ArticleACS chemical biology2017
Single Particle Observation of SV40 VP1 Polyanion-Induced Assembly Shows That Substrate Size and Structure Modulate Capsid Geometry.
Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed.
- Dynamics of viral self-assembly, viral genome packaging, and virus-cell interactions studied by optical tweezers.European biophysics journal : EBJ · 2026Review
- The evolution of nanopore measurements: from biological out-of-plane pores to plastic in-plane pores.Lab on a chip · 2026Review
- Disassembly of Single Virus Capsids Monitored in Real Time with Multicycle Resistive-Pulse Sensing.Analytical chemistry · 2022Article
- In Vitro Assembly of Virus-Like Particles and Their Applications.Life (Basel, Switzerland) · 2021Review
- Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways.ACS nano · 2020Article
- Revealing in real-time a multistep assembly mechanism for SV40 virus-like particles.Science advances · 2020Article
- pH stability and disassembly mechanism of wild-type simian virus 40.Soft matter · 2020Article
- Assembly Reactions of Hepatitis B Capsid Protein into Capsid Nanoparticles Follow a Narrow Path through a Complex Reaction Landscape.ACS nano · 2019Article
- Evolution of Intermediates during Capsid Assembly of Hepatitis B Virus with Phenylpropenamide-Based Antivirals.ACS infectious diseases · 2019Article
- Analytical Techniques to Characterize the Structure, Properties, and Assembly of Virus Capsids.Analytical chemistry · 2019Review
- Effect of dsDNA on the Assembly Pathway and Mechanical Strength of SV40 VP1 Virus-like Particles.Biophysical journal · 2018Article
- Length of encapsidated cargo impacts stability and structure of in vitro assembled alphavirus core-like particles.Journal of physics. Condensed matter : an Institute of Physics journal · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Simian virus 40 capsid protein (VP1) is a unique system for studying substrate-dependent assembly of a nanoparticle. Here, we investigate a simplest case of this system where 12 VP1 pentamers and a single polyanion, e.g., RNA, form a T = 1 particle. To test the roles of polyanion substrate length and structure during assembly, we characterized the assembly products with size exclusion chromatography, transmission electron microscopy, and single-particle resistive-pulse sensing. We found that 500 and 600 nt RNAs had the optimal length and structure for assembly of uniform T = 1 particles. Longer 800 nt RNA, shorter 300 nt RNA, and a linear 600 unit poly(styrene sulfonate) (PSS) polyelectrolyte produced heterogeneous populations of products. This result was surprising as the 600mer PSS and 500-600 nt RNA have similar mass and charge. Like ssRNA, PSS also has a short 4 nm persistence length, but unlike RNA, PSS lacks a compact tertiary structure. These data indicate that even for flexible substrates, shape as well as size affect assembly and are consistent with the hypothesis that work, derived from protein-protein and protein-substrate interactions, is used to compact the substrate.
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Registered trials
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