| http://purl.uniprot.org/citations/17082617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17082617 | http://www.w3.org/2000/01/rdf-schema#comment | "B*2704 is strongly associated to ankylosing spondylitis in Asian populations. It differs from the main HLA-B27 allotype, B*2705, in three amino acid changes. We analyzed the influence of tapasin, TAP, and immunoproteasome induction on maturation, surface expression, and T cell allorecognition of B*2704 and compared some of these features with B*2705 and B*2706, allotypes not associated to disease. In the tapasin-deficient .220 cell line, this chaperone significantly influenced the extent of folding of B*2704 and B*2705, but not their egress from the endoplasmic reticulum. In contrast, B*2706 showed faster folding and no accumulation in the endoplasmic reticulum in the absence of tapasin. Surface expression of B*2704 was more tapasin dependent than B*2705. However, expression of free H chain decreased in the presence of this chaperone for B*2705 but not B*2704, suggesting that more suboptimal ligands were loaded on B*2705 in the absence of tapasin. Despite its influence on surface expression, tapasin had little effect on allorecognition of B*2704. Both surface expression and T cell recognition of B*2704 were critically dependent on TAP, as established with TAP-deficient and TAP-proficient T2 cells. Both immunoproteasome and surface levels of B*2704 were induced by IFN-gamma, but this had little effect on allorecognition. Thus, except for the differential effects of tapasin on surface expression, the tapasin, TAP, and immunoproteasome dependency of B*2704 for maturation, surface expression, and T cell recognition are similar to B*2705, indicating that basic immunological features are shared by the two major HLA-B27 allotypes associated to ankylosing spondylitis in human populations."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.177.10.7015"xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/author | "Vazquez M."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/author | "Galocha B."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/author | "Lopez de Castro J.A."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/author | "Montserrat V."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/author | "Marcilla M."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/pages | "7015-7023"xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/title | "HLA-B*2704, an allotype associated with ankylosing spondylitis, is critically dependent on transporter associated with antigen processing and relatively independent of tapasin and immunoproteasome for maturation, surface expression, and T cell recognition: relationship to B*2705 and B*2706."xsd:string |
| http://purl.uniprot.org/citations/17082617 | http://purl.uniprot.org/core/volume | "177"xsd:string |
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