ArticleJournal of virology2013
Human cytosolic extracts stabilize the HIV-1 core.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 57 citations in OpenAlex.
- Structural basis of lenacapavir-induced HIV-1 capsid defects during virion maturation.Nature communications · 2026Article
- Capsid and integrase play essential apposing roles in viral ribonucleoprotein assembly during HIV-1 core morphogenesis.iScience · 2026Article
- Structural, biophysical, and virological mechanistic characterization of HIV-1 capsid-targeting antivirals.bioRxiv : the preprint server for biology · 2025Article
- HIV-1-induced translocation of CPSF6 to biomolecular condensates.Trends in microbiology · 2024Review
- Antiviral compounds modulate elasticity, strength and material fatigue of a virus capsid framework.Biophysical journal · 2022Article
- TRIM5α Restriction of HIV-1-N74D Viruses in Lymphocytes Is Caused by a Loss of Cyclophilin A Protection.Viruses · 2022Article
- GS-CA1 and lenacapavir stabilize the HIV-1 core and modulate the core interaction with cellular factors.iScience · 2022Article
- Review
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Nuclear restriction of HIV-1 infection by SUN1.Scientific reports · 2021Article
- The Role of Capsid in HIV-1 Nuclear Entry.Viruses · 2021Review
- Role of Transportin-SR2 in HIV-1 Nuclear Import.Viruses · 2021Review
- Capsid Lattice Destabilization Leads to Premature Loss of the Viral Genome and Integrase Enzyme during HIV-1 Infection.Journal of virology · 2020Article
- HIV-1 Maturation: Lessons Learned from Inhibitors.Viruses · 2020Review
- Capsid-Labelled HIV To Investigate the Role of Capsid during Nuclear Import and Integration.Journal of virology · 2020Article
- A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors.Scientific reports · 2019Article
- Off-Pathway Assembly: A Broad-Spectrum Mechanism of Action for Drugs That Undermine Controlled HIV-1 Viral Capsid Formation.Journal of the American Chemical Society · 2019Article
- PF74 Inhibits HIV-1 Integration by Altering the Composition of the Preintegration Complex.Journal of virology · 2019Article
- Retroviral Capsid Core Stability Assay.Bio-protocol · 2018Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The stability of the HIV-1 core in the cytoplasm is crucial for productive HIV-1 infection. Mutations that stabilize or destabilize the core showed defects on HIV-1 reverse transcription and infection. We developed a novel and simple assay to measure the stability of in vitro-assembled HIV-1 CA-NC complexes. The assay allowed us to demonstrate that cytosolic extracts strongly stabilize the HIV-1 core. Interestingly, stabilization of in vitro-assembled HIV-1 CA-NC complexes is not due solely to macromolecular crowding, suggesting the presence of specific cellular factors that stabilize the HIV-1 core. By using our novel assay, we measured the abilities of different drugs, such as PF74, CAP-1, IXN-053, cyclosporine, Bi2 (also known as BI-2), and the peptide CAI, to modulate the stability of in vitro-assembled HIV-1 CA-NC complexes. Interestingly, we found that PF74 and Bi2 strongly stabilized HIV-1 CA-NC complexes. On the other hand, the peptide CAI destabilized HIV-1 CA-NC complexes. We also found that purified cyclophilin A destabilizes in vitro-assembled HIV-1 CA-NC complexes in the presence of cellular extracts in a cyclosporine-sensitive manner. In agreement with previous observations using the fate-of-the-capsid assay, we also demonstrated the ability of recombinant CPSF6 to stabilize HIV-1 CA-NC complexes. Overall, our findings suggested that cellular extracts specifically stabilize the HIV-1 core. We believe that our assay can be a powerful tool to assess HIV-1 core stability in vitro.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.