A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
about
Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinaseInteractions formed by individually expressed TAP1 and TAP2 polypeptide subunitsA novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38deltaThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaMHC class I antigen processing and presenting machinery: organization, function, and defects in tumor cellsWhat is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?The N-terminal region of tapasin is required to stabilize the MHC class I loading complexThe transporter associated with antigen processing: function and implications in human diseasesTapasin enhances MHC class I peptide presentation according to peptide half-lifeProgranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteinsThe oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I moleculesTapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells.A comparison of viral immune escape strategies targeting the MHC class I assembly pathway.Human pathogen subversion of antigen presentation.Antigen processing and presentation--towards the millennium.Class I MHC molecules: assembly and antigen presentation.The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system.TAP deficiency syndrome.Glucose-regulated protein 58 modulates β-catenin protein stability in a cervical adenocarcinoma cell lineTapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complexGlycoprotein folding in the endoplasmic reticulum.Intracellular surveillance: controlling the assembly of MHC class I-peptide complexes.The effect of intracellular trafficking of CD1d on the formation of TCR repertoire of NKT cells.Age-related proteomic changes in the subventricular zone and their association with neural stem/progenitor cell proliferation.Calreticulin is required for development of the cumulus oocyte complex and female fertilityAccessory molecules in the assembly of major histocompatibility complex class I/peptide complexes: how essential are they for CD8(+) T-cell immune responses?Ca2+-dependent redox modulation of SERCA 2b by ERp57.The majority of H2-M3 is retained intracellularly in a peptide-receptive state and traffics to the cell surface in the presence of N-formylated peptidesHow sugars convey information on protein conformation in the endoplasmic reticulumPeptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis.Physical and functional interaction of transmembrane thioredoxin-related protein with major histocompatibility complex class I heavy chain: redox-based protein quality control and its potential relevance to immune responsesDependence of elevated human leukocyte antigen class I molecule expression on increased heavy chain, light chain (beta 2-microglobulin), transporter associated with antigen processing, tapasin, and peptide.ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexinDisruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum.Divalent cations regulate the folding and activation status of integrins during their intracellular trafficking.Differential contribution of TAP and tapasin to HLA class I antigen expression.Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly.Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex.Proteasome-independent HLA-B27 ligands arise mainly from small basic proteins.Competition for access to the rat major histocompatibility complex class I peptide-loading complex reveals optimization of peptide cargo in the absence of transporter associated with antigen processing (TAP) association.
P2860
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P2860
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
description
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1998
@ast
im Juni 1998 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1998/06/04)
@sk
vědecký článek publikovaný v roce 1998
@cs
wetenschappelijk artikel (gepubliceerd op 1998/06/04)
@nl
наукова стаття, опублікована в червні 1998
@uk
مقالة علمية (نشرت في 4-6-1998)
@ar
name
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@ast
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@en
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@nl
type
label
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@ast
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@en
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@nl
prefLabel
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@ast
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@en
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@nl
P1433
P1476
A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
@en
P2093
N. A. Morrice
S. J. Powis
P304
P356
10.1016/S0960-9822(98)70279-9
P407
P577
1998-06-04T00:00:00Z