Evidence map›Paper›PMID 21367906›Full record

ArticleJournal of virology2011

Structure of Bombyx mori densovirus 1, a silkworm pathogen.

Bärbel Kaufmann, Mohamed El-Far, Pavel Plevka, Valorie D Bowman, Yi Li, Peter Tijssen, Michael G Rossmann

Open access · greenAbstract read
In one paragraph

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. 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 · 2020
    Article
  7. Article
  8. Viruses · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Analysis of phases in the structure determination of an icosahedral virus.Acta crystallographica. Section D, Biological crystallography · 2011
    Article
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

7 authors at 2 institutions in 2 countries.

Bärbel KaufmannDepartment of Biological Sciences, Purdue University, 240 S. Martin Jischke Drive, West Lafayette, IN 47907-2032, USA.
Mohamed El-Far
Pavel Plevka
Valorie D Bowman
Yi Li
Peter Tijssen
Michael G Rossmann
Purdue University West Lafayette · USInstitut National de la Recherche Scientifique · CA

Funding

X-RAY STUDY OF HORMONE-RECEPTOR AND PROTEIN-ANTIBODY COMPLEXESP41RR007707 · NCRR · UNIVERSITY OF CHICAGO · PI SRAJER, VUKICA · 2002 to 2011
$17.3M
STRUCTURE OF A SMALL SPHERICAL VIRUSR37AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI ROSSMANN, MICHAEL G · 1986 to 2015
$6.6M
STRUCTURE OF A SMALL SPHERICAL VIRUSR01AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1985 to 2020
$2.4M
PARVOVIRUS STRUCTURE, CAPSID ASSEMBLY, AND RECEPTORSR01AI033468 · NIAID · CORNELL UNIVERSITY ITHACA · PI PARRISH, COLIN R. · 1993 to 2007
$2.3M
NCRR NIH HHS P41 RR007707NCRR NIH HHS RR007707NIAID NIH HHS AI 11219NIAID NIH HHS AI 33468NIAID NIH HHS R01 AI011219NIAID NIH HHS R01 AI033468NIAID NIH HHS R37 AI011219
6 · The paper itself

Abstract

Bombyx mori densovirus 1 (BmDNV-1), a major pathogen of silkworms, causes significant losses to the silk industry. The structure of the recombinant BmDNV-1 virus-like particle has been determined at 3.1-Å resolution using X-ray crystallography. It is the first near-atomic-resolution structure of a virus-like particle within the genus Iteravirus. The particles consist of 60 copies of the 55-kDa VP3 coat protein. The capsid protein has a β-barrel "jelly roll" fold similar to that found in many diverse icosahedral viruses, including archaeal, bacterial, plant, and animal viruses, as well as other parvoviruses. Most of the surface loops have little structural resemblance to other known parvovirus capsid proteins. In contrast to vertebrate parvoviruses, the N-terminal β-strand of BmDNV-1 VP3 is positioned relative to the neighboring 2-fold related subunit in a "domain-swapped" conformation, similar to findings for other invertebrate parvoviruses, suggesting domain swapping is an evolutionarily conserved structural feature of the Densovirinae.

Indexed as

AnimalsBombyxCrystallography, X-RayDensovirinaeMacromolecular SubstancesModels, MolecularProtein Structure, QuaternaryVirosomesMacromolecular SubstancesVirosomes

Identifiers

PMID21367906
PMCPMC3126189
OpenAlexW2140911333

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.