Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Critical role of endoplasmic reticulum aminopeptidase 1 in determining the length and sequence of peptides bound and presented by HLA-B27.

Arthritis & rheumatology (Hoboken, N.J.) - 1 Feb 2014

Chen Liye, Fischer Roman, Peng Yanchun, Reeves Emma, McHugh Kirsty, Ternette Nicola, Hanke Tomas, Dong Tao, Elliott Tim, Shastri Nilabh, Kollnberger Simon, James Edward, Kessler Benedikt, Bowness Paul

Abstract excerpt

OBJECTIVE: HLA-B27 and endoplasmic reticulum aminopeptidase 1 (ERAP1) are the two strongest genetic factors predisposing to ankylosing spondylitis (AS). A key aminopeptidase in class I major histocompatibility complex presentation, ERAP1 potentially contributes to the pathogenesis of AS by altering HLA-B27 peptide presentation. The aim of this study was to analyze the effects of ERAP1 on the HLA-B27 peptide...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aminopeptidases
Share to Epitopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Silencing

Share to HLA-B27 Antigen

Share to Minor Histocompatibility Antigens

Share to RNA, Small Interfering

Share to Spondylitis, Ankylosing

Share to T-Lymphocytes, Cytotoxic

Source

Identifiers

PMID: 24504800
DOI: 10.1002/art.38249

Genes

ERAP1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical role of endoplasmic reticulum aminopeptidase 1 in determining the length and sequence of peptides bound and presented by HLA-B27.PMID 24504800Read ↗

Dominant role of the ERAP1 polymorphism R528K in shaping the HLA-B27 Peptidome through differential processing determined by multiple peptide residues.Semantic proximity Read ↗

Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.Semantic proximity Read ↗

ERAP1 in ankylosing spondylitis: genetics, biology and pathogenetic role.Semantic proximity Read ↗

Endoplasmic reticulum aminopeptidase-1 alleles associated with increased risk of ankylosing spondylitis reduce HLA-B27 mediated presentation of multiple antigens.Semantic proximity Read ↗

The Human Leukocyte Antigen (HLA)-B27 Peptidome in Vivo, in Spondyloarthritis-susceptible HLA-B27 Transgenic Rats and the Effect of Erap1 Deletion.Semantic proximity Read ↗

Functional Interaction of the Ankylosing Spondylitis-Associated Endoplasmic Reticulum Aminopeptidase 2 With the HLA-B*27 Peptidome in Human Cells.Semantic proximity Read ↗

ERAP1: a potential therapeutic target for a myriad of diseasesSemantic proximity Read ↗

ERAP1 and ankylosing spondylitis.Semantic proximity Read ↗

ERAP1 structure, function and pathogenetic role in ankylosing spondylitis and other MHC-associated diseases.Semantic proximity Read ↗

Separate effects of the ankylosing spondylitis associated ERAP1 and ERAP2 aminopeptidases determine the influence of their combined phenotype on the HLA-B*27 peptidome.Semantic proximity Read ↗

Peptide handling by HLA-B27 subtypes influences their biological behavior, association with ankylosing spondylitis and susceptibility to endoplasmic reticulum aminopeptidase 1 (ERAP1).Semantic proximity Read ↗

ERAP1 enzyme-mediated trimming and structural analyses of MHC I–bound precursor peptides yield novel insights into antigen processing and presentationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.