Evidence map›Paper›PMID 23926103›Full record

ArticleThe Journal of biological chemistry2013

Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection.

Mónica Gordón-Alonso, Vera Rocha-Perugini, Susana Álvarez, Ángeles Ursa, Nuria Izquierdo-Useros, Javier Martinez-Picado, María A Muñoz-Fernández, Francisco Sánchez-Madrid

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.6field-weighted citation impact, top 17% 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, 31 citations in OpenAlex.

  1. Trial
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  12. Article
  13. Role of Drebrin at the Immunological Synapse.Advances in experimental medicine and biology · 2017
    Review
  14. Drebrin and Spermatogenesis.Advances in experimental medicine and biology · 2017
    Article
  15. Review
  16. Article
  17. Review
  18. Molecular determinants of the ratio of inert to infectious virus particles.Progress in molecular biology and translational science · 2015
    Review
  19. Article
  20. 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

8 authors at 4 institutions in 1 country.

Mónica Gordón-AlonsoFrom the Servicio de Inmunología, Instituto de Investigación Sanitaria de la Princesa, Hospital Universitario de la Princesa, 28006 Madrid, Spain.
Vera Rocha-Perugini
Susana Álvarez
Ángeles Ursa
Nuria Izquierdo-Useros
Javier Martinez-Picado
María A Muñoz-Fernández
Francisco Sánchez-Madrid
Hospital Universitario de La Princesa · ESHospital General Universitario Gregorio Marañón · ESInstitut d'Investigació en Ciències de la Salut Germans Trias i Pujol · ESSpanish National Centre for Cardiovascular Research · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HIV-1 contact with target cells triggers F-actin rearrangements that are essential for several steps of the viral cycle. Successful HIV entry into CD4(+) T cells requires actin reorganization induced by the interaction of the cellular receptor/co-receptor complex CD4/CXCR4 with the viral envelope complex gp120/gp41 (Env). In this report, we analyze the role of the actin modulator drebrin in HIV-1 viral infection and cell to cell fusion. We show that drebrin associates with CXCR4 before and during HIV infection. Drebrin is actively recruited toward cell-virus and Env-driven cell to cell contacts. After viral internalization, drebrin clustering is retained in a fraction of the internalized particles. Through a combination of RNAi-based inhibition of endogenous drebrin and GFP-tagged expression of wild-type and mutant forms, we establish drebrin as a negative regulator of HIV entry and HIV-mediated cell fusion. Down-regulation of drebrin expression promotes HIV-1 entry, decreases F-actin polymerization, and enhances profilin local accumulation in response to HIV-1. These data underscore the negative role of drebrin in HIV infection by modulating viral entry, mainly through the control of actin cytoskeleton polymerization in response to HIV-1.

Indexed as

ActinsCD4 AntigensCytoskeletonHIV-1HIV InfectionsHumansJurkat CellsMicroscopy, ConfocalNeuropeptidesProtein BindingReceptors, CXCR4RNA, Small InterferingVirus InternalizationActinsCD4 AntigensCXCR4 protein, humandrebrinsNeuropeptidesReceptors, CXCR4RNA, Small InterferingActinCxcr4CytoskeletonHIV-1Virus Entry

Identifiers

PMID23926103
PMCPMC3784756
OpenAlexW2026916032

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.