.1126/science.1230184 · Cited by 706
Epigenetic modifications of histones in cancer
Zhao, Z., & Shilatifard, A. (2019) · Genome Biology · doi:10.1186/s13059-019-1870-5 · Cited by 552
Guo, L., Li, X., & Tang, Q.-Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.619957 · Cited by 353
Metadata
- Authors
- Shinkai, Y., & Tachibana, M.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-04-15
- Volume
- 25
- Issue
- 8
- Pages
- 781-788
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2095626300
- Cited by
- 558
- References
- 88
- Type
- posted content
- Language
- en
- Open access
- diamond
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