Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
about
The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin bindingTapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathwayThe N-terminal amphipathic alpha-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretionERp57 is essential for efficient folding of glycoproteins sharing common structural domainsDisulfide bond formation in the mammalian endoplasmic reticulumWhat is the role of alternate splicing in antigen presentation by major histocompatibility complex class I molecules?Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase HeterodimerViral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolutionThe binding of TAPBPR and Tapasin to MHC class I is mutually exclusive.Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP.Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathwayTAPBPR 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.Profiling thiol metabolites and quantification of cellular glutathione using FT-ICR-MS spectrometry.Degradable conjugates from oxanorbornadiene reagentsMechanisms of function of tapasin, a critical major histocompatibility complex class I assembly factorIdentification and characterisation of the RalA-ERp57 interaction: evidence for GDI activity of ERp57.Essential glycan-dependent interactions optimize MHC class I peptide loadingProductive association between MHC class I and tapasin requires the tapasin transmembrane/cytosolic region and the tapasin C-terminal Ig-like domain.Direct peptide-regulatable interactions between MHC class I molecules and tapasin.Potential biomarkers associated with diabetic glomerulopathy through proteomics.The mechanism of HLA-DM induced peptide exchange in the MHC class II antigen presentation pathwayCylindrospermopsin effects on protein profile of HepG2 cells.Dynamics of major histocompatibility complex class I association with the human peptide-loading complex.Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentationImpaired tumor antigen processing by immunoproteasome-expressing CD40-activated B cells and dendritic cellsThyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading.The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules.How sugars convey information on protein conformation in the endoplasmic reticulumERAAP and tapasin independently edit the amino and carboxyl termini of MHC class I peptides.Pathogen evasion strategies for the major histocompatibility complex class I assembly pathway.ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activityViral proteins interfering with antigen presentation target the major histocompatibility complex class I peptide-loading complex.Peptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis.Molecular chaperones and photoreceptor function.Redox-regulated export of the major histocompatibility complex class I-peptide complexes from the endoplasmic reticulumThe quality control of MHC class I peptide loading.Intracellular assembly and trafficking of MHC class I molecules.
P2860
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P2860
Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@ast
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@en
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@nl
type
label
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@ast
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@en
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@nl
prefLabel
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@ast
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@en
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@nl
P2860
P356
P1433
P1476
Tapasin and ERp57 form a stabl ...... lass I peptide-loading complex
@en
P2093
David R Peaper
Peter Cresswell
P2860
P304
P356
10.1038/SJ.EMBOJ.7600814
P407
P577
2005-09-29T00:00:00Z