Results 51 to 60 of about 86,566 (299)

Mutations Located outside the Integrase Gene Can Confer Resistance to HIV-1 Integrase Strand Transfer Inhibitors

mBio, 2017
Resistance to the integrase strand transfer inhibitors raltegravir and elvitegravir is often due to well-identified mutations in the integrase gene. However, the situation is less clear for patients who fail dolutegravir treatment.
Isabelle Malet, Frédéric Subra, Charlotte Charpentier, Gilles Collin, Diane Descamps, Vincent Calvez, Anne-Geneviève Marcelin, Olivier Delelis   +7 more
doaj   +1 more source

Molecular features related to HIV integrase inhibition obtained from structure- and ligand-based approaches. [PDF]

PLoS ONE, 2014
Among several biological targets to treat AIDS, HIV integrase is a promising enzyme that can be employed to develop new anti-HIV agents. The aim of this work is to propose a mechanistic interpretation of HIV-1 integrase inhibition and to rationalize the ...
Luciana L de Carvalho, Vinícius G Maltarollo, Emmanuela Ferreira de Lima, Karen C Weber, Kathia M Honorio, Albérico B F da Silva   +5 more
doaj   +1 more source

The Drug-Induced Interface That Drives HIV-1 Integrase Hypermultimerization and Loss of Function

mBio, 2023
Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are an emerging class of small molecules that disrupt viral maturation by inducing the aberrant multimerization of IN. Here, we present cocrystal structures of HIV-1 IN with two potent ALLINIs, namely,
Matthew R. Singer, Tung Dinh, Lev Levintov, Arun S. Annamalai, Juan S. Rey, Lorenzo Briganti, Nicola J. Cook, Valerie E. Pye, Ian A. Taylor, Kyungjin Kim, Alan N. Engelman, Baek Kim, Juan R. Perilla, Mamuka Kvaratskhelia, Peter Cherepanov   +14 more
doaj   +1 more source

An Allosteric Mechanism for Inhibiting HIV-1 Integrase with a Small Molecule [PDF]

, 2009
HIV-1 integrase (IN) is a validated target for developing antiretroviral inhibitors. Using affinity acetylation and mass spectrometric (MS) analysis, we previously identified a tetra-acetylated inhibitor (2E)-3-[3,4-bis(acetoxy)phenyl]-2-propenoate-N ...
Burke, Terrence R., Jr., Eidahl, Jocelyn O., Hess, Sonja, Kessl, Jacques J., Kvaratskhelia, Mamuka, McKee, Christopher J., Shkriabai, Nikolozi, Zhao, Zhuojun   +7 more
core   +3 more sources

Modeling the HIV-1 Intasome: A Prototype View of the Target of Integrase Inhibitors

Viruses, 2010
The HIV-1 integrase enzyme is essential for integrating the viral DNA into the host chromosome. Infection is aborted in the absence of integration, making integrase an attractive antiviral target. Recently approved inhibitors of integrase bind tightly to
Robert Craigie, Zhiqi Yin
doaj   +1 more source

Nonhuman Primates and Humanized Mice for Studies of HIV-1 Integrase Inhibitors: A Review

Pathogens and Immunity, 2016
Since the discovery of the first inhibitors of HIV replication, drug resistance has been a major problem in HIV therapy, due, in part, to the high mutation rate of HIV.
Said A. Hassounah, Thibault Mesplède, Mark A. Wainberg   +2 more
doaj   +1 more source

Allosteric HIV-1 integrase inhibitors lead to premature degradation of the viral RNA genome and integrase in target cells [PDF]

, 2017
Recent evidence indicates that inhibition of HIV-1 integrase (IN) binding to the viral RNA genome by allosteric integrase inhibitors (ALLINIs) or through mutations within IN yields aberrant particles in which the viral ribonucleoprotein complexes (vRNPs)
Elliott, Jennifer, Errando, Manel, Koneru, Pratibha C, Kutluay, Sebla B, Kvaratskhelia, Mamuka, Lawson, Dana Q, Madison, Michaela K, Ozanturk, Ayse Naz, Townsend, Dana   +8 more
core   +2 more sources

