Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions.

Structure (London, England : 1993) - 4 Mar 2021

Gupta Kushol, Allen Audrey, Giraldo Carolina, Eilers Grant, Sharp Robert, Hwang Young, Murali Hemma, Cruz Katrina, Janmey Paul, Bushman Frederic, Van Duyne Gregory D

Abstract excerpt

The major effect of allosteric HIV integrase (IN) inhibitors (ALLINIs) is observed during virion maturation, where ALLINI treatment interrupts IN-RNA interactions via drug-induced IN aggregation, leading to the formation of aberrant virions. To understand the structural changes that accompany drug-induced aggregation, we determined the soft matter properties of ALLINI-induced IN aggregates. Using small-angle...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Allosteric Site

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Integrase

Share to HIV Integrase Inhibitors

Share to Mutation

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 33357410
DOI: 10.1016/j.str.2020.12.001
PMCID: PMC7935764

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions.PMID 33357410Read ↗

Structural Impact of Ex Vivo Resistance Mutations on HIV-1 Integrase Polymers Induced by Allosteric Inhibitors.Semantic proximity Read ↗

Architecture and assembly of HIV integrase multimers in the absence of DNA substrates.Semantic proximity Read ↗

Structural Basis for Inhibitor-Induced Aggregation of HIV IntegraseSemantic proximity Read ↗

A Critical Role of the C-terminal Segment for Allosteric Inhibitor-induced Aberrant Multimerization of HIV-1 IntegraseSemantic proximity Read ↗

Supercharged Assembly: A Broad-Spectrum Mechanism of Action for Drugs that Undermine Controlled HIV-1 Viral Capsid FormationSemantic proximity Read ↗

A Conformational Escape Reaction of HIV-1 against an Allosteric Integrase Inhibitor.Semantic proximity Read ↗

Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.Semantic proximity Read ↗

Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in MaturationSemantic proximity Read ↗

RNA G-Quadruplexes Function as a Tunable Switch of FUS Phase SeparationSemantic proximity Read ↗

Allosteric HIV-1 Integrase Inhibitors Lead to Premature Degradation of the Viral RNA Genome and Integrase in Target CellsSemantic proximity Read ↗

Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integrationSemantic proximity Read ↗

Integrase-RNA interactions underscore the critical role of integrase in HIV-1 virion morphogenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.