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"BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function." |
Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM |
Published April 6, 2001 in Cell volume 105 .
Pubmed ID: 11301010
Abstract:
| BRCA1 interacts in vivo with a novel protein, BACH1, a member of the DEAH helicase family. BACH1 binds directly to the BRCT repeats of BRCA1. A BACH1 derivative, bearing a mutation in a residue that was essential for catalytic function in other helicases, interfered with normal double-strand break repair in a manner that was dependent on its BRCA1 binding function. Thus, BACH1/BRCA1 complex formation contributes to a key BRCA1 activity. In addition, germline BACH1 mutations affecting the helicase domain were detected in two early-onset breast cancer patients and not in 200 matched controls. Thus, it is conceivable that, like BRCA1, BACH1 is a target of germline cancer-inducing mutations. |
This publication refers to following REPAIRtoire entries:
| Genes | |
| Proteins |
Last modification of this entry: Oct. 6, 2010
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