about
Loss of viral fitness and cross-recognition by CD8+ T cells limit HCV escape from a protective HLA-B27–restricted human immune responseStructural Basis for T Cell Alloreactivity among Three HLA-B14 and HLA-B27 AntigensCitrullination-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 peptideSelf/nonself perception, reproduction and the extended MHCHuman Leukocyte Antigen (HLA) B27 Allotype-Specific Binding and Candidate Arthritogenic Peptides Revealed through Heuristic Clustering of Data-independent Acquisition Mass Spectrometry (DIA-MS) Data.Two HLA-B14 subtypes (B*1402 and B*1403) differentially associated with ankylosing spondylitis differ substantially in peptide specificity but have limited peptide and T-cell epitope sharing with HLA-B27.Identification of endogenously presented peptides from Chlamydia trachomatis with high homology to human proteins and to a natural self-ligand of HLA-B27.Two MHC class I molecules associated with elite control of immunodeficiency virus replication, Mamu-B*08 and HLA-B*2705, bind peptides with sequence similarity.Endoplasmic reticulum aminopeptidase-1 alleles associated with increased risk of ankylosing spondylitis reduce HLA-B27 mediated presentation of multiple antigens.Interaction pattern of Arg 62 in the A-pocket of differentially disease-associated HLA-B27 subtypes suggests distinct TCR binding modes.A common minimal motif for the ligands of HLA-B*27 class I molecules.Human leukocyte antigen B27 selects for rare escape mutations that significantly impair hepatitis C virus replication and require compensatory mutations.Natural HLA-B*2705 protein ligands with glutamine as anchor motif: implications for HLA-B27 association with spondyloarthropathy.Peptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis.Endogenous processing and presentation of T-cell epitopes from Chlamydia trachomatis with relevance in HLA-B27-associated reactive arthritis.Increased diversity of the HLA-B40 ligandome by the presentation of peptides phosphorylated at their main anchor residueCombined effects of ankylosing spondylitis-associated ERAP1 polymorphisms outside the catalytic and peptide-binding sites on the processing of natural HLA-B27 ligandsNovel HLA-B27-restricted epitopes from Chlamydia trachomatis generated upon endogenous processing of bacterial proteins suggest a role of molecular mimicry in reactive arthritis.The Human Leukocyte Antigen (HLA)-B27 Peptidome in Vivo, in Spondyloarthritis-susceptible HLA-B27 Transgenic Rats and the Effect of Erap1 Deletion.A Molecular Basis for the Presentation of Phosphorylated Peptides by HLA-B Antigens.A comprehensive analysis of peptides presented by HLA-A1.Revisiting the arthritogenic peptide theory: quantitative not qualitative changes in the peptide repertoire of HLA-B27 allotypes.Critical role of endoplasmic reticulum aminopeptidase 1 in determining the length and sequence of peptides bound and presented by HLA-B27.Functional interaction of the ankylosing spondylitis-associated endoplasmic reticulum aminopeptidase 1 polymorphism and HLA-B27 in vivo.The peptide-binding motif of HLA-DR8 shares important structural features with other type 1 diabetes-associated alleles.Unusual viral ligand with alternative interactions is presented by HLA-Cw4 in human respiratory syncytial virus-infected cells.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.Proteasome-independent HLA-B27 ligands arise mainly from small basic proteins.Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype.Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.High-sensitivity HLA class I peptidome analysis enables a precise definition of peptide motifs and the identification of peptides from cell lines and patients' sera.Human Leukocyte Antigen (HLA)-DRB1*15:01 and HLA-DRB5*01:01 Present Complementary Peptide Repertoires.Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide.Natural MHC class I polymorphism controls the pathway of peptide dissociation from HLA-B27 complexesX-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide.Purification, crystallization and preliminary X-ray diffraction analysis of the human major histocompatibility antigen HLA-B*2703 complexed with a viral peptide and with a self-peptide.Expression, 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.Co-evolution of a primordial peptide-presentation system and cellular immunity.
