The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics
Link
http://www.nature.com/articles/ng1627.pdf
Reference28 articles.
1. Cantor, S.B. et al. BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell 105, 149–160 (2001).
2. Yu, X., Chini, C.C., He, M., Mer, G. & Chen, J. The BRCT domain is a phospho-protein binding domain. Science 302, 639–642 (2003).
3. Cantor, S. et al. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc. Natl. Acad. Sci. USA 101, 2357–2362 (2004).
4. Williams, R.S., Lee, M.S., Hau, D.D. & Glover, J.N. Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. Nat. Struct. Mol. Biol. 11, 519–525 (2004).
5. Clapperton, J.A. et al. Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat. Struct. Mol. Biol. 11, 512–518 (2004).
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