Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation
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In vitro mannose trimming property of human ER α-1,2 mannosidase IProtein folding and quality control in the ERStructural Basis of the Anti-HIV Activity of the Cyanobacterial Oscillatoria Agardhii AgglutininStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexStructure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic ReticulumA Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumYos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation.Misfolded proteins induce aggregation of the lectin Yos9.Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.Role of malectin in Glc(2)Man(9)GlcNAc(2)-dependent quality control of α1-antitrypsinIdentification of a fourth mannose 6-phosphate binding site in the cation-independent mannose 6-phosphate receptor.Glucosidase II and MRH-domain containing proteins in the secretory pathway.A Novel Role of OS-9 in the Maintenance of Intestinal Barrier Function from Hypoxia-induced Injury via p38-dependent Pathway.The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in the endoplasmic reticulum-associated degradation of misfolded receptor-like kinases.Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrateGolgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP.The mammalian endoplasmic reticulum-associated degradation systemLipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.Intracellular lectins are involved in quality control of glycoproteins.Convergent and divergent mechanisms of sugar recognition across kingdoms.Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Glycosylation-directed quality control of protein folding.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e.Defining the Interaction of Human Soluble Lectin ZG16p and Mycobacterial Phosphatidylinositol Mannosides.Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins.Characterization of the Grp94/OS-9 chaperone-lectin complex.Role of the unfolded protein response in determining the fate of tumor cells and the promise of multi-targeted therapies.The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation.
P2860
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P2860
Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural basis for oligosacc ...... 9 in ER-associated degradation
@ast
Structural basis for oligosacc ...... 9 in ER-associated degradation
@en
Structural basis for oligosacc ...... 9 in ER-associated degradation
@nl
type
label
Structural basis for oligosacc ...... 9 in ER-associated degradation
@ast
Structural basis for oligosacc ...... 9 in ER-associated degradation
@en
Structural basis for oligosacc ...... 9 in ER-associated degradation
@nl
prefLabel
Structural basis for oligosacc ...... 9 in ER-associated degradation
@ast
Structural basis for oligosacc ...... 9 in ER-associated degradation
@en
Structural basis for oligosacc ...... 9 in ER-associated degradation
@nl
P2093
P1433
P1476
Structural basis for oligosacc ...... 9 in ER-associated degradation
@en
P2093
Kazuo Yamamoto
Shinya Hanashima
Yoshiki Yamaguchi
P304
P356
10.1016/J.MOLCEL.2010.11.017
P50
P577
2010-12-01T00:00:00Z