A subset of HLA-B27 molecules contains peptides much longer than nonamers. - Wikidata - wikimedia - TriplyDB

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

http://www.wikidata.org/entity/Q35056650

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Sampling of major histocompatibility complex class I-associated peptidome suggests relatively looser global association of HLA-B*5101 with peptides Peptide binding characteristics of the non-classical class Ib MHC molecule HLA-E assessed by a recombinant random peptide approach Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells HLA-B27 subtypes differentially associated with disease exhibit subtle structural alterations From HLA-B27 to spondyloarthritis: a journey through the ER.Immunoproteomics: Mass spectrometry-based methods to study the targets of the immune response Antigen processing for MHC class I restricted presentation of exogenous influenza A virus nucleoprotein by B-lymphoblastoid cells Enhanced detection of human immunodeficiency virus type 1 (HIV-1) Nef-specific T cells recognizing multiple variants in early HIV-1 infection.Minimal alterations in the HLA-B27-bound peptide repertoire induced upon infection of lymphoid cells with Salmonella typhimurium.Peptide length preferences for rat and mouse MHC class I molecules using random peptide libraries.Tapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells.ERAP1 reduces accumulation of aberrant and disulfide-linked forms of HLA-B27 on the cell surface Cytotoxic T-cell-mediated response against Yersinia pseudotuberculosis in HLA-B27 transgenic rat.Identification of peptides from foot-and-mouth disease virus structural proteins bound by class I swine leukocyte antigen (SLA) alleles, SLA-1*0401 and SLA-2*0401.Rapid antigen processing and presentation of a protective and immunodominant HLA-B*27-restricted hepatitis C virus-specific CD8+ T-cell epitope.Kinetics of antigen expression and epitope presentation during virus infection.HLA-B27: natural function and pathogenic role in spondyloarthritis.Influence of dominant HIV-1 epitopes on HLA-A3/peptide complex formation.Assembly and peptide binding of major histocompatibility complex class II heterodimers in an in vitro translation system.Antigen processing and remodeling of the endosomal pathway: requirements for antigen cross-presentation.Use of proteomics to define targets of T-cell immunity.Trimming of antigenic peptides in an early secretory compartment.The peptide-binding motif for the human transporter associated with antigen processing Cytotoxic T lymphocyte epitopes of HIV-1 Nef: Generation of multiple definitive major histocompatibility complex class I ligands by proteasomes.Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing.HLA-B27 heavy chains contribute to spontaneous inflammatory disease in B27/human beta2-microglobulin (beta2m) double transgenic mice with disrupted mouse beta2m.A patient-derived cytotoxic T-lymphocyte clone and two peptide-dependent monoclonal antibodies recognize HLA-B27-peptide complexes with low stringency for peptide sequences.The Human Leukocyte Antigen (HLA)-B27 Peptidome in Vivo, in Spondyloarthritis-susceptible HLA-B27 Transgenic Rats and the Effect of Erap1 Deletion.Identification of pancreatic cancer-associated tumor antigen from HSP-enriched tumor lysate-pulsed human dendritic cells.HLA-B27 Anterior Uveitis: Immunology and Immunopathology.Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation.Alteration of HLA-B27 peptide presentation after infection of transfected murine L cells by Shigella flexneri.T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide.High resolution structures of highly bulged viral epitopes bound to major histocompatibility complex class I. Implications for T-cell receptor engagement and T-cell immunodominance.HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum.Presentation without proteolytic cleavage of endogenous precursors in the MHC class I antigen processing pathway.Cells expressing a major histocompatibility complex class I molecule with a single covalently bound peptide are highly immunogenic.Hypothesis: MHC class I, rather than just a flagpole for CD8+ T cells is also a protease in its own right.Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling.Characterization of a proteasome and TAP-independent presentation of intracellular epitopes by HLA-B27 molecules

P2860

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P2860

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

http://www.wikidata.org/entity/Q35056650

description

1994 nî lūn-bûn

@nan

1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

name

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@ast

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

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type

label

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@ast

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@en

prefLabel

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@ast

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@en

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

A subset of HLA-B27 molecules contains peptides much longer than nonamers.

@en

P2093

A Rehm

http://www.w3.org/2001/XMLSchema#string

A Ziegler

http://www.w3.org/2001/XMLSchema#string

B Uchanska-Ziegler

http://www.w3.org/2001/XMLSchema#string

F G UytdeHaag

http://www.w3.org/2001/XMLSchema#string

H Ploegh

http://www.w3.org/2001/XMLSchema#string

M J Kenter

http://www.w3.org/2001/XMLSchema#string

R G Urban

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R M Chicz

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W S Lane

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P2860

Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex

Specificity pockets for the side chains of peptide antigens in HLA-Aw68

Regional mapping of the gene for autosomal dominant spinocerebellar ataxia (SCA1) by localizing the closely linked D6S89 locus to 6p24.2----p23.05

Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter

The construction of cosmid libraries which can be used to transform eukaryotic cells

Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner

Multiple sequence analysis: pool sequencing of synthetic and natural peptide libraries.

Guilt by association: HLA-B27 and ankylosing spondylitis.

Peptide binding to HLA-A2 and HLA-B27 isolated from Escherichia coli. Reconstitution of HLA-A2 and HLA-B27 heavy chain/beta 2-microglobulin complexes requires specific peptides.

Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size.

P304

1534-1538

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scholarly article

P356

10.1073/PNAS.91.4.1534

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P407

P433

4

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P478

91

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P50

Jack L. Strominger

P577

1994-02-01T00:00:00Z

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15091693

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8108441

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P932

43194

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