A phosphatase complex that dephosphorylates γH2AX regulates DNA damage checkpoint recovery-Reference-Cited by-同舟云学术

A phosphatase complex that dephosphorylates γH2AX regulates DNA damage checkpoint recovery

Published:2005-11-20 Issue:7075 Volume:439 Page:497-501
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Keogh Michael-Christopher,Kim Jung-Ae,Downey Michael,Fillingham Jeffrey,Chowdhury Dipanjan,Harrison Jacob C.,Onishi Megumi,Datta Nira,Galicia Sarah,Emili Andrew,Lieberman Judy,Shen Xuetong,Buratowski Stephen,Haber James E.,Durocher Daniel,Greenblatt Jack F.,Krogan Nevan J.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature04384.pdf

Reference30 articles.

1. Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S. & Bonner, W. P. DNA double-strand breaks induce H2AX phosphorylation on serine 139. J. Biol. Chem. 273, 5858–5868 (1998)

2. Downs, J. A., Lowndes, N. F. & Jackson, S. P. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 408, 1001–1004 (2000)

3. Shroff, R. et al. Distribution and dynamics of chromatin modification at a defined DNA double strand break. Curr. Biol. 14, 1703–1711 (2004)

4. Nakamura, T. M., Du, L. L., Redon, C. & Russell, P. Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast. Mol. Cell. Biol. 24, 6215–6230 (2004)

5. Fernandez-Capetillo, O. et al. DNA-damage induced G2-M checkpoint activation by histone H2AX and 53BP1. Nature Cell Biol. 4, 993–997 (2002)

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