Evidence map›Paper›PMID 29599287›Full record

ArticleThe Journal of biological chemistry2018

The partial dissociation of MHC class I-bound peptides exposes their N terminus to trimming by endoplasmic reticulum aminopeptidase 1.

Athanasios Papakyriakou, Emma Reeves, Mary Beton, Halina Mikolajek, Leon Douglas, Grace Cooper, Tim Elliott, Jörn M Werner, Edward James

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-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

11 citing papers in PubMed, 26 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Athanasios PapakyriakouFrom the Centre for Biological Sciences, Faculty of Natural & Environmental Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.ORCID 0000-0003-3931-6232
Emma ReevesInstitute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom, and.
Mary BetonFrom the Centre for Biological Sciences, Faculty of Natural & Environmental Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.
Halina MikolajekFrom the Centre for Biological Sciences, Faculty of Natural & Environmental Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.
Leon DouglasInstitute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom, and.
Grace CooperInstitute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom, and.
Tim ElliottInstitute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom, and.
Jörn M WernerFrom the Centre for Biological Sciences, Faculty of Natural & Environmental Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom.ORCID 0000-0002-4712-1833
Edward JamesInstitute for Life Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdom, and eddjames@soton.ac.uk.ORCID 0000-0001-8638-7928
University of Southampton · GBUniversity Hospital Southampton NHS Foundation Trust · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L010402/1Cancer Research UK 16997Cancer Research UK A16997Medical Research Council MC_U117533887
6 · The paper itself

Abstract

Endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 process N-terminally extended antigenic precursors for optimal loading onto major histocompatibility complex class I (MHC I) molecules. We and others have demonstrated that ERAP1 processes peptides bound to MHC I, but the underlying mechanism is unknown. To this end, we utilized single-chain trimers (SCT) of the ovalbumin-derived epitope SIINFEKL (SL8) tethered to the H2-K

Indexed as

AminopeptidasesAntigen PresentationCrystallography, X-RayEpitopesHeLa CellsHistocompatibility Antigens Class IHumansMinor Histocompatibility AntigensModels, MolecularProtein ConformationProtein DomainsAminopeptidasesEpitopesERAP1 protein, humanHistocompatibility Antigens Class IMinor Histocompatibility Antigensantigen presentationantigen processingERAP1free energy calculationsH2-Kbmajor histocompatibility complex (MHC)molecular dynamicspeptide trimmingsingle chain trimerX-ray crystallography

Identifiers

PMID29599287
PMCPMC5961055
OpenAlexW2794996863

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.