Results 221 to 230 of about 13,949 (234)
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Substrate Recognition by Retroviral Integrases
1999Substrate recognition by the retroviral IN enzyme is critical for retroviral integration. To catalyze this recombination event, IN must recognize and act on two types of substrates, viral DNA and host DNA, yet the necessary interactions exhibit markedly different degrees of specificity.
Richard A. Katz, Michael Katzman
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Expert Opinion on Therapeutic Targets, 2001
Human immunodeficiency virus Type 1 (HIV-1) integrase is an essential enzyme for the obligatory integration of the viral DNA into the infected cell chromosome. As no cellular homologue of HIV integrase has been identified, this unique HIV-1 enzyme is an attractive target for the development of new therapeutics.
Jocelyn Yelle +2 more
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Human immunodeficiency virus Type 1 (HIV-1) integrase is an essential enzyme for the obligatory integration of the viral DNA into the infected cell chromosome. As no cellular homologue of HIV integrase has been identified, this unique HIV-1 enzyme is an attractive target for the development of new therapeutics.
Jocelyn Yelle +2 more
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Resistance to HIV integrase inhibitors
Current Opinion in HIV and AIDS, 2012HIV integrase inhibitors are potent antiretroviral drugs that efficiently decrease viral load in patients. Emergence of resistance mutations against this new class of drugs represents a threat to their long-term efficacy. The purpose of this review is to provide new information about the most recent mutations identified and other mutations that confer ...
Peter K. Quashie +2 more
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The Cis-Trans Paradox of Integrase
Science, 1997During recombination, strands of DNA break and are rejoined, producing the reshuffling of genetic information that underlies genetic diversity. Jayaram discusses the chemical mechanism underlying this process, including the controversial cis-trans paradox, as revealed by the x-ray crystallographic structure of the recombinase lambda ...
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ChemInform Abstract: Potential Inhibitors of HIV Integrase
ChemInform, 1999AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Vasu Nair, Christophe Mathe
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HIV Integrase Structure and Function
1999HIV integrase consists of three domains, the structures of which have been individually determined by X-ray crystallography or NMR spectroscopy. The core domain, spanning residues 50-212, is responsible for the catalytic activity of the enzyme.
Dominic Esposito, Robert Craigie
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Bioorganic & Medicinal Chemistry Letters, 2006
Integrase is one of three enzymes expressed by HIV and represents a validated target for therapy. This study reports on the discovery of a new triketoacid-based chemotype that selectively inhibits the strand transfer reaction of HIV-integrase. SAR studies showed that the template binds to integrase in a manner similar to the diketoacid-based inhibitors.
Yunhui Zhang +15 more
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Integrase is one of three enzymes expressed by HIV and represents a validated target for therapy. This study reports on the discovery of a new triketoacid-based chemotype that selectively inhibits the strand transfer reaction of HIV-integrase. SAR studies showed that the template binds to integrase in a manner similar to the diketoacid-based inhibitors.
Yunhui Zhang +15 more
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Using Phage Integrases in a Site-Specific Dual Integrase Cassette Exchange Strategy
2014ΦC31 integrase, a site-specific large serine recombinase, is a useful tool for genome engineering in a variety of eukaryotic species and cell types. ΦC31 integrase performs efficient recombination between its attB site and either its own placed attP site or a partially mismatched genomic pseudo attP site.
Michele P. Calos, Jonathan M. Geisinger
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In VitroAssays for Activities of Retroviral Integrase
Methods, 1997Integration of retroviral DNA, an essential step during the retroviral life cycle, is mediated by the viral protein integrase. Simple in vitro assays for measuring integrase activities are described, including catalysis (3'-end processing, 3'-end joining, disintegration), juxtaposition of viral DNA ends, DNA binding, and target site selection.
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