ArticleCell2007
Structure of full-length HIV-1 CA: a model for the mature capsid lattice.
Article in Cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 210 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.
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Who cites it
210 citing papers in PubMed.
- Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026Review
- HIV capsid inhibitors: Mechanisms, resistance, and therapeutic advances.PLoS pathogens · 2026Review
- TARDBP as a regulator of HIV-1 assembly and infection: a review of targeting the viral capsid precursor Pr55Gag and limiting viral core entry.Cell communication and signaling : CCS · 2026Review
- Transient Occupancy and Pore Dynamics: IP6 Behavior in HIV-1The journal of physical chemistry. B · 2026Article
- Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids.Journal of the American Chemical Society · 2025Article
- Review
- Structural Basis for Alternative Self-Assembly Pathways Leading to Different Human Immunodeficiency Virus Capsid-Like Nanoparticles.ACS nano · 2024Article
- HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly.Nature communications · 2024Article
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Arg18 Substitutions Reveal the Capacity of the HIV-1 Capsid Protein for Non-Fullerene Assembly.Viruses · 2024Article
- LoCoHD: a metric for comparing local environments of proteins.Nature communications · 2024Article
- Multidisciplinary studies with mutated HIV-1 capsid proteins reveal structural mechanisms of lattice stabilization.Nature communications · 2023Article
- Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity.International journal of molecular sciences · 2022Review
- Uracil derivatives as HIV-1 capsid protein inhibitors: design,RSC advances · 2022Article
- Clade-Specific Alterations within the HIV-1 Capsid Protein with Implications for Nuclear Translocation.Biomolecules · 2022Article
- Teaching old dogmas new tricks: recent insights into the nuclear import of HIV-1.Current opinion in virology · 2022Review
- Selection and identification of an RNA aptamer that specifically binds the HIV-1 capsid lattice and inhibits viral replication.Nucleic acids research · 2022Article
- Design, synthesis, and mechanistic investigations of phenylalanine derivatives containing a benzothiazole moiety as HIV-1 capsid inhibitors with improved metabolic stability.European journal of medicinal chemistry · 2022Article
- Design, synthesis, and mechanism study of dimerized phenylalanine derivatives as novel HIV-1 capsid inhibitors.European journal of medicinal chemistry · 2021Article
150 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
Abstract
The capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed hexameric arrays of the viral CA protein, but a high-resolution structure of the lattice has remained elusive. A three-dimensional map of two-dimensional crystals of the R18L mutant of HIV-1 CA was derived by electron cryocrystallography. The docking of high-resolution domain structures into the map yielded the first unambiguous model for full-length HIV-1 CA. Three important protein-protein assembly interfaces are required for capsid formation. Each CA hexamer is composed of an inner ring of six N-terminal domains and an outer ring of C-terminal domains that form dimeric linkers connecting neighboring hexamers. Interactions between the two domains of CA further stabilize the hexamer and provide a structural explanation for the mechanism of action of known HIV-1 assembly inhibitors.
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17923088What 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.