Evidence map›Paper›PMID 21777384›Full record

ReviewThe FEBS journal2011

The association of viral proteins with host cell dynein components during virus infection.

Javier Merino-Gracia, María F García-Mayoral, Ignacio Rodríguez-Crespo

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 2 pooled it
1.5field-weighted citation impact, top 20% 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

36 citing papers in PubMed, 2 syntheses or guidelines pooled it, 61 citations in OpenAlex.

  1. Pooled it
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  18. Journal of cell science · 2019
    Article
  19. Review
  20. Bicaudal D2 facilitates the cytoplasmic trafficking and nuclear import of HIV-1 genomes during infection.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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

3 authors at 2 institutions in 1 country.

Javier Merino-GraciaDepartamento de Bioquímica y Biología Molecular I, Universidad Complutense, Madrid, Spain.
María F García-Mayoral
Ignacio Rodríguez-Crespo
Universidad Complutense de Madrid · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

After fusion with the cellular plasma membrane or endosomal membranes, viral particles are generally too large to diffuse freely within the crowded cytoplasm environment. Thus, they will never reach the cell nucleus or the perinuclear areas where replication or reverse transcription usually takes place. It has been proposed that many unrelated viruses are transported along microtubules in a retrograde manner using the cellular dynein machinery or, at least, some dynein components. A putative employment of the dynein motor in a dynein-mediated transport has been suggested from experiments in which viral capsid proteins were used as bait in yeast two-hybrid screens using libraries composed of cellular proteins and dynein-associated chains were retrieved as virus-interacting proteins. In most cases DYNLL1, DYNLT1 or DYNLRB1 were identified as the dynein chains that interact with viral proteins. The importance of these dynein-virus interactions has been supported, in principle, by the observation that in some cases the dynein-interacting motifs of viral proteins altered by site-directed mutagenesis result in non-infective virions. Furthermore, overexpression of p50 dynamitin, which blocks the dynein-dynactin interaction, or incubation of infected cells with peptides that compete with viral polypeptides for dynein binding have been shown to alter the viral retrograde transport. Still, it remains to be proved that dynein light chains can bind simultaneously to incoming virions and to the dynein motor for retrograde transport to take place. In this review, we will analyse the association of viral proteins with dynein polypeptides and its implications for viral infection.

Indexed as

Virus Physiological PhenomenaAnimalsApoptosisBiological TransportCytopathogenic Effect, ViralDyneinsHumansMicrotubulesProtein Interaction Domains and MotifsProtein SubunitsViral ProteinsDyneinsProtein SubunitsViral Proteins

Identifiers

PMID21777384
PMCPMC7164101
OpenAlexW1647487758

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.