B-POCKET TRANSPLANT FROM HLA-A2 INTO B27 CHANGES REQUIREMENT FOR P-2 ANCHOR RESIDUE IN PEPTIDE PRESENTATION

B-POCKET TRANSPLANT FROM HLA-A2 INTO B27 CHANGES REQUIREMENT FOR P-2 ANCHOR RESIDUE IN PEPTIDE PRESENTATION

Xehetasun bibliografikoak
Egile Nagusiak:	Colbert, R, Rowlandjones, S, Mcmichael, A, Frelinger, J
Formatua:	Journal article
Argitaratua:	1993

Antzeko izenburuak

Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.
nork: Colbert, R, et al.
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Allele-specific B pocket transplant in class I major histocompatibility complex protein changes requirement for anchor residue at P2 of peptide.
nork: Colbert, R, et al.
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DIFFERENCES IN PEPTIDE PRESENTATION BETWEEN B27 SUBTYPES - THE IMPORTANCE OF THE P1 SIDE-CHAIN IN MAINTAINING HIGH-AFFINITY PEPTIDE BINDING TO B-ASTERISK-2703
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Structural homologies between two HLA B27-restricted peptides suggest residues important for interaction with HLA B27.
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Differences in peptide presentation between B27 subtypes: the importance of the P1 side chain in maintaining high affinity peptide binding to B*2703.
nork: Colbert, R, et al.
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Naturally occurring A pocket polymorphism in HLA-B*2703 increases the dependence on an accessory anchor residue at P1 for optimal binding of nonamer peptides.
nork: Griffin, T, et al.
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An HLA-B35-restricted epitope modified at an anchor residue results in an antagonist peptide.
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Significance of the six peptide-binding pockets of HLA-A2.1 in influenza A matrix peptide-specific cytotoxic T-lymphocyte reactivity.
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Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27.
nork: Bowness, P, et al.
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The solvent-inaccessible Cys67 residue of HLA-B27 contributes to T cell recognition of HLA-B27/peptide complexes.
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IDENTIFICATION OF T-CELL RECEPTOR RECOGNITION RESIDUES FOR AN INFLUENZA-VIRUS NONAMER PEPTIDE EPITOPE PRESENTED BY HLA B27
nork: Bowness, P, et al.
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Interaction of HLA-B27 homodimers with KIR3DL1 and KIR3DL2, unlike HLA-B27 heterotrimers, is independent of the sequence of bound peptide.
nork: Kollnberger, S, et al.
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Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies.
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HLA class I typing by PCR: HLA-B27 and an African B27 subtype.
nork: Hill, A, et al.
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The role of HLA-B27 in spondyloarthritis.
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HLA-B27-RESTRICTED PEPTIDE PRESENTATION TO CYTOTOXIC T-CELLS IN REACTIVE ARTHRITIS
nork: Bowness, P, et al.
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Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.
nork: McHugh, K, et al.
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ERAP2 is associated with ankylosing spondylitis in HLA-B27-positive and HLA-B27-negative patients.
nork: Robinson, P, et al.
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HLA-B27
nork: Bowness, P
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HOMOCYSTEINE AND HLA B27-ASSOCIATED ARTHROPATHIES
nork: Gao, X, et al.
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HLA-B27 transgenic rodents express cell surface HLA-B27 heavy chain homodimers and multimers.
nork: Bowness, P, et al.
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Functional characterisation of HLA-B27 in autoimmunity
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Identification of HLA-B27-restricted peptides from the Chlamydia trachomatis proteome with possible relevance to HLA-B27-associated diseases.
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Autoimmunity-associated T cell receptors recognize HLA-B*27-bound peptides
nork: Yang, X, et al.
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Residue Cys-67 of HLA-B27 contributes to antigen presentation and T cell recognition of HLA-B27 restricted T cell epitopes.
nork: Appel, H, et al.
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IMMUNOGENIC HIV VARIANT PEPTIDES THAT BIND TO HLA-B8 BUT FAIL TO STIMULATE CYTOTOXIC T-LYMPHOCYTE RESPONSES
nork: Mcadam, S, et al.
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HLA-B27: natural function and pathogenic role in spondyloarthritis.
nork: McMichael, A, et al.
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A cluster of mutations in HLA-A2 alpha 2 helix abolishes peptide recognition by T cells.
nork: Moots, R, et al.
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Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility.
nork: Evans, D, et al.
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Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility
nork: Evans, D, et al.
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The KIRs of HLA-B27: the role of HLA-B27 KIR interactions in infection and spondyloarthritis
nork: Wong-Baeza, I, et al.
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Identification and characterisation of cell surface HLA-B27 homodimers
nork: Bird, L, et al.
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Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
nork: Walters, L, et al.
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The human major histocompatibility complex class Ib molecule HLA-E binds signal sequence-derived peptides with primary anchor residues at positions 2 and 9.
nork: Braud, V, et al.
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Importance of a conserved TCR J alpha-encoded tyrosine for T cell recognition of an HLA B27/peptide complex.
nork: Bowness, P, et al.
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Genotyping HLA-B27 in spondyloarthropathies.
nork: Brown, M, et al.
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HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors.
nork: Kollnberger, S, et al.
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Genetic modulation of antigen presentation by HLA-B27 molecules.
nork: Pazmany, L, et al.
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Analysis of mutant HLA-A2 molecules. Differential effects on peptide binding and CTL recognition.
nork: Tussey, L, et al.
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Evidence of widespread binding of HLA class I molecules to peptides.
nork: Frelinger, J, et al.
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