Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome.
about
Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesisCloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesisHuman OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansHuman EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteinsHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPA dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposalEDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complexA novel ER alpha-mannosidase-like protein accelerates ER-associated degradationPost-translational modification of the myxoma-virus anti-inflammatory serpin SERP-1 by a virally encoded sialyltransferaseEDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sitesGenome wide analysis of common and specific stress responses in adult drosophila melanogasterThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyCrystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality controlStructural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidasesMnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the proteinEDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsinA novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradationFunctional and protein chemical characterization of the N-terminal domain of the rat corticotropin-releasing factor receptor 1The molecular basis of oculocutaneous albinism type 1 (OCA1): sorting failure and degradation of mutant tyrosinases results in a lack of pigmentationCyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradationEDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycansEDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimmingLectins and traffic in the secretory pathwayUnderstanding protein structure-function relationships in Family 47 alpha-1,2-mannosidases through computational docking of ligands.Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation.Functional contributions of noncysteine residues within the cystine knots of human chorionic gonadotropin subunits.Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules.Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER.Production of infectious hepatitis C virus by using RNA polymerase I-mediated transcription.Organizational diversity among distinct glycoprotein endoplasmic reticulum-associated degradation programsRole of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradationTRAM1 is involved in disposal of ER membrane degradation substrates.The hepatitis C virus E1 glycoprotein undergoes productive folding but accelerated degradation when expressed as an individual subunit in CHO cells.Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation.Oligosaccharide-based information in endoplasmic reticulum quality control and other biological systems.Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathwayGolgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control.
P2860
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P2860
Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Oligosaccharide modification i ...... degradation by the proteasome.
@ast
Oligosaccharide modification i ...... degradation by the proteasome.
@en
type
label
Oligosaccharide modification i ...... degradation by the proteasome.
@ast
Oligosaccharide modification i ...... degradation by the proteasome.
@en
prefLabel
Oligosaccharide modification i ...... degradation by the proteasome.
@ast
Oligosaccharide modification i ...... degradation by the proteasome.
@en
P2093
P2860
P356
P1476
Oligosaccharide modification i ...... degradation by the proteasome.
@en
P2093
P2860
P304
P356
10.1074/JBC.274.9.5861
P407
P577
1999-02-01T00:00:00Z