In-Silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate

@article{Savarino2007InSilicoDO,
  title={In-Silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate},
  author={Andrea Savarino},
  journal={Retrovirology},
  year={2007},
  volume={4},
  pages={21 - 21}
}
BackgroundHIV-1 integrase (IN) is an emerging drug target, as IN strand transfer inhibitors (INSTIs) are proving potent antiretroviral agents in clinical trials. One credible theory sees INSTIs as docking at the cellular (acceptor) DNA-binding site after IN forms a transitional complex with viral (donor) DNA. However, mapping of the DNA and INSTI binding sites within the IN catalytic core domain (CCD) has been uncertain.MethodsStructural superimpositions were conducted using the SWISS PDB and… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 47 CITATIONS

A comparison of HIV-1 and HIV-2 gag gene expression

VIEW 12 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

HIV-1 IN alternative molecular recognition of DNA induced by raltegravir resistance mutations.

  • Journal of molecular recognition : JMR
  • 2009
VIEW 3 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

References

Publications referenced by this paper.
SHOWING 1-10 OF 48 REFERENCES

A naphthyridine carboxamide provides evidence for discordant resistance between mechanistically identical inhibitors of HIV-1 integrase.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2004
VIEW 21 EXCERPTS
HIGHLY INFLUENTIAL

Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 1999
VIEW 6 EXCERPTS
HIGHLY INFLUENTIAL

Integrase inhibitors to treat HIV/Aids

  • Nature Reviews Drug Discovery
  • 2005
VIEW 10 EXCERPTS
HIGHLY INFLUENTIAL

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2005
VIEW 11 EXCERPTS
HIGHLY INFLUENTIAL