Evidence map›Paper›PMID 21508329›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.

Grazyna Kochan, Tobias Krojer, David Harvey, Roman Fischer, Liye Chen, Melanie Vollmar, Frank von Delft, Kathryn L Kavanagh, Matthew A Brown, Paul Bowness and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed, 4 pooled it
15.9field-weighted citation impact, top 1% 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

125 citing papers in PubMed, 4 syntheses or guidelines pooled it, 256 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Pooled it
  5. Trial
  6. Article
  7. Article
  8. Controlling intracellular processing to enhance spherical nucleic acid immune stimulation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
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  12. Article
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  14. The Role of Aminopeptidase ERAP1 in Human Pathology-A Review.Current issues in molecular biology · 2024
    Review
  15. Article
  16. Article
  17. Review
  18. Genome-Wide Analysis ofInternational journal of molecular sciences · 2023
    Article
  19. Review
  20. Article

65 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

13 authors at 5 institutions in 2 countries.

Grazyna KochanStructural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Headington OX3 7DQ, United Kingdom.
Tobias Krojer
David Harvey
Roman Fischer
Liye Chen
Melanie Vollmar
Frank von Delft
Kathryn L Kavanagh
Matthew A Brown
Paul Bowness
Paul Wordsworth
Benedikt M Kessler
Udo Oppermann
University of Oxford · GBGenomics England · GBNational Institute for Health Research · GBMRC Weatherall Institute of Molecular Medicine · GBThe University of Queensland · AU

Funding

Arthritis Research UK 18599Arthritis Research UK 18797Arthritis Research UK 19536CIHR 1097737Versus Arthritis 18599Wellcome TrustWellcome Trust 076113
6 · The paper itself

Abstract

Endoplasmatic reticulum aminopeptidase 1 (ERAP1) is a multifunctional enzyme involved in trimming of peptides to an optimal length for presentation by major histocompatibility complex (MHC) class I molecules. Polymorphisms in ERAP1 have been associated with chronic inflammatory diseases, including ankylosing spondylitis (AS) and psoriasis, and subsequent in vitro enzyme studies suggest distinct catalytic properties of ERAP1 variants. To understand structure-activity relationships of this enzyme we determined crystal structures in open and closed states of human ERAP1, which provide the first snapshots along a catalytic path. ERAP1 is a zinc-metallopeptidase with typical H-E-X-X-H-(X)(18)-E zinc binding and G-A-M-E-N motifs characteristic for members of the gluzincin protease family. The structures reveal extensive domain movements, including an active site closure as well as three different open conformations, thus providing insights into the catalytic cycle. A K(528)R mutant strongly associated with AS in GWAS studies shows significantly altered peptide processing characteristics, which are possibly related to impaired interdomain interactions.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAminopeptidasesAntigen PresentationCatalytic DomainCrystallography, X-RayHLA-B27 AntigenHumansMinor Histocompatibility AntigensModels, MolecularMutagenesis, Site-DirectedPolymorphism, Single NucleotideProtein ConformationProtein Processing, Post-TranslationalProtein Structure, TertiaryRecombinant ProteinsAminopeptidasesERAP1 protein, humanHLA-B27 AntigenMinor Histocompatibility AntigensRecombinant Proteins

Identifiers

PMID21508329
PMCPMC3093473
OpenAlexW1964156630

What OpenQuestion holds

Textmetadata
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.