Skip NavigationSkip to Content
Return Return to Search Results

Virtual screening application of a model of full-length HIV-1 integrase complexed with viral DNA

  1. Author:
    Liao, C. Z.
    Karki, R. G.
    March, C.
    Pommier, Y.
    Nicklaus, M. C.

  2. Author Address

    NCI, Med Chem Lab, Ctr Canc Res, NIH,DHHS, Frederick, MD 21702 USA. NCI, Mol Pharmacol Lab, Ctr Canc Res, NIH,DHHS, Bethesda, MD 20892 USA.;Nicklaus, MC, NCI, Med Chem Lab, Ctr Canc Res, NIH,DHHS, Frederick, MD 21702 USA.;mnl@helix.nih.gov
    1. Year: 2007
    2. Date: Oct
  2. Journal: Bioorganic & Medicinal Chemistry Letters
    1. 17
    2. 19
    3. Pages: 5361-5365
  4. Type of Article: Article
  5. ISSN: 0960-894X
  1. Abstract:

    To address the absence of experimental data on the full-length structure of HTV-1 integrase and the way it binds to viral and human DNA, we had previously [Karki, R. G.; Tang, Y.; Burke, T. R., Jr.; Nicklaus, M. C. J. Comput. Aided Mol. Des. 2004, 18, 739] constructed models of full-length HIV-1 integrase complexed with models of viral and human DNA. Here we describe the discovery of novel HIV-1 integrase strand transfer inhibitors based on one of these models. Virtual screening methods including docking and filtering by predicted ADME/Tox properties yielded several mu M level inhibitors of the strand transfer reaction catalyzed by wild-type HIV-1 integrase. (C) 2007 Published by Elsevier Ltd.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1016/j.bmcl.2007.08.011
  3. View record in Web of Science®
  4. WOS: 000250041400014

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel