Evidence map›Paper›PMID 29088112›Full record

ReviewViruses2017

Hijacking of the Ubiquitin/Proteasome Pathway by the HIV Auxiliary Proteins.

Tanja Seissler, Roland Marquet, Jean-Christophe Paillart

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 72 citations in OpenAlex.

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  10. Delivery of gene editing therapeutics.Nanomedicine : nanotechnology, biology, and medicine · 2023
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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.

Tanja SeisslerUniversité de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, UPR 9002, IBMC-15 rue René Descartes, F-67000 Strasbourg, France. t.seissler@ibmc-cnrs.unistra.fr.
Roland MarquetUniversité de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, UPR 9002, IBMC-15 rue René Descartes, F-67000 Strasbourg, France. r.marquet@ibmc-cnrs.unistra.fr.ORCID 0000-0002-4209-3976
Jean-Christophe PaillartUniversité de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, UPR 9002, IBMC-15 rue René Descartes, F-67000 Strasbourg, France. jc.paillart@ibmc-cnrs.unistra.fr.ORCID 0000-0003-1647-8917
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome system (UPS) ensures regulation of the protein pool in the cell by ubiquitination of proteins followed by their degradation by the proteasome. It plays a central role in the cell under normal physiological conditions as well as during viral infections. On the one hand, the UPS can be used by the cell to degrade viral proteins, thereby restricting the viral infection. On the other hand, it can also be subverted by the virus to its own advantage, notably to induce degradation of cellular restriction factors. This makes the UPS a central player in viral restriction and counter-restriction. In this respect, the human immunodeficiency viruses (HIV-1 and 2) represent excellent examples. Indeed, many steps of the HIV life cycle are restricted by cellular proteins, some of which are themselves components of the UPS. However, HIV itself hijacks the UPS to mediate defense against several cellular restriction factors. For example, the HIV auxiliary proteins Vif, Vpx and Vpu counteract specific restriction factors by the recruitment of cellular UPS components. In this review, we describe the interplay between HIV and the UPS to illustrate its role in the restriction of viral infections and its hijacking by viral proteins for counter-restriction.

Indexed as

Host-Pathogen InteractionsAntiviral Restriction FactorsCarrier ProteinsHIV InfectionsHuman Immunodeficiency Virus ProteinsHumansProteasome Endopeptidase ComplexProtein BindingTripartite Motif ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesViral Regulatory and Accessory ProteinsAntiviral Restriction FactorsCarrier ProteinsHuman Immunodeficiency Virus ProteinsMARCHF8 protein, humanProteasome Endopeptidase ComplexTRIM5 protein, humanTripartite Motif ProteinsUbiquitinUbiquitin-Protein LigasesViral Regulatory and Accessory ProteinsAPOBECBST2/TetherinHIVMarch8proteasomerestriction factorsSAMHD1TRIM5αubiquitin

Identifiers

PMID29088112
PMCPMC5707529
OpenAlexW2766076083

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.