Evidence map›Paper›PMID 10627545›Full record

ArticleJournal of virology2000

Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus.

D M Belnap, D J Filman, B L Trus, N Cheng, F P Booy, J F Conway, S Curry, C N Hiremath, S K Tsang, A C Steven and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 231 citations in OpenAlex.

  1. Particles of echovirus 18 open to release their genomes in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  9. ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Virion structure andJournal of virology · 2021
    Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. nanoDSF:Frontiers in microbiology · 2020
    Article
  17. Review
  18. Article
  19. Article
  20. Seneca Valley virus attachment and uncoating mediated by its receptor anthrax toxin receptor 1.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article

57 more citing papers are in PubMed but not listed here.

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.

D M BelnapLaboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
D J Filman
B L Trus
N Cheng
F P Booy
J F Conway
S Curry
C N Hiremath
S K Tsang
A C Steven
J M Hogle
Harvard University · USInstitute of Art · PLNational Institute of Arthritis and Musculoskeletal and Skin Diseases · US

Funding

Structural Analysis of Enterovirus Cell Entry PathwaysR01AI020566 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI HOGLE, JAMES M · 1985 to 2018
$9.0M
STRUCTURAL BIOLOGY OF VIRUS ASSEMBLYZ01AR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1987 to 2008
$3.0M
MOLECULAR GRAPHICS, COMPUTER MODELING, AND SEQUENCE ANALYSISZ01CT000090 · CIT · COMPUTER RESEARCH AND TECHNOLOGY · PI TRUS, BENES L · 1985 to 2008
$2.1M
HIGH-RESOLUTION CRYSTALLOGRAPHIC STUDIES OF POLIOVIRUSR37AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 1992 to 2001
$934k
Structual Analysis of Enterovirus Cell Entry PathwaysR21AI020566 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOGLE, JAMES M · 2002 to 2002
$258k
NIAID NIH HHS AI20566NIAID NIH HHS R01 AI020566NIAID NIH HHS R21 AI020566NIAID NIH HHS R37 AI020566Wellcome Trust
6 · The paper itself

Abstract

Upon interacting with its receptor, poliovirus undergoes conformational changes that are implicated in cell entry, including the externalization of the viral protein VP4 and the N terminus of VP1. We have determined the structures of native virions and of two putative cell entry intermediates, the 135S and 80S particles, at approximately 22-A resolution by cryo-electron microscopy. The 135S and 80S particles are both approximately 4% larger than the virion. Pseudoatomic models were constructed by adjusting the beta-barrel domains of the three capsid proteins VP1, VP2, and VP3 from their known positions in the virion to fit the 135S and 80S reconstructions. Domain movements of up to 9 A were detected, analogous to the shifting of tectonic plates. These movements create gaps between adjacent subunits. The gaps at the sites where VP1, VP2, and VP3 subunits meet are plausible candidates for the emergence of VP4 and the N terminus of VP1. The implications of these observations are discussed for models in which the externalized components form a transmembrane pore through which viral RNA enters the infected cell.

Indexed as

Membrane ProteinsCapsidCryoelectron MicroscopyCrystallography, X-RayImage Processing, Computer-AssistedModels, BiologicalModels, MolecularNucleic Acid ConformationPoliovirusProtein ConformationReceptors, VirusRNA, ViralVirionMembrane Proteinspoliovirus receptorReceptors, VirusRNA, Viral

Identifiers

PMID10627545
PMCPMC111469
OpenAlexW2165843771

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.