The Structure of calnexin, an ER chaperone involved in quality control of protein folding
about
Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperonesMajor histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly statusTROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.Protein tandem repeats - the more perfect, the less structuredSugar activation and glycosylation in PlasmodiumGlycoprotein Quality Control and Endoplasmic Reticulum StressN-linked sugar-regulated protein folding and quality control in the ERCrystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulumCrystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain familyThe crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftMalectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-GlycosylationInsights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase HeterodimerAnalysis of the specific interactions between the lectin domain of malectin and diglucosidesStructural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domainStructural Basis of Carbohydrate Recognition by CalreticulinStructural and Functional Relationships between the Lectin and Arm Domains of CalreticulinX-Ray Structure of the Human Calreticulin Globular Domain Reveals a Peptide-Binding Area and Suggests a Multi-Molecular MechanismStructure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic ReticulumN-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding CycleLocalization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulinERp57 is a multifunctional thiol-disulfide oxidoreductaseThe evolutionary history of calreticulin and calnexin genes in green plantsTitanium Dioxide Nanoparticles Induce Endoplasmic Reticulum Stress-Mediated Autophagic Cell Death via Mitochondria-Associated Endoplasmic Reticulum Membrane Disruption in Normal Lung CellsEnhanced clathrin-dependent endocytosis in the absence of calnexinThe EF-hand Ca2+-binding protein p22 plays a role in microtubule and endoplasmic reticulum organization and dynamics with distinct Ca2+-binding requirementsAssociation of calnexin with mutant peripheral myelin protein-22 ex vivo: a basis for "gain-of-function" ER diseasesCa2+-dependent nuclear export mediated by calreticulin.Topological analysis of Hedgehog acyltransferase, a multipalmitoylated transmembrane proteinStructures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties.Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol.Molecular Chaperone Calnexin Regulates the Function of Drosophila Sodium Channel Paralytic.Dimerization and oligomerization of the chaperone calreticulin.Protein kinase C (PKC)-induced phosphorylation of ROMK1 is essential for the surface expression of ROMK1 channelsMonitoring chaperone engagement of substrates in the endoplasmic reticulum of live cellsCalnexin Delta 185-520 partially reverses the misprocessing of the Delta F508 cystic fibrosis transmembrane conductance regulator.Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library.Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosisDirect observation of molecular arrays in the organized smooth endoplasmic reticulum.Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathwayThe structure of calreticulin C-terminal domain is modulated by physiological variations of calcium concentration.
P2860
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P2860
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@ast
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@en
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@nl
type
label
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@ast
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@en
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@nl
prefLabel
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@ast
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@en
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@nl
P2093
P921
P1433
P1476
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
@en
P2093
P304
P356
10.1016/S1097-2765(01)00318-5
P577
2001-09-01T00:00:00Z