ArticleJournal of virology1999
Actin associates with the nucleocapsid domain of the human immunodeficiency virus Gag polyprotein.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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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
51 citing papers in PubMed, 99 citations in OpenAlex.
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- Review
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Involvement of Actin-Regulating Factor Cofilin in the Inclusion Body Formation and RNA Synthesis of Human Parainfluenza Virus Type 3 via Interaction With the Nucleoprotein.Frontiers in microbiology · 2019Article
- All-Round Manipulation of the Actin Cytoskeleton by HIV.Viruses · 2018Review
- M2BP inhibits HIV-1 virion production in a vimentin filaments-dependent manner.Scientific reports · 2016Article
- Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells.Journal of virology · 2015Article
- Nucleocapsid Protein: A Desirable Target for Future Therapies Against HIV-1.Current topics in microbiology and immunology · 2015Review
- The nucleocapsid domain of Gag is dispensable for actin incorporation into HIV-1 and for association of viral budding sites with cortical F-actin.Journal of virology · 2014Article
- Investigating the role of F-actin in human immunodeficiency virus assembly by live-cell microscopy.Journal of virology · 2014Article
- ROCK1 and LIM kinase modulate retrovirus particle release and cell-cell transmission events.Journal of virology · 2014Article
- HIV-1 triggers WAVE2 phosphorylation in primary CD4 T cells and macrophages, mediating Arp2/3-dependent nuclear migration.The Journal of biological chemistry · 2014Article
- Novel anti-HIV therapeutics targeting chemokine receptors and actin regulatory pathways.Immunological reviews · 2013Review
- Genistein interferes with SDF-1- and HIV-mediated actin dynamics and inhibits HIV infection of resting CD4 T cells.Retrovirology · 2013Article
- Involvement of LIM kinase 1 in actin polarization in human CD4 T cells.Communicative & integrative biology · 2012Article
- The trinity of the cortical actin in the initiation of HIV-1 infection.Retrovirology · 2012Review
- Protein kinase C-delta regulates HIV-1 replication at an early post-entry step in macrophages.Retrovirology · 2012Article
- Dynamic Association between HIV-1 Gag and Membrane Domains.Molecular biology international · 2012Article
- How HIV-1 takes advantage of the cytoskeleton during replication and cell-to-cell transmission.Viruses · 2011Review
- Filamin A protein interacts with human immunodeficiency virus type 1 Gag protein and contributes to productive particle assembly.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, it was shown that actin molecules are present in human immunodeficiency virus type 1 (HIV-1) particles. We have examined the basis for incorporation and the location of actin molecules within HIV-1 and murine retrovirus particles. Our results show that the retroviral Gag polyprotein is sufficient for actin uptake. Immunolabeling studies demonstrate that actin molecules localize to a specific radial position within the immature particle, clearly displaced from the matrix domain underneath the viral membrane but in proximity to the nucleocapsid (NC) domain of the Gag polyprotein. When virus or subviral Gag particles were disrupted with nonionic detergent, actin molecules remained associated with the disrupted particles. Actin molecules remained in a stable complex with the NC cleavage product (or an NC-RNA complex) after treatment of the disrupted HIV-1 particles with recombinant HIV-1 protease. In contrast, matrix and capsid molecules were released. The same result was obtained when mature HIV-1 particles were disrupted with detergent. Taken together, these results indicate that actin molecules are associated with the NC domain of the viral polyprotein.
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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.