ArticleJournal of virology2008
Visualization of the externalized VP2 N termini of infectious human parvovirus B19.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 79 citations in OpenAlex.
- Article
- Article
- Article
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- Infectious parvovirus B19 circulates in the blood coated with active host protease inhibitors.Nature communications · 2024Article
- Article
- Parvovirus B19 in Rheumatic Diseases.Microorganisms · 2024Review
- Therapeutic Potential of Engineered Virus-like Particles of Parvovirus B19.Pathogens (Basel, Switzerland) · 2023Review
- Bipartite genome and structural organization of the parvovirus Acheta domesticus segmented densovirus.Nature communications · 2023Article
- Tracking of Human Parvovirus B19 Virus-Like Particles Using Short Peptide Tags Reveals a Membrane-Associated Extracellular Release of These Particles.Journal of virology · 2023Article
- Capsid Structure of Aleutian Mink Disease Virus and Human Parvovirus 4: New Faces in the Parvovirus Family Portrait.Viruses · 2022Article
- Nuclear entry and egress of parvoviruses.Molecular microbiology · 2022Review
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Structural Dynamics and Activity of B19V VP1u during the pHs of Cell Entry and Endosomal Trafficking.Viruses · 2022Article
- Comparative structural, biophysical, and receptor binding study of true type and wild type AAV2.Journal of structural biology · 2021Article
- The N-terminal 5-68 amino acids domain of the minor capsid protein VP1 of human parvovirus B19 enters human erythroid progenitors and inhibits B19 infection.Journal of virology · 2021Article
- 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
- Article
- Structure of Parvovirus B19 Decorated by Fabs from a Human Antibody.Journal of virology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The structures of infectious human parvovirus B19 and empty wild-type particles were determined by cryoelectron microscopy (cryoEM) to 7.5-A and 11.3-A resolution, respectively, assuming icosahedral symmetry. Both of these, DNA filled and empty, wild-type particles contain a few copies of the minor capsid protein VP1. Comparison of wild-type B19 with the crystal structure and cryoEM reconstruction of recombinant B19 particles consisting of only the major capsid protein VP2 showed structural differences in the vicinity of the icosahedral fivefold axes. Although the unique N-terminal region of VP1 could not be visualized in the icosahedrally averaged maps, the N terminus of VP2 was shown to be exposed on the viral surface adjacent to the fivefold beta-cylinder. The conserved glycine-rich region is positioned between two neighboring, fivefold-symmetrically related VP subunits and not in the fivefold channel as observed for other parvoviruses.
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.