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Binding of peptides naturally presented by HLA–B27 to the differentially disease–associated B*2704 and B*2706 subtypes, and to mutants mimicking their polymorphism

Data up to Jan 2025

Published1996
Citations38
References42

Total Citations Per Year

Abstract

References (42)

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1994 • 46 citations

Clonal analysis of alloreactive T cell responses against the closely related B*2705 and B*2703 subtypes. Implications for HLA-B27 association to spondyloarthropathy.

1994 • 46 citations

Changes in the repertoire of peptides bound to HLA-B27 subtypes and to site-specific mutants inside and outside pocket B.

1993 • 41 citations

Pocket Mutations of HLA-B27 Show That Anchor Residues Act Cumulatively to Stabilize Peptide Binding

1994 • 39 citations

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1994 • 37 citations

Modulation of peptide binding by HLA‐B27 polymorphism in pockets A and B, and peptide specificity of B*2703

1995 • 33 citations

The nucleotide sequence of HLA-B * 2704 reveals a new amino acid substitution in exon 4 which is also present in HLA-B * 2706

1996 • 22 citations

Peptide-presenting similarities among functionally distant HLA-B27 subtypes revealed by alloreactive T lymphocytes of unusual specificity.

1992 • 19 citations

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1995 • 17 citations

Structure of HLA‐B27‐specific T cell epitopes. Antigen presentation in B2703 is limited mostly to a subset of the antigenic determinants on B2705

1994 • 15 citations

The Asp116-His116 substitution in a novel HLA-B27 subtype influences the acceptance of the peptide C-terminal anchor

1995 • 13 citations

Nucleotide sequence of HLA-B * 2706

1994 • 13 citations

Differences in peptide-binding specificity of two ankylosing spondylitis-associated HLA-B27 subtypes

1995 • 13 citations

Nucleotide sequence of HLA-B * 2706

1995 • 13 citations

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Binding of peptides naturally presented by HLA–B27 to the differentially… (1996) – Tissue Antigens | Metascience Observatory Explorer