ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome-Reference-Cited by-同舟云学术

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ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome

Published:2011-06-12 Issue:7 Volume:18 Page:769-776
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Iwase Shigeki,Xiang Bin,Ghosh Sharmistha,Ren Ting,Lewis Peter W,Cochrane Jesse C,Allis C David,Picketts David J,Patel Dinshaw J,Li Haitao,Shi Yang

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2062.pdf

Reference55 articles.

1. Li, H. et al. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442, 91–95 (2006).

2. Wysocka, J. et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442, 86–90 (2006).

3. Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442, 96–99 (2006).

4. Peña, P.V. et al. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442, 100–103 (2006).

5. Bannister, A.J. et al. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410, 120–124 (2001).

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