Evidence map›Paper›PMID 21468303›Full record

ArticlePLoS biology2011

Enzymatic blockade of the ubiquitin-proteasome pathway.

Robert Ernst, Jasper H L Claessen, Britta Mueller, Sumana Sanyal, Eric Spooner, Annemarthe G van der Veen, Oktay Kirak, Christian D Schlieker, Wilhelm A Weihofen, Hidde L Ploegh

Abstract read
In one paragraph

Article in PLoS biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
–field-weighted citation impact
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

59 citing papers in PubMed.

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  19. Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling.Proceedings of the National Academy of Sciences of the United States of America · 2016
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Robert ErnstWhitehead Institute for Biomedical Research, Cambridge, Massachusetts, USA.
Jasper H L Claessen
Britta Mueller
Sumana Sanyal
Eric Spooner
Annemarthe G van der Veen
Oktay Kirak
Christian D Schlieker
Wilhelm A Weihofen
Hidde L Ploegh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-dependent processes control much of cellular physiology. We show that expression of a highly active, Epstein-Barr virus-derived deubiquitylating enzyme (EBV-DUB) blocks proteasomal degradation of cytosolic and ER-derived proteins by preemptive removal of ubiquitin from proteasome substrates, a treatment less toxic than the use of proteasome inhibitors. Recognition of misfolded proteins in the ER lumen, their dislocation to the cytosol, and degradation are usually tightly coupled but can be uncoupled by the EBV-DUB: a misfolded glycoprotein that originates in the ER accumulates in association with cytosolic chaperones as a deglycosylated intermediate. Our data underscore the necessity of a DUB activity for completion of the dislocation reaction and provide a new means of inhibition of proteasomal proteolysis with reduced cytotoxicity.

Indexed as

Signal TransductionBiocatalysisCell LineEndoplasmic ReticulumGlycoproteinsHerpesvirus 4, HumanHumansMolecular ChaperonesProteasome Endopeptidase ComplexProtein FoldingProtein Processing, Post-TranslationalProtein TransportSubstrate SpecificityUbiquitinViral ProteinsGlycoproteinsMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinViral Proteins

Identifiers

PMID21468303
PMCPMC3066133

What OpenQuestion holds

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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.