Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I.
about
Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradationA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsA luminal flavoprotein in endoplasmic reticulum-associated degradationHuman EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteinsThe otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ERThe retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulumDefining the glycan destruction signal for endoplasmic reticulum-associated degradationHtm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulumEDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsinEDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimmingQuantitative analysis of a ubiquitin-dependent substrate using capillary electrophoresis with dual laser-induced fluorescence.Role for a Zinc Finger Protein (Zfp111) in Transformation of 208F Rat Fibroblasts by Jaagsiekte Sheep Retrovirus Envelope Protein.SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond.Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.N-glycan structure dictates extension of protein folding or onset of disposal.SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteinsSorting things out through endoplasmic reticulum quality control.Protein N-glycosylation, protein folding, and protein quality control.Specificity and regulation of the endoplasmic reticulum-associated degradation machinery.Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Two distinct pathways for cyclooxygenase-2 protein degradation.The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system.
P2860
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P2860
Processing of N-linked glycans during endoplasmic-reticulum-associated degradation of a short-lived variant of ribophorin I.
description
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name
Processing of N-linked glycans ...... lived variant of ribophorin I.
@en
Processing of N-linked glycans ...... lived variant of ribophorin I.
@nl
type
label
Processing of N-linked glycans ...... lived variant of ribophorin I.
@en
Processing of N-linked glycans ...... lived variant of ribophorin I.
@nl
prefLabel
Processing of N-linked glycans ...... lived variant of ribophorin I.
@en
Processing of N-linked glycans ...... lived variant of ribophorin I.
@nl
P2093
P2860
P356
P1433
P1476
Processing of N-linked glycans ...... -lived variant of ribophorin I
@en
P2093
Andrea Caprini
Eva Schwaiger
Jean-Pierre Frénoy
Myriam Ermonval
N Erwin Ivessa
Odile Kellermann
P2860
P304
P356
10.1042/BJ20030887
P407
P577
2003-12-01T00:00:00Z