Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype.
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Structural Basis for T Cell Alloreactivity among Three HLA-B14 and HLA-B27 AntigensDifferent Vaccine Vectors Delivering the Same Antigen Elicit CD8+ T Cell Responses with Distinct Clonotype and Epitope SpecificityCitrullination-dependent differential presentation of a self-peptide by HLA-B27 subtypesLoss of recognition by cross-reactive T cells and its relation to a C-terminus-induced conformational reorientation of an HLA-B*2705-bound peptideVitAL: Viterbi algorithm for de novo peptide designIndividual characterization of stably expanded T cell clones in ankylosing spondylitis patients.Distortion of the Major Histocompatibility Complex Class I Binding Groove to Accommodate an Insulin-derived 10-Mer PeptidePeptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis.Pathogenesis of ankylosing spondylitis.Novel HLA-B27-restricted epitopes from Chlamydia trachomatis generated upon endogenous processing of bacterial proteins suggest a role of molecular mimicry in reactive arthritis.The role of the unfolded protein response in axial spondyloarthritis.Functional Genomics and Its Bench-to-Bedside Translation Pertaining to the Identified Susceptibility Alleles and Loci in Ankylosing Spondylitis.The Ankylosing Spondylitis-associated HLA-B*2705 presents a B*0702-restricted EBV epitope and sustains the clonal amplification of cytotoxic T cells in patients.DockTope: a Web-based tool for automated pMHC-I modelling.Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.Characterization of a proteasome and TAP-independent presentation of intracellular epitopes by HLA-B27 moleculesExpression, purification and preliminary X-ray crystallographic analysis of the human major histocompatibility antigen HLA-B*1402 in complex with a viral peptide and with a self-peptideMolecular determinants of major histocompatibility complex class I complex stability: shaping antigenic features through short and long range electrostatic interactions.NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy.
P2860
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P2860
Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype.
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年論文
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2005年論文
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2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
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2005年论文
@wuu
2005年论文
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2005年论文
@zh-cn
name
Conformational dimorphism of s ...... se-associated HLA-B27 subtype.
@en
type
label
Conformational dimorphism of s ...... se-associated HLA-B27 subtype.
@en
prefLabel
Conformational dimorphism of s ...... se-associated HLA-B27 subtype.
@en
P2093
P2860
P50
P356
P1476
Conformational dimorphism of s ...... se-associated HLA-B27 subtype.
@en
P2093
Christine Rückert
Jacek Biesiadka
Maria Teresa Fiorillo
Roberto Moretti
Wolfram Saenger
P2860
P304
P356
10.1074/JBC.M508528200
P407
P577
2005-10-12T00:00:00Z