Evidence map›Paper›PMID 23898184›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Characterization of an early-stage fusion intermediate of Sindbis virus using cryoelectron microscopy.

Sheng Cao, Wei Zhang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

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  19. Article
  20. Fusion of Enveloped Viruses in Endosomes.Traffic (Copenhagen, Denmark) · 2016
    Review
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

2 authors.

Sheng CaoInstitute of Molecular Virology, University of Minnesota, Minneapolis, MN 55455, USA.
Wei Zhang

Funding

Structural Studies of Alphavirus Membrane Fusion In SituR21AI079473 · NIAID · UNIVERSITY OF MINNESOTA · PI ZHANG, WEI · 2009 to 2010
$404k
NIAID NIH HHS R21 AI079473NIAID NIH HHS R21AI079473
6 · The paper itself

Abstract

The sequential steps in the alphavirus membrane fusion pathway have been postulated based on the prefusion and postfusion crystal structures of the viral fusion protein E1 in conjunction with biochemical studies. However, the molecular structures of the hypothesized fusion intermediates have remained obscure due to difficulties inherent in the dynamic nature of the process. We developed an experimental system that uses liposomes as the target membrane to capture Sindbis virus, a prototypical alphavirus, in its membrane-binding form at pH 6.4. Cryoelectron micrograph analyses and 3D reconstructions showed that the virus retains its overall icosahedral structure at this mildly acidic pH, except in the membrane-binding region, where monomeric E1 associates with the target membrane and the E2 glycoprotein retains its original trimeric organization. The remaining E2 trimers may hinder E1 homotrimerization and are a potential target for antiviral drugs.

Indexed as

Models, MolecularCryoelectron MicroscopyHydrogen-Ion ConcentrationLiposomesSindbis VirusViral Fusion ProteinsLiposomesViral Fusion Proteinsclass II viral fusion proteinenveloped virusesimage processingprotein organizationviral entry

Identifiers

PMID23898184
PMCPMC3746934

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.