Article

Emphasizing the structural and computational characterisation of an HIV-1 IN binding interface against potential inhibitors for a promising drug strategy

2026-03-09

Abstract excerpt

<title>Abstract</title> <p>HIV/AIDS has remained a deadly and incurable human disease. The current strand transfer inhibitors (INSTIs), such as raltegravir (RAL), face drawbacks, including a low genetic barrier to resistance and potential cross-resistance. The design of small-molecule antivirals targeting the integration step of the viral life cycle has been the recent highlight of the IN allosteric inhibitor (IN...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: fbde450d-3a28-552a-8bb3-23a9b9c857b1
DOI: 10.21203/rs.3.rs-8984808/v1

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Emphasizing the structural and computational characterisation of an HIV-1 IN binding interface against potential inhibitors for a promising drug strategyDOI 10.21203/rs.3.rs-8984808/v1Read

Biological and structural analysis of new potent Integrase-LEDGF allosteric HIV-1 inhibitorsSemantic proximity Read

Molecular mechanism of HIV‐1 integrase–vDNA interactions and strand transfer inhibitor action: A molecular modeling perspectiveSemantic proximity Read

Understanding the effect of drug-resistant mutations of HIV-1 intasome on raltegravir action through molecular modeling studySemantic proximity Read

Dynamic receptor-based pharmacophore model development and its application in designing novel HIV-1 integrase inhibitors.Semantic proximity Read

Impact of resistance mutations on inhibitor binding to HIV-1 integrase.Semantic proximity Read

Elucidating the molecular determinants for binding modes of a third-generation HIV-1 integrase strand transfer inhibitor: Importance of side chain and solvent reorganizationSemantic proximity Read

Induced-fit docking approach provides insight into the binding mode and mechanism of action of HIV-1 integrase inhibitors.Semantic proximity Read

MK-0536 Inhibits HIV-1 Integrases Resistant to RaltegravirSemantic proximity Read

The structural and mechanistic bases for the viral resistance to allosteric HIV-1 integrase inhibitor pirmitegravirSemantic proximity Read

Molecular dynamic simulations to investigate the structural impact of known drug resistance mutations on HIV-1C Integrase-Dolutegravir binding.Semantic proximity Read

Structural Implications of Genotypic Variations in HIV-1 Integrase From Diverse SubtypesSemantic proximity Read

Blocking the interaction between HIV-1 integrase and human LEDGF/p75: mutational studies, virtual screening and molecular dynamics simulations.Semantic proximity Read