Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
about
Multimeric structures of HLA-G isoforms function through differential binding to LILRB receptorsHLA-B27-associated reactive arthritis: pathogenetic and clinical considerationsKennedy Institute of Rheumatology Division, Imperial College London, 12-13 November 2003: towards a molecular toolkit for studying lymphocyte function in inflammatory arthritisUse of HLA-B27 tetramers to identify low-frequency antigen-specific T cells in Chlamydia-triggered reactive arthritis.Aetiology and pathogenesis of reactive arthritis: role of non-antigen-presenting effects of HLA-B27Ankylosing spondylitis: A state of the art factual backboneHLA-B27 and psoriatic disease: a modern view of an old relationshipHLA-B27 misfolding and ankylosing spondylitisHLA-B27-Homodimer-Specific Antibody Modulates the Expansion of Pro-Inflammatory T-Cells in HLA-B27 Transgenic RatsFrom HLA-B27 to spondyloarthritis: a journey through the ER.Inhibiting HLA-B27 homodimer-driven immune cell inflammation in spondylarthritis.Functionally distinct ERAP1 allotype combinations distinguish individuals with Ankylosing Spondylitis.Pathogenicity of Misfolded and Dimeric HLA-B27 MoleculesTh17 cells expressing KIR3DL2+ and responsive to HLA-B27 homodimers are increased in ankylosing spondylitis.Analysis of the CD8+ T cell response to the G1 domain of aggrecan in ankylosing spondylitis.Association of the programmed cell death 1 (PDCD1) gene polymorphism with ankylosing spondylitis in the Korean population.The Leukocyte Immunoglobulin-Like Receptor Family Member LILRB5 Binds to HLA-Class I Heavy Chains.Mechanisms of Disease: the immunopathogenesis of spondyloarthropathies.Silencing or inhibition of endoplasmic reticulum aminopeptidase 1 (ERAP1) suppresses free heavy chain expression and Th17 responses in ankylosing spondylitis.Activation-Induced Killer Cell Immunoglobulin-like Receptor 3DL2 Binding to HLA-B27 Licenses Pathogenic T Cell Differentiation in Spondyloarthritis.KIR3DL2 binds to HLA-B27 dimers and free H chains more strongly than other HLA class I and promotes the expansion of T cells in ankylosing spondylitisAnkylosing spondylitis: from cells to genesPeptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis.HLA-B27 misfolding and spondyloarthropathies.The arthritis-associated HLA-B*27:05 allele forms more cell surface B27 dimer and free heavy chain ligands for KIR3DL2 than HLA-B*27:09.A homodimeric complex of HLA-G on normal trophoblast cells modulates antigen-presenting cells via LILRB1.Combined effects of ankylosing spondylitis-associated ERAP1 polymorphisms outside the catalytic and peptide-binding sites on the processing of natural HLA-B27 ligandsThe multi-faceted nature of HLA class I dimer molecules.ERAP1 in the pathogenesis of ankylosing spondylitis.Endoplasmic reticulum aminopeptidases in the pathogenesis of ankylosing spondylitis.Polymorphisms in the F Pocket of HLA-B27 Subtypes Strongly Affect Assembly, Chaperone Interactions, and Heavy-Chain Misfolding.A dual chain chimeric antigen receptor (CAR) in the native antibody format for targeting immune cells towards cancer cells without the need of an scFv.Understanding inflammation in juvenile idiopathic arthritis: How immune biomarkers guide clinical strategies in the systemic onset subtype.F pocket flexibility influences the tapasin dependence of two differentially disease-associated MHC Class I proteins.The D0 Ig-like domain plays a central role in the stronger binding of KIR3DL2 to B27 free H chain dimers.Peptide handling by HLA-B27 subtypes influences their biological behavior, association with ankylosing spondylitis and susceptibility to endoplasmic reticulum aminopeptidase 1 (ERAP1).Causes and consequences of endoplasmic reticulum stress in rheumatic disease.Critical role of endoplasmic reticulum aminopeptidase 1 in determining the length and sequence of peptides bound and presented by HLA-B27.Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.
P2860
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P2860
Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Lymphoblastoid cells express H ...... following endosomal recycling.
@en
type
label
Lymphoblastoid cells express H ...... following endosomal recycling.
@en
prefLabel
Lymphoblastoid cells express H ...... following endosomal recycling.
@en
P2093
P356
P1476
Lymphoblastoid cells express H ...... following endosomal recycling
@en
P2093
Andrew J McMichael
Chen Au Peh
Lucy A Bird
Simon Kollnberger
P304
P356
10.1002/EJI.200323678
P407
P577
2003-03-01T00:00:00Z