Evidence map›Paper›PMID 20347598›Full record

ReviewCytokine2010

The functions of the HIV1 protein Vpr and its action through the DCAF1.DDB1.Cullin4 ubiquitin ligase.

Laurieann Casey, Xiaoyun Wen, Carlos M C de Noronha

Abstract readReview
In one paragraph

Review in Cytokine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

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  15. The restriction factors of human immunodeficiency virus.The Journal of biological chemistry · 2012
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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

3 authors at 1 institution in 1 country.

Laurieann CaseyCenter for Immunology and Microbial Disease, Albany Medical College, 43 New Scotland Avenue, Albany, NY 12208, USA.
Xiaoyun Wen
Carlos M C de Noronha
Albany Medical Center Hospital · US

Funding

Vpr as a Mediator Proteasomal DegradationR01AI073178 · NIAID · ALBANY MEDICAL COLLEGE · PI DE NORONHA, CARLOS M · 2007 to 2010
$1.4M
NIAID NIH HHS R01 AI073178NIAID NIH HHS R01AI073178
6 · The paper itself

Abstract

Among the proteins encoded by human and simian immunodeficiency viruses (HIV and SIV) at least three, Vif, Vpu and Vpr, subvert cellular ubiquitin ligases to block the action of anti-viral defenses. This review focuses on Vpr and its HIV2/SIV counterparts, Vpx and Vpr, which all engage the DDB1.Cullin4 ubiquitin ligase complex through the DCAF1 adaptor protein. Here, we discuss the multiple functions that have been linked to Vpr expression and summarize the current knowledge on the role of the ubiquitin ligase complex in carrying out a subset of these activities.

Indexed as

Amino Acid SequenceCarrier ProteinsCullin ProteinsDNA-Binding ProteinsGene Products, vprHIV-1HumansMolecular Sequence DataProtein Serine-Threonine KinasesUbiquitin-Protein LigasesVirus ReplicationCarrier ProteinsCullin ProteinsDCAF1 protein, humanDDB1 protein, humanDNA-Binding ProteinsGene Products, vprProtein Serine-Threonine KinasesUbiquitin-Protein Ligases

Identifiers

PMID20347598
PMCPMC2880205
OpenAlexW2088542873

What OpenQuestion holds

Textmetadata
LicenceTDM
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.