Evidence map›Paper›PMID 21768348›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Crystal structure of the human astrovirus capsid spike.

Jinhui Dong, Liping Dong, Ernesto Méndez, Yizhi Tao

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. TwoViruses · 2025
    Article
  8. Article
  9. Review
  10. Neonatal Fc receptor is a functional receptor for classical human astrovirus.Genes to cells : devoted to molecular & cellular mechanisms · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Complete genome sequence and phylogenetic analysis of a goose astrovirus isolate in China.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  19. Structure of the divergent human astrovirus MLB capsid spike.Structure (London, England : 1993) · 2022
    Article
  20. 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

4 authors at 2 institutions in 2 countries.

Jinhui DongDepartment of Biochemistry and Cell Biology, Rice University, 6100 Main Street, MS140, Houston, TX 77005, USA.
Liping Dong
Ernesto Méndez
Yizhi Tao
Rice University · USUniversidad Nacional Autónoma de México · MX

Funding

Structural basis of protein-primed RNA synthesis by birnavirusesR01AI067638 · NIAID · RICE UNIVERSITY · PI TAO, YIZHI JANE · 2007 to 2011
$1.6M
NIAID NIH HHS AI067638NIAID NIH HHS R01 AI067638
6 · The paper itself

Abstract

Astroviruses are single-stranded, plus-sense RNA viruses that infect both mammals and birds, causing gastroenteritis and other extraintestinal diseases. Clinical studies have established astroviruses as the second leading cause of viral diarrhea in young children. Here we report the crystal structure of the human astrovirus dimeric surface spike determined to 1.8-Å resolution. The overall structure of each spike/projection domain has a unique three-layered β-sandwiches fold, with a core, six-stranded β-barrel structure that is also found in the hepatitis E virus capsid protrusions, suggesting a closer phylogenetic relationship between these two viruses than previously acknowledged. Based on a hepatitis E virus capsid model, we performed homology modeling and produced a complete, T = 3 astrovirus capsid model with features remarkably similar to those observed in a cryoelectron microscopy reconstruction image of a human astrovirus. Mapping conserved residues onto the astrovirus projection domain revealed a putative receptor binding site with amino acid compositions characteristic for polysaccharide recognition. Our results will have an important impact on future characterization of astrovirus structure and function, and will likely have practical applications in the development of vaccines and antivirals.

Indexed as

Protein Structure, QuaternaryAvastrovirusCaco-2 CellsCapsidCapsid ProteinsCryoelectron MicroscopyCrystallizationDextran SulfateDose-Response Relationship, DrugHeparan SulfateHumansModels, MolecularProtein MultimerizationProtein SubunitsRecombinant ProteinsX-Ray DiffractionCapsid ProteinsDextran SulfateHeparan SulfateProtein SubunitsRecombinant Proteins

Identifiers

PMID21768348
PMCPMC3150915
OpenAlexW2068644948

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.