Evidence map›Paper›PMID 23545452›Full record

ReviewMolecular immunology2013

Antigenic peptide trimming by ER aminopeptidases--insights from structural studies.

Efstratios Stratikos, Lawrence J Stern

Abstract readReview
In one paragraph

Review in Molecular immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

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  8. How a tailor achieves the perfect fit.The Journal of biological chemistry · 2020
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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

2 authors at 2 institutions in 2 countries.

Efstratios StratikosNational Center for Scientific Research Demokritos, Athens, Greece. stratos@rrp.demokritos.gr
Lawrence J Stern
National Centre of Scientific Research "Demokritos" · GRUniversity of Massachusetts Chan Medical School · US

Funding

Structure and Function of MHC ProteinsR37AI038996 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J. · 2008 to 2017
$4.1M
Structure and Function of Class II MHC ProteinsR01AI038996 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J · 1996 to 2006
$1.6M
Structure and Function of Class II MHC ProteinsR56AI038996 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J · 2007 to 2007
$324k
NIAID NIH HHS AI38996NIAID NIH HHS R01 AI038996NIAID NIH HHS R37 AI038996
6 · The paper itself

Abstract

Generation and destruction of antigenic peptides by ER resident aminopeptidases ERAP1 and ERAP2 have been shown in the last few years to be important for the correct functioning and regulation of the adaptive immune response. These two highly homologous aminopeptidases appear to have evolved complex mechanisms well suited for their biological role in antigen presentation. Furthermore, polymorphic variability in these enzymes appears to affect their function and predispose individuals to disease. This review discusses our current understanding of the molecular mechanisms behind ERAP1/2 function as suggested by several recently determined crystallographic structures of these enzymes.

Indexed as

Adaptive ImmunityAminopeptidasesAnimalsAntigensEndoplasmic ReticulumHumansMinor Histocompatibility AntigensModels, MolecularPeptide FragmentsAminopeptidasesAntigensERAP1 protein, humanERAP2 protein, humanMinor Histocompatibility AntigensPeptide Fragments

Identifiers

PMID23545452
PMCPMC3657621
OpenAlexW2026074167

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.