Evidence map›Paper›PMID 21157433›Full record

ArticleThe EMBO journal2011

Atomic model of an infectious rotavirus particle.

Ethan C Settembre, James Z Chen, Philip R Dormitzer, Nikolaus Grigorieff, Stephen C Harrison

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers.

0numbers the graph read from it
0cells of the map it votes in
171citing papers in PubMed
8.4field-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

171 citing papers in PubMed, 303 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanism of membrane perforation in rotavirus cell entry.bioRxiv : the preprint server for biology · 2026
    Article
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111 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

5 authors at 4 institutions in 1 country.

Ethan C SettembreLaboratory of Molecular Medicine, Children's Hospital, Boston, MA, USA.
James Z Chen
Philip R Dormitzer
Nikolaus Grigorieff
Stephen C Harrison
Howard Hughes Medical Institute · USBoston Children's Hospital · USBrandeis University · USNova Medical (United States) · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALZ, THOMAS · 2001 to 2016
$23.7M
STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
Rotavirus VP4: Structure and functionR01AI053174 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2007
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS CA-13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI-53174NIAID NIH HHS R01 AI053174NIGMS NIH HHS P01 GM062580NIGMS NIH HHS P01 GM62580
6 · The paper itself

Abstract

Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 Å resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the β-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry.

Indexed as

Models, MolecularVirus InternalizationCapsid ProteinsCell MembraneCryoelectron MicroscopyCrystallographyProtein Structure, SecondaryRotavirusVirionCapsid ProteinsVP4 protein, Rotavirus

Identifiers

PMID21157433
PMCPMC3025467
OpenAlexW1838465562

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.