Evidence map›Paper›PMID 18336256›Full record

ReviewCurrent HIV research2008

Advances in the structural understanding of Vif proteins.

Pierre Barraud, Jean-Christophe Paillart, Roland Marquet, Carine Tisné

Open access · greenAbstract readReview
In one paragraph

Review in Current HIV research, 2008. 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
1.7field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Structural perspectives on HIV-1 Vif and APOBEC3 restriction factor interactions.Protein science : a publication of the Protein Society · 2020
    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 4 institutions in 1 country.

Pierre BarraudLaboratoire de Cristallographie et RMN biologiques, Université Paris-Descartes, CNRS UMR 8015, Paris, France.
Jean-Christophe Paillart
Roland Marquet
Carine Tisné
Architecture et Réactivité de l'arN · FRCentre National de la Recherche Scientifique · FRInstitut de Biologie Moléculaire et Cellulaire · FRLaboratoire de Cristallographie et RMN Biologiques · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multidomain HIV-1 Vif protein recruits several cellular partners to achieve neutralization of the antiviral activity of APOBEC3 proteins. Vif neutralizes APOBEC3G and APOBEC3F predominantly by forming an E3 ubiquitin ligase with Cullin5, ElonginB and ElonginC that targets these proteins for degradation by the ubiquitin-proteasome pathway. Vif associates with the Cullin5-ElonginB-ElonginC complex by binding directly to ElonginC via its SOCS-box motif and to Cullin5 via hydrophobic residues within a zinc-binding region formed by a conserved HCCH motif. The HIV-1 Vif-Cullin5-ElonginBC complex is then able to ubiquitinate the APOBEC3G factor bound to Vif by its N-terminal domain. In this review, we summarize the current knowledge about the structural determinants of Vif that allow it to interact with cellular and viral partners.

Indexed as

Amino Acid MotifsGene Products, vifHIV-1HIV-2HumansProtein BindingProtein Structure, TertiarySimian Immunodeficiency VirusGene Products, vif

Identifiers

PMID18336256
PMCPMC2704546
OpenAlexW2158361338

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.