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Viruses 2010, 2(4), 900-926; doi:10.3390/v2040900

HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors

 and *
Department of Microbiology and Immunology, McGill University, Lyman Duff Medical Building (D6), 3775 University St., Montreal, QC, H3A 2B4, Canada
* Author to whom correspondence should be addressed.
Received: 28 January 2010 / Revised: 22 March 2010 / Accepted: 24 March 2010 / Published: 30 March 2010
(This article belongs to the Special Issue Retroviral Enzymes)
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Since the human immunodeficiency virus (HIV) was discovered as the etiological agent of acquired immunodeficiency syndrome (AIDS), it has encouraged much research into antiviral compounds. The reverse transcriptase (RT) of HIV has been a main target for antiviral drugs. However, all drugs developed so far inhibit the polymerase function of the enzyme, while none of the approved antiviral agents inhibit specifically the necessary ribonuclease H (RNase H) function of RT. This review provides a background on structure-function relationships of HIV-1 RNase H, as well as an outline of current attempts to develop novel, potent chemotherapeutics against a difficult drug target.
Keywords: HIV; reverse transcriptase; RNase H; inhibitors; drug resistance HIV; reverse transcriptase; RNase H; inhibitors; drug resistance
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Beilhartz, G.L.; Götte, M. HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors. Viruses 2010, 2, 900-926.

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