ArticleNature communications2020
TRIM5α self-assembly and compartmentalization of the HIV-1 viral capsid.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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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
43 citing papers in PubMed, 67 citations in OpenAlex.
- Mechanistic Insights into HIV-1 Capsid Interactions with CPSF6.bioRxiv : the preprint server for biology · 2026Article
- MxB N-Terminus Adopts a Stable α-Helix to Engage the HIV-1 Capsid Trimer Interface.bioRxiv : the preprint server for biology · 2026Article
- Mechanism of HIV-1 Capsid Rupture and Uncoating by Reverse Transcription.bioRxiv : the preprint server for biology · 2026Article
- Study of retroviral restrictions in a Tadarida bat cell line enlightens specific early blocks and TRIM5 locus multiplication.Journal of virology · 2026Article
- Atomistic characterization of the maturation mechanisms in the HIV-1 capsid domain.Nature communications · 2026Article
- HIV-1 nuclear import is selective and depends on both capsid elasticity and nuclear pore adaptability.Nature microbiology · 2025Article
- The Complex Interactions Between HIV-1 and Human Host Cell Genome: From Molecular Mechanisms to Clinical Practice.International journal of molecular sciences · 2025Review
- Interface flexibility controls the nucleation and growth of supramolecular networks.Nature chemistry · 2025Article
- Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025Review
- Visualizing the virus world inside the cell by cryo-electron tomography.Journal of virology · 2024Review
- Review
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Review
- HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The cyclophilin A-binding loop of the capsid regulates the human TRIM5α sensitivity of nonpandemic HIV-1.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Multidisciplinary studies with mutated HIV-1 capsid proteins reveal structural mechanisms of lattice stabilization.Nature communications · 2023Article
- Understanding Virus Structure and Dynamics through Molecular Simulations.Journal of chemical theory and computation · 2023Review
- A Tripartite Complex HIV-1 Tat-Cyclophilin A-Capsid Protein Enables Tat Encapsidation That Is Required for HIV-1 Infectivity.Journal of virology · 2023Article
- Performance efficient macromolecular mechanics via sub-nanometer shape based coarse graining.Nature communications · 2023Article
- Modeling membrane reshaping driven by dynamic protein assemblies.Current opinion in structural biology · 2023Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The tripartite-motif protein, TRIM5α, is an innate immune sensor that potently restricts retrovirus infection by binding to human immunodeficiency virus capsids. Higher-ordered oligomerization of this protein forms hexagonally patterned structures that wrap around the viral capsid, despite an anomalously low affinity for the capsid protein (CA). Several studies suggest TRIM5α oligomerizes into a lattice with a symmetry and spacing that matches the underlying capsid, to compensate for the weak affinity, yet little is known about how these lattices form. Using a combination of computational simulations and electron cryo-tomography imaging, we reveal the dynamical mechanisms by which these lattices self-assemble. Constrained diffusion allows the lattice to reorganize, whereas defects form on highly curved capsid surfaces to alleviate strain and lattice symmetry mismatches. Statistical analysis localizes the TRIM5α binding interface at or near the CypA binding loop of CA. These simulations elucidate the molecular-scale mechanisms of viral capsid cellular compartmentalization by TRIM5α.
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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.