ArticleJournal of virology2011
Structure of a packaging-defective mutant of minute virus of mice indicates that the genome is packaged via a pore at a 5-fold axis.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 61 citations in OpenAlex.
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Development of canine parvovirus-2-based recombinant pseudoviruses expression system: a potential vaccine platform.Veterinary research · 2026Article
- Insights into the AAV packaging mechanism: Cryo-EM Structure of the AAV2 Rep-Capsid Packaging Complex.bioRxiv : the preprint server for biology · 2025Article
- Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling.Virology journal · 2025Article
- Article
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- Article
- Antiviral alternatives against important members of the subfamily Parvovirinae: a review.Archives of virology · 2024Review
- Assembly of Structurally Simple Icosahedral Viruses.Sub-cellular biochemistry · 2024Review
- The Structures and Functions of Parvovirus Capsids and Missing Pieces: the Viral DNA and Its Packaging, Asymmetrical Features, Nonprotein Components, and Receptor or Antibody Binding and Interactions.Journal of virology · 2023Review
- Bipartite genome and structural organization of the parvovirus Acheta domesticus segmented densovirus.Nature communications · 2023Article
- Article
- Cryo-EM structure of adeno-associated virus 4 at 2.2 Å resolution.Acta crystallographica. Section D, Structural biology · 2023Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- A new perspective on the evolution and diversity of the genusVirus evolution · 2022Article
- Adeno-associated Virus 9 Structural Rearrangements Induced by Endosomal Trafficking pH and Glycan Attachment.Journal of virology · 2021Article
- Concepts to Reveal Parvovirus-Nucleus Interactions.Viruses · 2021Review
- The VP1u of Human Parvovirus B19: A Multifunctional Capsid Protein with Biotechnological Applications.Viruses · 2020Review
- Molecular biology and structure of a novel penaeid shrimp densovirus elucidate convergent parvoviral host capsid evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural Characterization of Cuta- and Tusavirus: Insight into Protoparvoviruses Capsid Morphology.Viruses · 2020Article
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
The parvovirus minute virus of mice (MVM) packages a single copy of its linear single-stranded DNA genome into preformed capsids, in a process that is probably driven by a virus-encoded helicase. Parvoviruses have a roughly cylindrically shaped pore that surrounds each of the 12 5-fold vertices. The pore, which penetrates the virion shell, is created by the juxtaposition of 10 antiparallel β-strands, two from each of the 5-fold-related capsid proteins. There is a bottleneck in the channel formed by the symmetry-related side chains of the leucines at position 172. We report here the X-ray crystal structure of the particles produced by a leucine-to-tryptophan mutation at position 172 and the analysis of its biochemical properties. The mutant capsid had its 5-fold channel blocked, and the particles were unable to package DNA, strongly suggesting that the 5-fold pore is the packaging portal for genome entry.
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.