| http://purl.uniprot.org/citations/24352655 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24352655 | http://www.w3.org/2000/01/rdf-schema#comment | "ERAP1 polymorphism involving residues 528 and 575/725 is associated with ankylosing spondylitis among HLA-B27-positive individuals. We used four recombinant variants to address the combined effects of the K528R and D575N polymorphism on the processing of HLA-B27 ligands. The hydrolysis of a fluorogenic substrate, Arg-528/Asp-575 < Lys-528/Asp-575 < Arg-528/Asn-575 < Lys-528/Asn-575, indicated that the relative activity of variants carrying Arg-528 or Lys-528 depends on residue 575. Asp-575 conferred lower activity than Asn-575, but the difference depended on residue 528. The same hierarchy was observed with synthetic precursors of HLA-B27 ligands, but the effects were peptide-dependent. Sometimes the epitope yields were variant-specific at all times. For other peptides, concomitant generation and destruction led to similar epitope amounts with all the variants at long, but not at short, digestion times. The generation/destruction balance of two related HLA-B27 ligands was analyzed in vitro and in live cells. Their relative yields at long digestion times were comparable with those from HLA-B27-positive cells, suggesting that ERAP1 was a major determinant of the abundance of these peptides in vivo. The hydrolysis of fluorogenic and peptide substrates by an HLA-B27 ligand or a shorter peptide, respectively, was increasingly inhibited as a function of ERAP1 activity, indicating that residues 528 and 575 affect substrate inhibition of ERAP1 trimming. The significant and complex effects of co-occurring ERAP1 polymorphisms on multiple HLA-B27 ligands, and their potential to alter the immunological and pathogenetic features of HLA-B27 as a function of the ERAP1 context, explain the epistatic association of both molecules in ankylosing spondylitis."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.529610"xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/author | "Lopez de Castro J.A."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/author | "Gomez-Molina P."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/author | "Martin-Esteban A."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/author | "Sanz-Bravo A."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/pages | "3978-3990"xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/title | "Combined effects of ankylosing spondylitis-associated ERAP1 polymorphisms outside the catalytic and peptide-binding sites on the processing of natural HLA-B27 ligands."xsd:string |
| http://purl.uniprot.org/citations/24352655 | http://purl.uniprot.org/core/volume | "289"xsd:string |
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