ArticleVirology2012
The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.
Article in Virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Speed Matters: Directed Assembly of Icosahedral HPV Virus-Like Particles.Journal of the American Chemical Society · 2025Article
- Fluorescence, Circular Dichroism and Mass Spectrometry as Tools to Study Virus Structure.Sub-cellular biochemistry · 2024Review
- Self-assembly coupled to liquid-liquid phase separation.PLoS computational biology · 2023Article
- Modelling ribosome kinetics and translational control on dynamic mRNA.PLoS computational biology · 2023Article
- Applications of Charge Detection Mass Spectrometry in Molecular Biology and Biotechnology.Chemical reviews · 2022Review
- Article
- Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.The Journal of biological chemistry · 2016Article
- Assembly and Release of Hepatitis B Virus.Cold Spring Harbor perspectives in medicine · 2015Review
- A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly.Journal of virology · 2015Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Effects of an early conformational switch defect during ϕX174 morphogenesis are belatedly manifested late in the assembly pathway.Journal of virology · 2013Article
- Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In vitro assembly of bacteriophage P22 procapsids requires coat protein and sub-stoichiometric concentrations of the internal scaffolding protein. If there is no scaffolding protein, coat protein assembles aberrantly, but only at higher concentrations. Too much scaffolding protein results in partial procapsids. By treating the procapsid as a lattice that can bind and be stabilized by scaffolding protein we dissect procapsid assembly as a function of protein concentration and scaffolding/coat protein ratio. We observe that (i) the coat-coat association is weaker for procapsids than for aberrant polymer formation, (ii) scaffolding protein makes a small but sufficient contribution to stability to favor the procapsid form, and (iii) there are multiple classes of scaffolding protein binding sites. This approach should be applicable to other heterogeneous virus assembly reactions and will facilitate our ability to manipulate such in vitro reactions to probe assembly, and for development of nanoparticles.
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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.