Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.

@article{Iwatani2006BiochemicalAO,
  title={Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect.},
  author={Yasumasa Iwatani and Hiroaki Takeuchi and Klaus Strebel and Judith G Levin},
  journal={Journal of virology},
  year={2006},
  volume={80 12},
  pages={5992-6002}
}
APOBEC3G (APO3G), a cytidine deaminase with two zinc finger domains, inhibits human immunodeficiency virus type 1 replication in the absence of Vif. Here, we provide a comprehensive molecular analysis of the deaminase and nucleic acid binding activities of human APO3G using a pure system containing only one protein component, i.e., highly purified, catalytically active enzyme expressed in a baculovirus system. We demonstrate that APO3G deaminates cytosines in single-stranded DNA (ssDNA) only… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 81 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 54 references

Similar Papers

Loading similar papers…