HIV-1 Integrase Inhibitors That Are Active against Drug-Resistant Integrase Mutants

Antimicrobial Agents and Chemotherapy, 2020
The currently recommended first-line therapy for HIV-1-infected patients is an integrase (IN) strand transfer inhibitor (INSTI), either dolutegravir (DTG) or bictegravir (BIC), in combination with two nucleoside reverse transcriptase inhibitors (NRTIs ...
Steven J. Smith, X. Zhao, D. Passos, D. Lyumkis, T. Burke, S. Hughes   +5 more
semanticscholar   +1 more source

Integrase Inhibitor Prodrugs: Approaches to Enhancing the Anti-HIV Activity of β-Diketo Acids

Molecules, 2015
HIV integrase, encoded at the 3′-end of the HIV pol gene, is essential for HIV replication. This enzyme catalyzes the incorporation of HIV DNA into human DNA, which represents the point of “no-return” in HIV infection.
Vasu Nair, Maurice Okello
doaj   +1 more source

Effectiveness of dolutegravir-based regimens as either first-line or switch antiretroviral therapy: data from the Icona cohort [PDF]

, 2019
Introduction: Concerns about dolutegravir (DTG) tolerability in the real-life setting have recently arisen. We aimed to estimate the risk of treatment discontinuation and virological failure of DTG-based regimens from a large cohort of HIV-infected ...
Abeli C., Acinapura R., alungo A., Andreoni M., Angarano G., Antinori A., aracino A., atini A., azzarin A., Bagella P., Bai F., Baldelli F., Baldin G., Balotta C., Bandera A., Barocci V., Bassetti M., Blanc P., Bobbio N., Bonfanti P., Bonora S., Borderi M., Borgia G., Cacopardo B., Calcagno A., Capetti A., Capobianchi M. R., Capozzi M., Caramello P., Carletti F., Carrara S., Cascio A., Cassola G., Castagna A., Castelli F., Castelnuovo F., Cattelan A. M., Cauda R., Ceccherini-Silberstein F., Ceccherini-Silberstein F., Cecchetto M., Celesia B., Chiodera A., Cicalini S., Cingolani A., Cinque P., Colomba C., Costantini A., Cozzi-Lepri A., Cozzi-Lepri A., Cristaudo A., d'Arminio Monforte A., De Luca A., Di Biagio A., Di Caro A., Di Giuli C., Di Martino F., Di Perri G., Esposito V., Fabrizio C., Falasca K., Fanti I., Fontana Del Vecchio R., Francisci D., Galli L., Galli M., Gentile I., Giacometti I. A., Gianotti N., Girardi E., Gori A., Graziano S., Guaraldi G., i V., Iaiani G., Iardino R., Ippolito G., Lapadula G., lessandrini A., Lichtner M., Lo Caputo S., Lorenzini P., Lorenzotti S., Macchia M., Maddaloni L., Madeddu G., Maggiolo F., Maggiolo F., Magnani G., Manfrin V., Marchetti G., Marinello S., Mastrorosa I., Mazzarello G., Menzaghi B., Migliorino C., Milini P., Minardi C., Moioli M. C., Molteni C., Mondi A., Monno L., Mussini C., Nozza S., Nunnari G., ondero A., Orofino G. C., Pan A., Parruti G., Pellicano G., Pellizzer G., Perno C. F., Petrone F., Piolini R., Plazzi M. M., Pozzetto I., Prota G., Puoti M., Puzzolante C., Quartu S., Quiros Roldan E., Rezza G., Ridolfo A. L., Rivano Capparucia M., Rizzardini G., Rodano' A., Rossetti B., Rossotti R., Rusconi S., Rusconi S., Salpietro S., Sangiovanni V., Santoro M. M., Sarmati L., Savinelli S., Schiaroli E., Sciandra M., Segala D., Sighinolfi L., Sozio F., Starnini G., Suardi C., Tavelli A., Tavelli A., Tincati C., Truffa S., Ursitti M. A., Vecchiet J., Vergori A., Verucchi G., Viale P., Vichi F., Viscoli C., Viviani F., von Schloesser F., Vullo V.   +155 more
core   +4 more sources