Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. - Wikidata - awgldk - TriplyDB

Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.

Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.

http://www.wikidata.org/entity/Q37465835

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A peptide filtering relation quantifies MHC class I peptide optimization Calreticulin is the dominant pro-phagocytic signal on multiple human cancers and is counterbalanced by CD47 Calreticulin controls the rate of assembly of CD1d molecules in the endoplasmic reticulum Structural Mechanism of ER Retrieval of MHC Class I by Cowpox Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathway Bioengineering a unique deimmunized bispecific targeted toxin that simultaneously recognizes human CD22 and CD19 receptors in a mouse model of B-cell metastases.The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules Calreticulin binds to gentamicin and reduces drug-induced ototoxicity.Productive association between MHC class I and tapasin requires the tapasin transmembrane/cytosolic region and the tapasin C-terminal Ig-like domain.Ikaros deficiency in host hematopoietic cells separates GVL from GVHD after experimental allogeneic hematopoietic cell transplantation Adopting the rapamycin trapping assay to track the trafficking of murine MHC class I alleles, H-2K(b)Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Proteomic screening identifies calreticulin as a miR-27a direct target repressing MHC class I cell surface exposure in colorectal cancer.Mutant calreticulin-expressing cells induce monocyte hyperreactivity through a paracrine mechanism Glycoprotein folding and quality-control mechanisms in protein-folding diseases Generation of MHC class I ligands in the secretory and vesicular pathways.Running the gauntlet: from peptide generation to antigen presentation by MHC class I.Calreticulin in the immune system: ins and outs Release from endoplasmic reticulum matrix proteins controls cell surface transport of MHC class I molecules.F pocket flexibility influences the tapasin dependence of two differentially disease-associated MHC Class I proteins.Three tapasin docking sites in TAP cooperate to facilitate transporter stabilization and heterodimerization.Mutational analysis reveals a complex interplay of peptide binding and multiple biological features of HLA-B27.ERAAP Shapes the Peptidome Associated with Classical and Nonclassical MHC Class I Molecules.Human cytomegalovirus disrupts the major histocompatibility complex class I peptide-loading complex and inhibits tapasin gene transcription.In the beginning and at the end: calreticulin.Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER-Golgi intermediate compartment.Loading of antigenic peptides on to class I MHC Dissociation of the Antigenic peptide:MHC:B2M peptide loading complex

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Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules.

http://www.wikidata.org/entity/Q37465835

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 22 October 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@en

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@nl

type

label

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@en

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@nl

prefLabel

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@en

Calreticulin-dependent recycli ...... ding of MHC class I molecules.

@nl

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The EMBO Journal

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Calreticulin-dependent recycli ...... ding of MHC class I molecules.

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Anthony Williams

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

Christopher Howe

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

Clemens Schneeweiss

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

Esther Ghanem

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

Gytis Jankevicius

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

Malgorzata Garstka

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

Mohammed Al-Balushi

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

Nasia Kontouli

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

Sebastian Springer

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

Susanne Fritzsche

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

P2860

Calreticulin Is a receptor for nuclear export.

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

Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum

Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C

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

Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP

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

Expression and localization of two low molecular weight GTP-binding proteins, Rab8 and Rab10, by epitope tag

COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.

The mechanism of action of tapasin in the peptide exchange on MHC class I molecules determined from kinetics simulation studies

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3730-3744

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scholarly article

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10.1038/EMBOJ.2009.296

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23

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28

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Antony N Antoniou

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2009-10-22T00:00:00Z

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38030837

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19851281

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2790484

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