Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294-Reference-Cited by-同舟云学术

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Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

Published:2009-02-15 Issue:3 Volume:16 Page:312-317
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Chang Yanqi,Zhang Xing,Horton John R,Upadhyay Anup K,Spannhoff Astrid,Liu Jin,Snyder James P,Bedford Mark T,Cheng Xiaodong

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.1560.pdf

Reference37 articles.

1. Jenuwein, T. The epigenetic magic of histone lysine methylation. FEBS J. 273, 3121–3135 (2006).

2. Grewal, S.I. & Jia, S. Heterochromatin revisited. Nat. Rev. Genet. 8, 35–46 (2007).

3. Tachibana, M. et al. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16, 1779–1791 (2002).

4. Tachibana, M. et al. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3–K9. Genes Dev. 19, 815–826 (2005).

5. McGarvey, K.M. et al. Silenced tumor suppressor genes reactivated by DNA demethylation do not return to a fully euchromatic chromatin state. Cancer Res. 66, 3541–3549 (2006).

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