Evidence map›Paper›PMID 10400786›Full record

ArticleJournal of virology1999

Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity.

R McKenna, N H Olson, P R Chipman, T S Baker, T F Booth, J Christensen, B Aasted, J M Fox, M E Bloom, J B Wolfinbarger and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 83 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

R McKennaDepartment of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom. mamckenna@ufl.edu
N H Olson
P R Chipman
T S Baker
T F Booth
J Christensen
B Aasted
J M Fox
M E Bloom
J B Wolfinbarger
M Agbandje-McKenna
National Institute of Allergy and Infectious Diseases · USPurdue University West Lafayette · USUniversity of Warwick · GB

Funding

Microscopy &Image Analysis of Unstained MacromoleculesR37GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2013
$5.6M
MICROSCOPY &IMAGE ANALYSIS OF UNSTAINED MACROMOLECULESR01GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 1985 to 2017
$4.3M
STRUCTURES OF ALPHAVIRUS SPIKES AND RECEPTORSP01AI035212 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI ROSSMANN, MICHAEL G · 1994 to 1997
–
NIAID NIH HHS P01 AI035212NIGMS NIH HHS GM33050NIGMS NIH HHS R01 GM033050NIGMS NIH HHS R37 GM033050
6 · The paper itself

Abstract

The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A resolution by cryo-electron microscopy and image reconstruction techniques. A structure-based sequence alignment of the VP2 capsid protein of canine parvovirus (CPV) provided a means to construct an atomic model of the ADVG-VP2 capsid. The ADVG-VP2 reconstruction reveals a capsid structure with a mean external radius of 128 A and several surface features similar to those found in human parvovirus B19 (B19), CPV, feline panleukopenia virus (FPV), and minute virus of mice (MVM). Dimple-like depressions occur at the icosahedral twofold axes, canyon-like regions encircle the fivefold axes, and spike-like protrusions decorate the threefold axes. These spikes are not present in B19, and they are more prominent in ADV compared to the other parvoviruses owing to the presence of loop insertions which create mounds near the threefold axes. Cylindrical channels along the fivefold axes of CPV, FPV, and MVM, which are surrounded by five symmetry-related beta-ribbons, are closed in ADVG-VP2 and B19. Immunoreactive peptides made from segments of the ADVG-VP2 capsid protein map to residues in the mound structures. In vitro tissue tropism and in vivo pathogenic properties of ADV map to residues at the threefold axes and to the wall of the dimples.

Indexed as

Protein Structure, SecondaryAleutian Mink DiseaseAleutian Mink Disease VirusAmino Acid SequenceAnimalsCapsidCapsid ProteinsCatsCell LineCryoelectron MicroscopyDogsHumansMiceModels, MolecularMolecular Sequence DataRecombinant Fusion ProteinsCapsid ProteinsRecombinant Fusion ProteinsVP2 protein, Aleutian mink disease virus

Identifiers

PMID10400786
PMCPMC112773
OpenAlexW1807754389

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.