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Science 302 (5645): 579-580

Copyright © 2003 by the American Association for the Advancement of Science

CELL SIGNALING:
The BRCT Domain: Signaling with Friends?

Keith W. Caldecott

The tandem BRCT domains of the tumor suppressor protein BRCA1 are thought to contribute to this protein's function in the cellular response to DNA damage. In his Perspective, Caldecott discusses new work (Yu et al., Manke et al.) showing that the BRCT domains of BRCA1 and of other proteins bind specifically to phosphorylated amino acids in their protein partners.


The author is at the Genome Damage and Stability Center, University of Sussex, Brighton BN1 9RR, UK. E-mail: k.w.caldecott{at}sussex.ac.uk


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Structure of the DNA-bound BRCA1 C-terminal Region from Human Replication Factor C p140 and Model of the Protein-DNA Complex.
M. Kobayashi, E. AB, A. M. J. J. Bonvin, and G. Siegal (2010)
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PTIP Regulates 53BP1 and SMC1 at the DNA Damage Sites.
J. Wu, M. J. Prindle, G. R. Dressler, and X. Yu (2009)
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The Mre11-Rad50-Nbs1 Complex Mediates Activation of TopBP1 by ATM.
H. Y. Yoo, A. Kumagai, A. Shevchenko, A. Shevchenko, and W. G. Dunphy (2009)
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Viral Transport of DNA Damage That Mimics a Stalled Replication Fork.
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Claspin and the Activated Form of ATR-ATRIP Collaborate in the Activation of Chk1.
A. Kumagai, S.-M. Kim, and W. G. Dunphy (2004)
J. Biol. Chem. 279, 49599-49608
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Genetic Steps of Mammalian Homologous Repair with Distinct Mutagenic Consequences.
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Mol. Cell. Biol. 24, 9305-9316
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