Residue Cys-67 of HLA-B27 contributes to antigen presentation and T cell recognition of HLA-B27 restricted T cell epitopes.

Residue Cys-67 of HLA-B27 contributes to antigen presentation and T cell recognition of HLA-B27 restricted T cell epitopes.

Manylion Llyfryddiaeth
Prif Awduron:	Appel, H, Kuhne, M, Kuon, W, Kuhlmann, S, Kollnberger, S, Weiss, E, Bowness, P, Sieper, J
Fformat:	Conference item
Cyhoeddwyd:	2004

Eitemau Tebyg

The solvent-inaccessible Cys67 residue of HLA-B27 contributes to T cell recognition of HLA-B27/peptide complexes.
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Cyhoeddwyd: (2004)

Use of HLA-B27 tetramers to identify low-frequency antigen-specific T cells in Chlamydia-triggered reactive arthritis.
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Use of HLA-B27 tetramers to identify low-frequency antigen-specific T cells in Chlamydia-triggered reactive arthritis.
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Cyhoeddwyd: (2004)

Identification of HLA-B27-restricted peptides from the Chlamydia trachomatis proteome with possible relevance to HLA-B27-associated diseases.
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Cyhoeddwyd: (2001)

The KIRs of HLA-B27: the role of HLA-B27 KIR interactions in infection and spondyloarthritis
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EXPRESSION OF HLA-B27 HEAVY CHAIN FORMS IN ANKYLOSING SPONDYLITIS AND HLA-B27 POSITIVE CELL LINES
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Cyhoeddwyd: (2012)

HLA-B27 transgenic rodents express cell surface HLA-B27 heavy chain homodimers and multimers.
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HLA B27 can form heavy chain homodimers in vivo and in vivo, possible role of cys 67.
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HLA-B27
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Cyhoeddwyd: (2015)

Factors determining the cell surface expression of a novel HLA-B27 epitope
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Identification and characterisation of cell surface HLA-B27 homodimers
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HLA-B-27 heavy chain homodimer formation and natural killer cell family interaction - comparison of two HLA-B-27 subtypes in vitro
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Functional characterisation of HLA-B27 in autoimmunity
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Direct visualisation of HLA-B27 forms in cell lines and Spondyloarthropathy tissues
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HLA-B27-Homodimer-Specific Antibody Modulates the Expansion of Pro-Inflammatory T-Cells in HLA-B27 Transgenic Rats.
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Cell-surface expression and immune receptor recognition of HLA-B27 homodimers.
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HLA-B27 HEAVY CHAIN DIMER EXPRESSION IN SPONDYLOARTHRITIS
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Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.
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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.
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Dimers are forever. Expression and recognition of abnormal HLA-B27 in spondylo arthritis
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Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
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THE ARTHRITIS-ASSOCIATED HLA-B(star)27:05 FORMS MORE CELL SURFACE B27 DIMER AND FREE HEAVY CHAIN LIGANDS FOR KIR3DL2 AND LILRB2 IMMUNORECEPTORS THAN HLA(star)B27:09
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The role of HLA-B27 interactions with natural killer receptors in the pathogenesis of spondyloarthritis
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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.
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HLA-B27 homodimers differ in their interactions with LILRB1, LILRB2, KIR3DL1 and KIR3DL2 compared to HLA-B27 heterotrimers
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