Evidence map›Paper›PMID 25019511›Full record

ArticlePloS one2014

Visualization and analysis of hepatitis C virus structural proteins at lipid droplets by super-resolution microscopy.

Dennis Eggert, Kathrin Rösch, Rudolph Reimer, Eva Herker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Measles virus reprograms CD4Frontiers in cell and developmental biology · 2026
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  11. Superresolution imaging of viral protein trafficking.Medical microbiology and immunology · 2015
    Review
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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 1 country.

Dennis EggertHeinrich-Pette-Institute, Leibniz Institute for Experimental Virology, University of Hamburg, Hamburg, Germany; Institute of Physical Chemistry, University of Hamburg, Hamburg, Germany.
Kathrin RöschHeinrich-Pette-Institute, Leibniz Institute for Experimental Virology, University of Hamburg, Hamburg, Germany.
Rudolph ReimerHeinrich-Pette-Institute, Leibniz Institute for Experimental Virology, University of Hamburg, Hamburg, Germany.
Eva HerkerHeinrich-Pette-Institute, Leibniz Institute for Experimental Virology, University of Hamburg, Hamburg, Germany.
Leibniz Institute of Virology (LIV) · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytosolic lipid droplets are central organelles in the Hepatitis C Virus (HCV) life cycle. The viral capsid protein core localizes to lipid droplets and initiates the production of viral particles at lipid droplet-associated ER membranes. Core is thought to encapsidate newly synthesized viral RNA and, through interaction with the two envelope proteins E1 and E2, bud into the ER lumen. Here, we visualized the spatial distribution of HCV structural proteins core and E2 in vicinity of small lipid droplets by three-color 3D super-resolution microscopy. We observed and analyzed small areas of colocalization between the two structural proteins in HCV-infected cells with a diameter of approximately 100 nm that might represent putative viral assembly sites.

Indexed as

HepacivirusLipid DropletsMicroscopy, ConfocalMicroscopy, FluorescenceViral Structural ProteinsViral Structural Proteins

Identifiers

PMID25019511
PMCPMC4094509
OpenAlexW2093278823

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.