Evidence map›Paper›PMID 30076303›Full record

ArticleNature communications2018

A stochastic assembly model for Nipah virus revealed by super-resolution microscopy.

Qian Liu, Lei Chen, Hector C Aguilar, Keng C Chou

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

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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.

Qian LiuDepartment of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada.
Lei ChenDepartment of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada.
Hector C AguilarDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY, 14853, USA.
Keng C ChouDepartment of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada. kcchou@chem.ubc.ca.ORCID http://orcid.org/0000-0002-8782-5253
University of British Columbia · CACornell University · US

Funding

Mechanisms of Nipah virus fusion and entryR01AI109022 · NIAID · WASHINGTON STATE UNIVERSITY · PI AGUILAR-CARRENO, HECTOR · 2014 to 2024
$4.3M
NIAID NIH HHS R01 AI109022
6 · The paper itself

Abstract

Understanding virus assembly mechanisms is important for developing therapeutic interventions. Nipah virus (NiV) is of interest because of its high mortality rate and efficient human-human transmissions. The current model for most enveloped viruses suggests that matrix proteins (M) recruit attachment glycoproteins (G) and fusion glycoproteins (F) to the assembly site at the plasma membrane. Here we report an assembly model that differs in many aspects from the current one. Examining NiV proteins on the cell plasma membrane using super-resolution microscopy reveals that clusters of F and G are randomly distributed on the plasma membrane regardless of the presence or absence of M. Our data suggests a model in which the M molecules assemble at the plasma membrane to form virus-like particles (VLPs), while the incorporation of F and G into the nascent VLPs is stochastic.

Indexed as

Virus AssemblyAnimalsCell LineCell MembraneGlycoproteinsHeLa CellsHumansMicroscopyNipah VirusTransfectionViral Envelope ProteinsViral Fusion ProteinsViral Matrix ProteinsVirionF protein, Nipah virusGlycoproteinsViral Envelope ProteinsViral Fusion ProteinsViral Matrix Proteins

Identifiers

PMID30076303
PMCPMC6076310
OpenAlexW2886478099

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.