Dimers are forever. Expression and recognition of abnormal HLA-B27 in spondylo arthritis

Dimers are forever. Expression and recognition of abnormal HLA-B27 in spondylo arthritis

Bibliographic Details
Main Authors:	Bowness, P, Chan, A, Bobzin, C, Kollnberger, S, McMichael, A
Format:	Journal article
Published:	2005

Similar Items

HLA-B27 HEAVY CHAIN DIMER EXPRESSION IN SPONDYLOARTHRITIS
by: Rysnik, O, et al.
Published: (2012)

Cell-surface expression and immune receptor recognition of HLA-B27 homodimers.
by: Kollnberger, S, et al.
Published: (2002)

Functional characterisation of HLA-B27 in autoimmunity
by: Kollnberger, S, et al.
Published: (2001)

CELL SURFACE EXPRESSION OF HLA B27 HEAVY CHAINS AND SPECIFIC RECOGNITION BY IMMUNE RECEPTORS, POSSIBLE ROLE IN SPONDYLOARTHROPATHY
by: Kollnberger, S, et al.
Published: (2002)

HLA-B27 transgenic rodents express cell surface HLA-B27 heavy chain homodimers and multimers.
by: Bowness, P, et al.
Published: (2003)

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
by: Shaw, J, et al.
Published: (2013)

The KIRs of HLA-B27: the role of HLA-B27 KIR interactions in infection and spondyloarthritis
by: Wong-Baeza, I, et al.
Published: (2011)

Identification and characterisation of cell surface HLA-B27 homodimers
by: Bird, L, et al.
Published: (2002)

The role of B27 heavy chain dimer immune receptor interactions in spondyloarthritis.
by: Kollnberger, S, et al.
Published: (2009)

Residue Cys-67 of HLA-B27 contributes to antigen presentation and T cell recognition of HLA-B27 restricted T cell epitopes.
by: Appel, H, et al.
Published: (2004)

The role of HLA-B27 in spondyloarthritis.
by: Allen, R, et al.
Published: (1999)

Interaction of HLA-B27 homodimers with KIR3DL1 and KIR3DL2, unlike HLA-B27 heterotrimers, is independent of the sequence of bound peptide.
by: Kollnberger, S, et al.
Published: (2007)

Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27.
by: Bowness, P, et al.
Published: (1994)

IDENTIFICATION OF T-CELL RECEPTOR RECOGNITION RESIDUES FOR AN INFLUENZA-VIRUS NONAMER PEPTIDE EPITOPE PRESENTED BY HLA B27
by: Bowness, P, et al.
Published: (1995)

The solvent-inaccessible Cys67 residue of HLA-B27 contributes to T cell recognition of HLA-B27/peptide complexes.
by: Appel, H, et al.
Published: (2004)

HLA-B27-RESTRICTED PEPTIDE PRESENTATION TO CYTOTOXIC T-CELLS IN REACTIVE ARTHRITIS
by: Bowness, P, et al.
Published: (1995)

Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
by: Bird, L, et al.
Published: (2003)

HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors.
by: Kollnberger, S, et al.
Published: (2004)

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.
by: Cauli, A, et al.
Published: (2013)

EXPRESSION OF HLA-B27 HEAVY CHAIN FORMS IN ANKYLOSING SPONDYLITIS AND HLA-B27 POSITIVE CELL LINES
by: Rysnik, O, et al.
Published: (2012)

HLA-B27: natural function and pathogenic role in spondyloarthritis.
by: McMichael, A, et al.
Published: (2002)

The role of HLA-B27 interactions with natural killer receptors in the pathogenesis of spondyloarthritis
by: Kollnberger, S, et al.
Published: (2007)

HLA-B27
by: Bowness, P
Published: (2015)

HLA-B-27 heavy chain homodimer formation and natural killer cell family interaction - comparison of two HLA-B-27 subtypes in vitro
by: Giles, J, et al.
Published: (2008)

Direct visualisation of HLA-B27 forms in cell lines and Spondyloarthropathy tissues
by: Rysnik, O, et al.
Published: (2013)

Use of HLA-B27 tetramers to identify low-frequency antigen-specific T cells in Chlamydia-triggered reactive arthritis.
by: Appel, H, et al.
Published: (2004)

Use of HLA-B27 tetramers to identify low-frequency antigen-specific T cells in Chlamydia-triggered reactive arthritis.
by: Appel, H, et al.
Published: (2004)

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 Spondylitis.
by: Wong-Baeza, I, et al.
Published: (2013)

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 spondylitis.
by: Wong-Baeza, I, et al.
Published: (2013)

Importance of a conserved TCR J alpha-encoded tyrosine for T cell recognition of an HLA B27/peptide complex.
by: Bowness, P, et al.
Published: (1998)

THE ROLE OF HLA-B27 KIR3DL2 INTERACTIONS IN THE PATHOGENESIS OF SPONDYLOARTHRITIS
by: Kollnberger, S, et al.
Published: (2012)

Th17 cells expressing KIR3DL2+ and responsive to HLA-B27 homodimers are increased in ankylosing spondylitis.
by: Bowness, P, et al.
Published: (2011)

Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B*2705.
by: Stewart-Jones, G, et al.
Published: (2005)

HLA-B*2709 FORMS LESS CELL SURFACE B27 DIMER AND FREE HEAVY CHAIN LIGANDS FOR KIR3DL2 AND LILRB2 IMMUNORECEPTORS THAN ARTHRITIS-ASSOCIATED HLA-B*2705
by: Shaw, J, et al.
Published: (2012)

The pathogenesis of spondyloarthritides - HLA-B-27 homodimer expression on human monocyte/macrophage cell lines
by: McHugh, K, et al.
Published: (2008)

Molecular determinants for KIR3DL2 binding to HLA-B27 and other HLA-class I ligands
by: Hatano, H, et al.
Published: (2013)

Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.
by: McHugh, K, et al.
Published: (2014)

KIR3DL2 INTERACTION WITH HLA-B27 PROMOTES THE SURVIVAL OF TH17 CELLS IN ANKYLOSING SPONDYLITIS
by: Kollnberger, S, et al.
Published: (2010)

Identification of HLA-B27-restricted peptides from the Chlamydia trachomatis proteome with possible relevance to HLA-B27-associated diseases.
by: Kuon, W, et al.
Published: (2001)

TARGETING MONOCYTE-EXPRESSED HLA-B27 HOMODIMERS IN ANKYLOSING SPONDYLITIS
by: Bowness, P, et al.
Published: (2010)