about
The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradationHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationEndoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognitionX-Ray Structure of the Human Calreticulin Globular Domain Reveals a Peptide-Binding Area and Suggests a Multi-Molecular MechanismThe Peptide-Receptive Transition State of MHC Class I Molecules: Insight from Structure and Molecular DynamicsA structural and molecular dynamics approach to understanding the peptide-receptive transition state of MHC-I molecules.Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationViral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolutionA transcriptome-proteome integrated network identifies endoplasmic reticulum thiol oxidoreductase (ERp57) as a hub that mediates bone metastasisChronic beryllium disease: an updated model interaction between innate and acquired immunityMzb1 protein regulates calcium homeostasis, antibody secretion, and integrin activation in innate-like B cellsCalnexin deficiency leads to dysmyelination.Calreticulin: non-endoplasmic reticulum functions in physiology and disease.Compartmentalized MHC class I antigen processing enhances immunosurveillance by circumventing the law of mass action.Ovalbumin-derived precursor peptides are transferred sequentially from gp96 and calreticulin to MHC class I in the endoplasmic reticulum.Single residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation.A functional variant in ERAP1 predisposes to multiple sclerosis.Abacavir induces loading of novel self-peptides into HLA-B*57: 01: an autoimmune model for HLA-associated drug hypersensitivity.Mechanisms of function of tapasin, a critical major histocompatibility complex class I assembly factorFluorescence-based phenotypic selection allows forward genetic screens in haploid human cells.Archaeosome adjuvant overcomes tolerance to tumor-associated melanoma antigens inducing protective CD8 T cell responses.Essential glycan-dependent interactions optimize MHC class I peptide loadingEndoplasmic reticulum aminopeptidase associated with antigen processing defines the composition and structure of MHC class I peptide repertoire in normal and virus-infected cells.The carboxypeptidase ACE shapes the MHC class I peptide repertoireHLA-B*57 Micropolymorphism shapes HLA allele-specific epitope immunogenicity, selection pressure, and HIV immune controlThe disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosisThe mechanism of HLA-DM induced peptide exchange in the MHC class II antigen presentation pathwayEpstein-Barr viral BNLF2a protein hijacks the tail-anchored protein insertion machinery to block antigen processing by the transport complex TAP.Promiscuous binding of extracellular peptides to cell surface class I MHC proteinHost glycans and antigen presentationEndogenous viral antigen processing generates peptide-specific MHC class I cell-surface clusters.PPE38 of Mycobacterium marinum triggers the cross-talk of multiple pathways involved in the host response, as revealed by subcellular quantitative proteomics.Comparative expression profiling for human endoplasmic reticulum-resident aminopeptidases 1 and 2 in normal kidney versus distinct renal cell carcinoma subtypesIntracellular assembly and trafficking of MHC class I molecules.Detection of GAD65 autoreactive T-cells by HLA class I tetramers in type 1 diabetic patients.Disulfide formation in the ER and mitochondria: two solutions to a common process.Identifying Zn-bound histidine residues in metalloproteins using hydrogen-deuterium exchange mass spectrometry.Monitoring peptide processing for MHC class I molecules in the endoplasmic reticulum.Unique effect of Cu(II) in the metal-induced amyloid formation of β-2-microglobulinInsights into the processing of MHC class I ligands gained from the study of human tumor epitopes.
P2860
Q24294989-38AAF2FA-D771-4453-8E2D-BE21A58DCB4CQ24337606-617CB4CB-A7C0-4CC9-B69B-120CD13089B4Q26823628-38D05A79-2D97-4BFE-8058-9217386B4B61Q27667309-6DF10883-D83E-42C4-B0B1-BBE6AF31B802Q27670624-D2D7801A-7640-43B4-B1A1-CAC8FBC19DDAQ27691442-E86F41E1-76DB-48D7-A951-FD6EBB6D21A8Q27934273-FDD684FA-7B7D-422C-9D32-D7DBBCD3657AQ28083232-6F1050D2-A3D4-4E39-AC33-2CB174E3D08DQ28289791-7E2202A8-6C5C-4AC5-B7DD-EFB791C4FC19Q28386885-2543D871-9E4D-43D7-B6A3-280151507748Q28586494-8FCC0C79-FD31-47CB-BC8F-0BC9B2B28378Q30431936-60C057C2-9398-44B9-97F7-ED7C76809FE8Q33694634-8475F52E-1AF3-4DE2-A544-6486E2231730Q33859470-8F18724D-2A66-462A-BE57-0FEB1211DA8DQ33867072-9EEDF369-9BA6-439E-98DF-F48856CC2FD3Q33927361-CB652D69-3B21-4835-8FE8-197A2BC1333FQ34130800-8ED24E2E-FBD8-4526-A241-8263F1E170A2Q34140322-D794B2BF-4587-45D4-A3FE-07968B2EFA41Q34317136-F2B675E5-B0DD-4906-AB98-C143D0A20A58Q34321600-A1F032F0-C510-469A-890B-8187699D0B4FQ34557185-54739528-E78D-4812-9921-D3B1006CC75DQ34720708-C6898D4F-1C4C-48D2-94A6-CC366DB980B9Q34921343-5DA64E57-3CE2-4799-9F95-99747DD695F2Q35402189-7EA76F3D-7950-4115-B242-6E278F38856FQ35665876-3549F2A7-F22F-452C-8E48-21697B18B5A2Q35776997-847E3510-4DDE-4FCE-9B4F-21EB8F533770Q35785432-A4A61772-2269-4398-A949-FEF8CA033D66Q35842145-50B48B56-5BBD-4977-835E-45CD1775EBA0Q35849608-50572373-CE11-4C16-8429-B71DD9C93CE5Q36205138-59A6ABBD-6C26-4437-8BC8-6426E6857F31Q36279987-DEB6EF87-8096-4DE0-BC55-DCE2A0DC6499Q36822439-800E798F-FC33-482F-AAD2-CB6E552223FDQ36853385-CDE1D854-BBAD-4174-906B-DD2B18C9F82CQ37438723-F4D2E519-9634-4222-8B53-6B16B3A0541CQ37474056-17B9F8B5-A3D5-4C68-8E08-D3E277A18F68Q37508527-42D5D14B-56C9-40D1-8D2F-5977718C303EQ37550787-F606FA55-8F17-4D29-AB67-EF0992A13397Q37598087-BE451E03-DD92-4669-B706-E0F31AF13BECQ37701317-604FB031-EF2F-4B4B-BF7C-C81FF1F714AAQ37851050-2F2E0611-0675-4515-8EEA-E0DE3DAF828F
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 29 October 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The quality control of MHC class I peptide loading.
@en
The quality control of MHC class I peptide loading.
@nl
type
label
The quality control of MHC class I peptide loading.
@en
The quality control of MHC class I peptide loading.
@nl
prefLabel
The quality control of MHC class I peptide loading.
@en
The quality control of MHC class I peptide loading.
@nl
P2860
P1476
The quality control of MHC class I peptide loading.
@en
P2093
Peter Cresswell
P2860
P304
P356
10.1016/J.CEB.2008.09.005
P577
2008-10-29T00:00:00Z