Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A.

@article{Cui2004AnalysisOT,
  title={Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A.},
  author={Sheng Cui and Daniele Arosio and Kevin M. Doherty and Robert M. Brosh and A. Falaschi and Alessandro Vindigni},
  journal={Nucleic acids research},
  year={2004},
  volume={32 7},
  pages={2158-70}
}
RecQ helicases are required for the maintenance of genome stability. Characterization of the substrate specificity and identification of the binding partners of the five human RecQ helicases are essential for understanding their function. In the present study, we have developed an efficient baculovirus expression system that allows us to obtain milligram quantities of recombinant RECQ1. Our gel filtration and dynamic light scattering experiments show that RECQ1 has an apparent molecular mass of… CONTINUE READING
38 Citations
70 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 38 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 70 references

Similar Papers

Loading similar papers…