Essential glycan-dependent interactions optimize MHC class I peptide loading - Wikidata - wikimedia - TriplyDB

Essential glycan-dependent interactions optimize MHC class I peptide loading

Essential glycan-dependent interactions optimize MHC class I peptide loading

http://www.wikidata.org/entity/Q34720708

about

Pathways of antigen processing.TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.Distinct assembly profiles of HLA-B molecules.Differential proteomics identifies PDIA3 as a novel chemoprevention target in human colon cancer cells.A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.The regulatory power of glycans and their binding partners in immunity Endoplasmic reticulum glycoprotein quality control regulates CD1d assembly and CD1d-mediated antigen presentation Running the gauntlet: from peptide generation to antigen presentation by MHC class I.Protein secretion and the endoplasmic reticulum.Calreticulin in the immune system: ins and outs The many functions of the endoplasmic reticulum chaperones and folding enzymes.Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.TAPBPR: a new player in the MHC class I presentation pathway.Recent advances in Major Histocompatibility Complex (MHC) class I antigen presentation: Plastic MHC molecules and TAPBPR-mediated quality control.In vitro reconstitution of the MHC class I peptide-loading complex.Direct evidence for conformational dynamics in major histocompatibility complex class I molecules.Editing peptide presentation to T cells.Structure of the human MHC-I peptide-loading complex.Single-particle electron microscopy structure of UDP-glucose:glycoprotein glucosyltransferase suggests a selectivity mechanism for misfolded proteins.Conservation of sequence motifs suggests that the nonclassical MHC class I lineages CD1/PROCR and UT were established before the emergence of tetrapod species.Mouse Norovirus infection reduces the surface expression of MHC class I proteins and inhibits CD8+ T cell recognition and activation The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling

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Essential glycan-dependent interactions optimize MHC class I peptide loading

http://www.wikidata.org/entity/Q34720708

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Essential glycan-dependent interactions optimize MHC class I peptide loading

@ast

Essential glycan-dependent interactions optimize MHC class I peptide loading

@en

Essential glycan-dependent interactions optimize MHC class I peptide loading

@nl

type

label

Essential glycan-dependent interactions optimize MHC class I peptide loading

@ast

Essential glycan-dependent interactions optimize MHC class I peptide loading

@en

Essential glycan-dependent interactions optimize MHC class I peptide loading

@nl

prefLabel

Essential glycan-dependent interactions optimize MHC class I peptide loading

@ast

Essential glycan-dependent interactions optimize MHC class I peptide loading

@en

Essential glycan-dependent interactions optimize MHC class I peptide loading

@nl

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PNAS.1102524108

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

P1476

Essential glycan-dependent interactions optimize MHC class I peptide loading

@en

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David R Peaper

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

Peter Cresswell

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

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Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin

Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing

Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status

A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes

Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer

Crystal structure of the bb' domains of the protein disulfide isomerase ERp57

Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57

Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP

Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit

A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum

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4950-4955

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scholarly article

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10.1073/PNAS.1102524108

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12

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108

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Pamela A. Wearsch

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2011-03-07T00:00:00Z

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50304322

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21383180

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3064348

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