Structural requirements for the BARD1 tumor suppressor in chromosomal stability and homology-directed DNA repair.

@article{Laufer2007StructuralRF,
  title={Structural requirements for the BARD1 tumor suppressor in chromosomal stability and homology-directed DNA repair.},
  author={Marsha Laufer and Subhadra V. Nandula and Ami P Modi and Shuang Wang and Maria Jasin and V. V. S. Murty and Thomas Ludwig and Richard D. Baer},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 47},
  pages={
          34325-33
        }
}
The BRCA1 tumor suppressor exists as a heterodimeric complex with BARD1, and this complex is thought to mediate many of the functions ascribed to BRCA1, including its role in tumor suppression. The two proteins share a common structural organization that features an N-terminal RING domain and two C-terminal BRCT motifs, whereas BARD1 alone also contains three tandem ankyrin repeats. In normal cells, the BRCA1/BARD1 heterodimer is believed to enhance chromosome stability by promoting homology… CONTINUE READING
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E3 ligase activity of BRCA1 is not essential for mammalian cell viability or homology-directed repair of double-strand DNA breaks.

Proceedings of the National Academy of Sciences of the United States of America • 2008
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