ArticleNature communications2018
Quantitative characterization of all single amino acid variants of a viral capsid-based drug delivery vehicle.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
27 citing papers in PubMed, 65 citations in OpenAlex.
- Viral capsid delivery of cGAMP enhances STING-dependent antitumor immune response.bioRxiv : the preprint server for biology · 2026Article
- Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.Annual review of biochemistry · 2026Review
- Screening metatranscriptomes for ultrastable RNA secondary structures reveals hidden bacteriophages and novel capsid nanomaterials.bioRxiv : the preprint server for biology · 2026Article
- Process for Standardizing and Assessing the Parameters Governing MS2 Virus-Like Particle Reassembly around Nucleic Acid Cargo.bioRxiv : the preprint server for biology · 2026Article
- Measuring the selective packaging of RNA molecules by viral coat proteins in cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Exploring the Effects of Intersubunit Interface Mutations on Virus-Like Particle Structure and Stability.Biochemistry · 2024Article
- Magnetically Induced Thermal Effects on Tobacco Mosaic Virus-Based Nanocomposites for a Programmed Disassembly of Protein Cages.ACS applied bio materials · 2024Article
- Effect of coat-protein concentration on the self-assembly of bacteriophage MS2 capsids around RNA.Nanoscale · 2024Article
- Virus-like particle encapsulation of functional proteins: advances and applications.Theranostics · 2024Review
- DNA-origami-directed virus capsid polymorphism.Nature nanotechnology · 2023Article
- Article
- Systematic engineering of virus-like particles to identify self-assembly rules for shifting particle size.Virology · 2023Article
- Deep mutational scanning: A versatile tool in systematically mapping genotypes to phenotypes.Frontiers in genetics · 2023Review
- Fitness Landscape-Guided Engineering of Locally Supercharged Virus-like Particles with Enhanced Cell Uptake Properties.ACS chemical biology · 2022Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
- Viral Phrenology.Viruses · 2021Article
- The viral capsid as novel nanomaterials for drug delivery.Future science OA · 2021Review
- Role of Phage Capsid in the Resistance to UV-C Radiations.International journal of molecular sciences · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Self-assembling proteins are critical to biological systems and industrial technologies, but predicting how mutations affect self-assembly remains a significant challenge. Here, we report a technique, termed SyMAPS (Systematic Mutation and Assembled Particle Selection), that can be used to characterize the assembly competency of all single amino acid variants of a self-assembling viral structural protein. SyMAPS studies on the MS2 bacteriophage coat protein revealed a high-resolution fitness landscape that challenges some conventional assumptions of protein engineering. An additional round of selection identified a previously unknown variant (CP[T71H]) that is stable at neutral pH but less tolerant to acidic conditions than the wild-type coat protein. The capsids formed by this variant could be more amenable to disassembly in late endosomes or early lysosomes-a feature that is advantageous for delivery applications. In addition to providing a mutability blueprint for virus-like particles, SyMAPS can be readily applied to other self-assembling proteins.
Indexed as
Identifiers
What 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.