A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal
about
MiR-221 influences effector functions and actin cytoskeleton in mast cellsSEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesMalectin forms a complex with ribophorin I for enhanced association with misfolded glycoproteinsMannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsA luminal flavoprotein in endoplasmic reticulum-associated degradationHuman OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansGRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumRoad to ruin: targeting proteins for degradation in the endoplasmic reticulumYos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Five Questions (with their Answers) on ER-Associated DegradationCyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradationDerlin-2-deficient mice reveal an essential role for protein dislocation in chondrocytesA Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog.Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates.Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER.Identification of cellular proteins interacting with equine infectious anemia virus S2 protein.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradationRole of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of α1-antitrypsinGlucosidase II and MRH-domain containing proteins in the secretory pathway.Differential dependence on N-glycosylation of anthrax toxin receptors CMG2 and TEM8A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.OS9 Protein Interacts with Na-K-2Cl Co-transporter (NKCC2) and Targets Its Immature Form for the Endoplasmic Reticulum-associated Degradation Pathway.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.The mammalian endoplasmic reticulum-associated degradation systemStrategies for carbohydrate recognition by the mannose 6-phosphate receptors.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesGRP94 in ER quality control and stress responsesSorting things out through endoplasmic reticulum quality control.ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum.Endoplasmic reticulum-associated degradation of glycoproteins in plantsSpecificity and regulation of the endoplasmic reticulum-associated degradation machinery.The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle FunctionERAD and how viruses exploit it.Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant.Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Glycosylation-directed quality control of protein folding.Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control.
P2860
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P2860
A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@ast
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en-gb
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@nl
type
label
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@ast
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en-gb
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@nl
prefLabel
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@ast
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en-gb
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@nl
P2860
P50
P921
P356
P1476
A dual task for the Xbp1-respo ...... s and enhancing their disposal
@en
P2093
Riccardo Bernasconi
P2860
P304
P356
10.1074/JBC.M802272200
P407
P577
2008-06-13T00:00:00Z