Evidence map›Paper›PMID 22727420›Full record

ReviewProgress in molecular biology and translational science2012

Immunoproteasomes: structure, function, and antigen presentation.

Deborah A Ferrington, Dale S Gregerson

Abstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 255 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
255citing papers in PubMed, 3 pooled it
–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

255 citing papers in PubMed, 3 syntheses or guidelines pooled it.

  1. Pooled it
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  16. Aberrant SUMOylation Restricts the Targetable Cancer Immunopeptidome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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195 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

2 authors.

Deborah A FerringtonDepartment of Ophthalmology, University of Minnesota, Minneapolis, Minnesota, USA.
Dale S Gregerson

Funding

SIGNIFICANCE OF IMMUNOLOGICAL SEQUESTRATION IN THE EYER01EY011542 · NEI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI GREGERSON, DALE SANNES · 1996 to 2010
$3.8M
Proteasome Function in the Aging RetinaR01EY013623 · NEI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI FERRINGTON, DEBORAH ANN · 2003 to 2010
$2.2M
Immune-mediated Neuroprotection of Retinal Ganglion CellsR01EY021003 · NEI · UNIVERSITY OF MINNESOTA · PI GREGERSON, DALE SANNES · 2010 to 2012
$1.3M
Immunoproteasome: A key component of the cellular stress responseR21AG032391 · NIA · UNIVERSITY OF MINNESOTA · PI FERRINGTON, DEBORAH ANN · 2008 to 2009
$315k
NEI NIH HHS R01 EY011542NEI NIH HHS R01 EY013623NEI NIH HHS R01 EY021003NIA NIH HHS R21 AG032391
6 · The paper itself

Abstract

Immunoproteasomes contain replacements for the three catalytic subunits of standard proteasomes. In most cells, oxidative stress and proinflammatory cytokines are stimuli that lead to elevated production of immunoproteasomes. Immune system cells, especially antigen-presenting cells, express a higher basal level of immunoproteasomes. A well-described function of immunoproteasomes is to generate peptides with a hydrophobic C terminus that can be processed to fit in the groove of MHC class I molecules. This display of peptides on the cell surface allows surveillance by CD8 T cells of the adaptive immune system for pathogen-infected cells. Functions of immunoproteasomes, other than generating peptides for antigen presentation, are emerging from studies in immunoproteasome-deficient mice, and are complemented by recently described diseases linked to mutations or single-nucleotide polymorphisms in immunoproteasome subunits. Thus, this growing body of literature suggests a more pleiotropic role in cell function for the immunoproteasome.

Indexed as

Amino Acid SequenceAnimalsAntigen PresentationAntigen-Presenting CellsCatalytic DomainDiseaseGene Expression RegulationHumansMolecular Sequence DataProteasome Endopeptidase ComplexProteasome Endopeptidase Complex

Identifiers

PMID22727420
PMCPMC4405001

What OpenQuestion holds

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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.