Discover Community Create You

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

Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integration

27 Feb 2025

Abstract excerpt

Human immunodeficiency virus type 1 (HIV-1) capsid, which is the target of the antiviral lenacapavir, protects the viral genome and binds multiple host proteins to influence intracellular trafficking, nuclear import, and integration. Previously, we showed that capsid binding to cleavage and polyadenylation specificity factor 6 (CPSF6) in the cytoplasm is competitively inhibited by cyclophilin A (CypA) binding and...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 40013779
DOI: 10.1128/mbio.00169-25

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integrationPMID 40013779Read ↗

HIV-1 capsid and viral DNA integrationSemantic proximity Read ↗

Interactions of HIV-1 Capsid with Host Factors and Their Implications for Developing Novel TherapeuticsSemantic proximity Read ↗

A model for cofactor use during HIV-1 reverse transcription and nuclear entrySemantic proximity Read ↗

CPSF6 defines a conserved capsid interface that modulates HIV-1 replication.Semantic proximity Read ↗

Capsid-CPSF6 Interaction Licenses Nuclear HIV-1 Trafficking to Sites of Viral DNA IntegrationSemantic proximity Read ↗

Truncated CPSF6 Forms Higher-Order Complexes That Bind and Disrupt HIV-1 Capsid.Semantic proximity Read ↗

Multiple Roles of HIV-1 Capsid during the Virus Replication CycleSemantic proximity Read ↗

HIV-1 uncoats in the nucleus near sites of integrationSemantic proximity Read ↗

Capsid-CPSF6 Interaction Is Dispensable for HIV-1 Replication in Primary Cells but Is Selected during Virus Passage <i>In Vivo</i>Semantic proximity Read ↗

The HIV-1 capsid core is an opportunistic nuclear import receptorSemantic proximity Read ↗

HIV-1 Infection Regulates Gene Expression by Altering Alternative Polyadenylation Through CPSF6 and CPSF5 DelocalizationSemantic proximity Read ↗

The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the MatterSemantic proximity Read ↗

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