Results 1 to 10 of about 989 (99)

Allosteric Integrase Inhibitor Influences on HIV-1 Integration and Roles of LEDGF/p75 and HDGFL2 Host Factors [PDF]

Viruses, 2022
Allosteric integrase (IN) inhibitors (ALLINIs), which are promising preclinical compounds that engage the lens epithelium-derived growth factor (LEDGF)/p75 binding site on IN, can inhibit different aspects of human immunodeficiency virus 1 (HIV-1 ...
Parmit Kumar Singh, Wen Li, Gregory J. Bedwell, Hind J. Fadel, Eric M. Poeschla, Alan N. Engelman   +5 more
doaj   +5 more sources

A highly potent and safe pyrrolopyridine-based allosteric HIV-1 integrase inhibitor targeting host LEDGF/p75-integrase interaction site.

PLoS Pathogens, 2021
Allosteric integrase inhibitors (ALLINIs) are a class of experimental anti-HIV agents that target the noncatalytic sites of the viral integrase (IN) and interfere with the IN-viral RNA interaction during viral maturation.
Tatsuya Maehigashi, Seohyun Ahn, Uk-Il Kim, Jared Lindenberger, Adrian Oo, Pratibha C Koneru, Bijan Mahboubi, Alan N Engelman, Mamuka Kvaratskhelia, Kyungjin Kim, Baek Kim   +10 more
doaj   +5 more sources

The structural and mechanistic bases for the viral resistance to allosteric HIV-1 integrase inhibitor pirmitegravir [PDF]

mBio
Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are investigational antiretroviral agents that potently impair virion maturation by inducing hyper-multimerization of IN and inhibiting its interaction with viral genomic RNA. The pyrrolopyridine-based
Tung Dinh, Zahira Tber, Juan S. Rey, Seema Mengshetti, Arun S. Annamalai, Reed Haney, Lorenzo Briganti, Franck Amblard, James R. Fuchs, Peter Cherepanov, Kyungjin Kim, Raymond F. Schinazi, Juan R. Perilla, Baek Kim, Mamuka Kvaratskhelia   +14 more
doaj   +6 more sources

Optimizing the Multimerization Properties of Quinoline-Based Allosteric HIV-1 Integrase Inhibitors [PDF]

Viruses
Allosteric HIV-1 Integrase (IN) Inhibitors or ALLINIs bind at the dimer interface of the IN, away from the enzymatic catalytic site, and disable viral replication by inducing over-multimerization of IN.
Jian Sun, Jacques J. Kessl
doaj   +4 more sources

The allosteric HIV-1 integrase inhibitor BI-D affects virion maturation but does not influence packaging of a functional RNA genome. [PDF]

PLoS ONE, 2014
The viral integrase (IN) is an essential protein for HIV-1 replication. IN inserts the viral dsDNA into the host chromosome, thereby aided by the cellular co-factor LEDGF/p75.
Nikki van Bel, Yme van der Velden, Damien Bonnard, Erwann Le Rouzic, Atze T Das, Richard Benarous, Ben Berkhout   +6 more
doaj   +6 more sources

A Conformational Escape Reaction of HIV-1 against an Allosteric Integrase Inhibitor [PDF]

Journal of Virology, 2020
Understanding the mechanism of HIV-1 resistance to anti-HIV-1 drugs could lead to the development of novel drugs with increased efficiency, resulting in more effective ART. ART composed of more potent and long-acting anti-HIV-1 drugs can greatly improve drug adherence and also provide HIV-1 prevention such as preexposure prophylaxis.
Tomofumi Nakamura, Teruya Nakamura, Masayuki Amano, Toshikazu Miyakawa, Yuriko Yamagata, Masao Matsuoka, Hirotomo Nakata   +6 more
  +8 more sources

Multi-Substituted Quinolines as HIV-1 Integrase Allosteric Inhibitors [PDF]

Viruses, 2022
Allosteric HIV-1 integrase (IN) inhibitors, or ALLINIs, are a new class of antiviral agents that bind at the dimer interface of the IN, away from the enzymatic catalytic site and block viral replication by triggering an aberrant multimerization of the viral enzyme.
Long Phi Dinh, Jian Sun, Courtney D. Glenn, Krunal Patel, Julie A. Pigza, Matthew G. Donahue, Larry Yet, Jacques J. Kessl   +7 more
openaire   +4 more sources

Biological and Structural Analyses of New Potent Allosteric Inhibitors of HIV-1 Integrase [PDF]

Antimicrobial Agents and Chemotherapy, 2023
HIV-1 integrase-LEDGF allosteric inhibitors (INLAIs) share the binding site on the viral protein with the host factor LEDGF/p75. These small molecules act as molecular glues promoting hyper-multimerization of HIV-1 IN protein to severely perturb maturation of viral particles.
Damien Bonnard, Erwann Le Rouzic, Matthew R. Singer, Zhe Yu, Frédéric Le Strat, Claire Batisse, Julien Batisse, Céline Amadori, Sophie Chasset, Valerie E. Pye, Stéphane Emiliani, Benoit Ledoussal, Marc Ruff, François Moreau, Peter Cherepanov, Richard Benarous   +15 more
openaire   +3 more sources

Structural Studies of the HIV-1 Integrase Protein: Compound Screening and Characterization of a DNA-Binding Inhibitor. [PDF]

PLoS ONE, 2015
Understanding the HIV integrase protein and mechanisms of resistance to HIV integrase inhibitors is complicated by the lack of a full length HIV integrase crystal structure. Moreover, a lentiviral integrase structure with co-crystallised DNA has not been
Peter K Quashie, Ying-Shan Han, Said Hassounah, Thibault Mesplède, Mark A Wainberg   +4 more
doaj   +1 more source

Multimodal Functionalities of HIV-1 Integrase

Viruses, 2022
Integrase is the retroviral protein responsible for integrating reverse transcripts into cellular genomes. Co-packaged with viral RNA and reverse transcriptase into capsid-encased viral cores, human immunodeficiency virus 1 (HIV-1) integrase has long ...
Alan N. Engelman, Mamuka Kvaratskhelia
doaj   +1 more source