P2860
Q27487784-87C6DE1B-309F-4DA9-8A16-931A73FA0DCEQ27646543-20AB9FCE-E3C3-459C-88BD-D08A1D1BC619Q27651301-31FE55B3-E4C7-4BDD-96F8-67D8120DCE13Q27666781-0EAA27A0-6478-4801-B47F-5BC489667F1EQ28742269-CAEFD6C8-D67A-4673-9603-C78A7974BE24Q31050720-BB0C8B9D-F658-4AA0-8257-BC4F2FA94041Q33222105-73B113D3-0608-4A5B-8FB8-06C91E9553A4Q33302499-1D9B0147-E2D4-4A0A-AE8C-3ED3E54D5CB4Q33459720-22B1E335-B7B5-428A-8C91-7DA5E131E30FQ33924181-488CA4A7-7613-45B9-B6B3-AE87B14854F2Q34189720-27260434-895C-4169-9E96-3BB9E484C6A3Q35288793-6967EA4A-AB04-4400-AD3B-6064F052F1FDQ35446259-72788BD3-A90A-4D87-988D-E8C2634A9F3AQ36760435-81D605DB-50AA-4091-8860-0B3729C9EB38Q37167616-1D5392C6-73E1-433C-89FF-AB9F8596283CQ37294455-A6D660B9-3820-4A71-B754-405956064F21Q37563889-FB623727-35B6-464F-BDE9-C67403B5E9CFQ37583449-4F2399E1-F981-4969-9C48-F787F046D159Q37846210-52D9AEDC-4CD1-4DD1-A18D-CBB0B5C2AC59Q38380973-F10DE3EB-C1AE-4E53-9808-5237FE1B9885Q38727506-3670198E-07BD-44DD-9864-8D14E0534D1BQ38886434-5B426D08-01FF-478F-9273-3643B0AC2AD1Q38938313-815F675A-98DC-457C-9AFC-C09CDFEEC74CQ39026274-E1F1E3A1-27CF-4296-85C6-F33546967EBCQ39291937-DF3BC9E3-5CB1-4BEC-98DB-EA74E327E8AEQ39528303-9EC6B8CF-E452-47C8-869D-B9D2982575BAQ39639898-CADF53C4-6AF4-4226-B499-2A5C95F9B9D6Q39715318-D69AD95C-5D31-4FB9-AE1A-661F51E1E988Q40169540-372DA94F-F40D-4BE5-ABD8-BA8C5B91816AQ40362650-03AF3D8B-FD5C-4C44-9D9B-0F40615DE606Q41176761-8A0FF42C-0BA4-4F70-ABF7-C7C38ABAB993Q41410124-90E3368D-80E7-424A-BB5D-A846D14EE0B6Q41487863-5E6D2050-6DC3-4296-84ED-3B142946363BQ41542768-96A0A48E-C899-46E1-AE98-7B03B296E0A1Q41678328-0DFD263E-71F7-4085-8139-684A057B3668Q42001737-857EE9DF-60C6-40F9-B5F2-081FBA97699FQ42411694-BCA38BAF-35CC-4B51-A9C2-B37895642CB8Q42625853-34BCA0D6-A0AC-440C-BBF8-BE8179A5ED7AQ46573488-DDEBD85C-E28A-4DC0-A79F-A546A0E13311Q47222154-80C9A2F9-48CC-46A8-ACA5-6514F28409B7
P2860
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
HLA-B27: a registry of constitutive peptide ligands.
@en
type
label
HLA-B27: a registry of constitutive peptide ligands.
@en
prefLabel
HLA-B27: a registry of constitutive peptide ligands.
@en
P2860
P50
P1433
P1476
HLA-B27: a registry of constitutive peptide ligands
@en
P2093
Lopez de Castro JA
P2860
P304
P356
10.1111/J.0001-2815.2004.00220.X
P577
2004-05-01T00:00:00Z