The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
EZH2: biology, disease, and structure-based drug discovery
Open accessAbstract
EZH2 is the catalytic subunit of the polycomb repressive complex 2 (PRC2), which is a highly conserved histone methyltransferase that methylates lysine 27 of histone 3. Overexpression of EZH2 has been found in a wide range of cancers, including those of the prostate and breast. In this review, we address the current understanding of the oncogenic role of EZH2, including its PRC2-dependent transcriptional repression and PRC2-independent gene activation. We also discuss the connections between EZH2 and other silencing enzymes, such as DNA methyltransferase and histone deacetylase. We comprehensively address the architecture of the PRC2 complex and the crucial roles of each subunit. Finally, we summarize new progress in developing EZH2 inhibitors, which could be a new epigenetic therapy for cancers.
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Cites
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
The polycomb group protein EZH2 is involved in progression of prostate cancer
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Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
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EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer.
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Self-citationA selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
Knutson, S. K., Wigle, T. J., Warholic, N. M., Sneeringer, C. J., Allain, C. J., Klaus, C. R., Sacks, J. D., Raimondi, A., Majer, C. R., Song, J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1084 · Cited by 776
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Chemical mechanisms of histone lysine and arginine modifications
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Structural Biology of Human H3K9 Methyltransferases
Wu, H., Min, J., Lunin, V. V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C. H., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008570 · Cited by 268
Cited by
Hydrocarbon Stapled Peptides as Modulators of Biological Function
Cromm, P. M., Spiegel, J., & Grossmann, T. N. (2015) · ACS Chemical Biology · doi:10.1021/cb501020r · Cited by 290
Metadata
- Authors
- Tan, J.-Z., Yan, Y., Wang, X.-X., Jiang, Y., & Xu, H. E.
- Venue
- Acta Pharmacologica Sinica
- Published
- 2013-12-23
- Volume
- 35
- Issue
- 2
- Pages
- 161-174
- ISSN
- 0253-9756 (ISSN-L)
- 1671-4083
- 1745-7254
- OpenAlex
- W2094051261
- Cited by
- 234
- References
- 10
- FWCI
- 6.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tan, J.-Z., Yan, Y., Wang, X.-X., Jiang, Y., & Xu, H. E. (2014). EZH2: biology, disease, and structure-based drug discovery. Acta Pharmacologica Sinica. https://doi.org/10.1038/aps.2013.161
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
