Evidence map›Paper›PMID 10402464›Full record

ArticleThe Journal of cell biology1999

Intracellular localization of proteasomal degradation of a viral antigen.

L C Antón, U Schubert, I Bacík, M F Princiotta, P A Wearsch, J Gibbs, P M Day, C Realini, M C Rechsteiner, J R Bennink and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

77 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Article
  8. Review
  9. Varied Role of Ubiquitylation in Generating MHC Class I Peptide Ligands.Journal of immunology (Baltimore, Md. : 1950) · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Endogenous viral antigen processing generates peptide-specific MHC class I cell-surface clusters.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. MHC class I antigen processing distinguishes endogenous antigens based on their translation from cellular vs. viral mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Review

17 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 2 countries.

L C AntónLaboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.
U Schubert
I Bacík
M F Princiotta
P A Wearsch
J Gibbs
P M Day
C Realini
M C Rechsteiner
J R Bennink
J W Yewdell
National Institute of Allergy and Infectious Diseases · USUniversity of Utah · USLeibniz Institute of Virology (LIV) · DENational Cancer Institute · US

Funding

Proteolytic Generation Of Antigenic PeptidesZIAAI000658 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI BENNINK, JACK R · 2009 to 2012
$1.9M
PROTEOLYTIC GENERATION OF ANTIGENIC PEPTIDESZ01AI000658 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI BENNINK, JACK R · 1992 to 2008
$1.1M
6 · The paper itself

Abstract

To better understand proteasomal degradation of nuclear proteins and viral antigens we studied mutated forms of influenza virus nucleoprotein (NP) that misfold and are rapidly degraded by proteasomes. In the presence of proteasome inhibitors, mutated NP (dNP) accumulates in highly insoluble ubiquitinated and nonubiquitinated species in nuclear substructures known as promyelocytic leukemia oncogenic domains (PODs) and the microtubule organizing center (MTOC). Immunofluorescence revealed that dNP recruits proteasomes and a selective assortment of molecular chaperones to both locales, and that a similar (though less dramatic) effect is induced by proteasome inhibitors in the absence of dNP expression. Biochemical evidence is consistent with the idea that dNP is delivered to PODs/MTOC in the absence of proteasome inhibitors. Restoring proteasome activity while blocking protein synthesis results in disappearance of dNP from PODs and the MTOC and the generation of a major histocompatibility complex class I-bound peptide derived from dNP but not NP. These findings demonstrate that PODs and the MTOC serve as sites of proteasomal degradation of misfolded dNP and probably cellular proteins as well, and imply that antigenic peptides are generated at one or both of these sites.

Indexed as

Antigen PresentationNucleoproteinsAntigens, ViralCanavanineCentrosomeCysteine EndopeptidasesEnzyme InhibitorsFluorescent Antibody TechniqueHistocompatibility Antigens Class IHumansLeupeptinsMolecular ChaperonesMultienzyme ComplexesMutationNucleocapsid ProteinsOrthomyxoviridaeAntigens, Viralbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCanavanineCysteine EndopeptidasesEnzyme InhibitorsHistocompatibility Antigens Class ILeupeptinsMolecular ChaperonesMultienzyme ComplexesNucleocapsid ProteinsNucleoproteinsPeptide FragmentsProteasome Endopeptidase ComplexUbiquitinsViral Core Proteins

Identifiers

PMID10402464
PMCPMC2199725
OpenAlexW2156681015

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.