Results 221 to 230 of about 42,534 (266)

Raltegravir: an integrase inhibitor for HIV-1

Expert Opinion on Investigational Drugs, 2008
The need to develop antiretroviral agents with novel mechanisms of action persists for the treatment of both antiretroviral- experienced and antiretroviral-naive patients with HIV/AIDS. This is mandated, in part, by the perpetual advent of antiretroviral-resistant HIV-1 strains.
Teresa H, Evering, Martin, Markowitz
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The Hunt for HIV-1 Integrase Inhibitors

AIDS Patient Care and STDs, 2006
Currently, there are three distinct mechanistic classes of antiretrovirals: inhibitors of the HIV- 1 reverse transcriptase and protease enzymes and inhibitors of HIV entry, including receptor and coreceptor binding and cell fusion. A new drug class that inhibits the HIV-1 integrase enzyme (IN) is in development and may soon be available in the clinic ...
Max, Lataillade, Michael J, Kozal
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QSAR studies of HIV-1 integrase inhibition

Bioorganic & Medicinal Chemistry, 2002
Compounds from a wide variety of structural classes inhibit HIV-1 integrase. However, a single unified understanding of the relationship between the structures and activities of these compounds still eludes researchers. We report herein the development of QSAR models for integrase inhibition.
Hongbin, Yuan, Abby L, Parrill
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Hydroxylated Aromatic Inhibitors of HIV-1 Integrase

Journal of Medicinal Chemistry, 1995
Efficient replication of HIV-1 requires integration of a DNA copy of the viral genome into a chromosome of the host cell. Integration is catalyzed by the viral integrase, and we have previously reported that phenolic moieties in compounds such as flavones, caffeic acid phenethyl ester (CAPE, 2), and curcumin confer inhibitory activity against HIV-1 ...
Terrence R. Jr. Burke, Mark Fesen, Abhijit Mazumder, Jessie Yung, Jian Wang, Adelaide M. Carothers, Dezider Grunberger, John Driscoll, Yves Pommier, Kurt Kohn   +9 more
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Dihydroxypyridopyrazine-1,6-dione HIV-1 integrase inhibitors

Bioorganic & Medicinal Chemistry Letters, 2007
A series of potent novel dihydroxypyridopyrazine-1,6-dione HIV-1 integrase inhibitors was identified. These compounds inhibited the strand transfer process of HIV-1 integrase and viral replication in cells. Compound 6 is active against replication of HIV with a CIC(95) of 0.31 microM and exhibits no shift in potency in the presence of 50% normal human ...
John S, Wai, Boyoung, Kim, Thorsten E, Fisher, Linghang, Zhuang, Mark W, Embrey, Peter D, Williams, Donnette D, Staas, Chris, Culberson, Terry A, Lyle, Joseph P, Vacca, Daria J, Hazuda, Peter J, Felock, William A, Schleif, Lori J, Gabryelski, Lixia, Jin, I-Wu, Chen, Joan D, Ellis, Rama, Mallai, Steven D, Young   +18 more
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Metal-Dependent Inhibition of HIV-1 Integrase

Journal of Medicinal Chemistry, 2002
Human immunodeficiency virus type 1 integrase (HIV-1 IN) is an essential enzyme for effective viral replication. Therefore, IN inhibitors are being sought for chemotherapy against AIDS. We had previously identified a series of salicylhydrazides as potent inhibitors of IN in vitro (Neamati, N.; et al. J. Med. Chem. 1998, 41, 3202-3209.).
Nouri, Neamati, Zhaiwei, Lin, Rajeshri G, Karki, Ann, Orr, Kiriana, Cowansage, Dirk, Strumberg, Godwin C G, Pais, Johannes H, Voigt, Marc C, Nicklaus, Heather E, Winslow, He, Zhao, Jim A, Turpin, Jizu, Yi, Anna Marie, Skalka, Terrence R, Burke, Yves, Pommier   +15 more
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Styrylquinazoline Derivatives as HIV-1 Integrase Inhibitors

Archiv der Pharmazie, 2002
Styrylquinazoline derivatives were prepared by Perkin condensation and evaluated for inhibitory activity against HIV-1 integrase. Among them, compound 5c containing a free catechol ring was the most potent (IC(50)=0.8 +/- 1.9 microM)and showed 6-fold more potency than the corresponding styrylquinoline compound (IC(50) = 130.7 +/- 8.6 microM).
Jae Yeol, Lee, Jang Hyun, Park, Sook Ja, Lee, Hokoon, Park, Yong Sup, Lee   +4 more
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Structure and Function of HIV-1 Integrase

Current Topics in Medicinal Chemistry, 2004
HIV-1 integrase is a multidomain enzyme which is required for the integration of viral DNA into the host genome. It is one of three enzymes of HIV, the others being the Reverse Transcriptase and the Protease. It is an attractive target for therapeutic drug design. The enzyme consists of three domains.
Thang K, Chiu, David R, Davies
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HIV‐1 integrase inhibitors: 2005–2006 update

Medicinal Research Reviews, 2007
AbstractHIV‐1 integrase (IN) catalyzes the integration of proviral DNA into the host genome, an essential step for viral replication. Inhibition of IN catalytic activity provides an attractive strategy for antiretroviral drug design. Currently two IN inhibitors, MK‐0518 and GS‐9137, are in advanced stages of human clinical trials.
Raveendra, Dayam, Rambabu, Gundla, Laith Q, Al-Mawsawi, Nouri, Neamati   +3 more
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Expression of HIV‐1 integrase in CEM cells inhibits HIV‐1 replication

The Journal of Gene Medicine, 2004
AbstractBackgroundHIV‐1 integrase (IN) is an interesting target for the gene therapy of AIDS. Although the in vivo functions are not well characterized, it is thought that IN has pleiotropic effects and plays a central role in the interplay between the virus and the host cell. Expression of IN in mammalian cells has proven difficult. We have previously
Johan, van Griensven, Xiaojing, Zhan, Bénédicte, Van Maele, Wim, Pluymers, Martine, Michiels, Erik, De Clercq, Peter, Cherepanov, Zeger, Debyser   +7 more
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