A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.
about
A membrane protein required for dislocation of misfolded proteins from the ERA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsA ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ERThe retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulumInhibition of p97-dependent protein degradation by Eeyarestatin IN-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity.Varicella-Zoster Virus Infectious Cycle: ER Stress, Autophagic Flux, and Amphisome-Mediated TraffickingSignal peptide peptidase is required for dislocation from the endoplasmic reticulumThe PUB domain functions as a p97 binding module in human peptide N-glycanaseERAD: the long road to destructionThe AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptorGlycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substratesEndo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cellsTMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I.The cytoplasmic peptide:N-glycanase (NGLY1) - Structure, expression and cellular functionsN-glycosylation enhances presentation of a MHC class I-restricted epitope from tyrosinaseMan2C1, an alpha-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol.N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cellsRequirements for the selective degradation of endoplasmic reticulum-resident major histocompatibility complex class I proteins by the viral immune evasion molecule mK3.A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Cleavage by signal peptide peptidase is required for the degradation of selected tail-anchored proteins.Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation.Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasomeThe p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.Insight into the mechanism of human herpesvirus 7 U21-mediated diversion of class I MHC molecules to lysosomes.The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Lipid droplet formation is dispensable for endoplasmic reticulum-associated degradation.Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Cyclophilin C Participates in the US2-Mediated Degradation of Major Histocompatibility Complex Class I Molecules.Search and destroy: ER quality control and ER-associated protein degradation.The Png1-Rad23 complex regulates glycoprotein turnover.SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Versatility of the endoplasmic reticulum protein folding factory.Viral modulation of antigen presentation: manipulation of cellular targets in the ER and beyond.gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulumHuman cytomegalovirus gH stability and trafficking are regulated by ER-associated degradation and transmembrane architecture.Structure and function of the AAA+ ATPase p97/Cdc48p.F-box proteins that contain sugar-binding domains.
P2860
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P2860
A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A glycosylated type I membrane ...... de: N-glycanase is compromised
@nl
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@ast
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en-gb
type
label
A glycosylated type I membrane ...... de: N-glycanase is compromised
@nl
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@ast
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en-gb
prefLabel
A glycosylated type I membrane ...... de: N-glycanase is compromised
@nl
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@ast
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en-gb
P2093
P2860
P3181
P356
P1433
P1476
A glycosylated type I membrane ...... e: N-glycanase is compromised.
@en
P2093
Christian Hirsch
Daniël Blom
Hidde L Ploegh
Patrick Stern
P2860
P304
P3181
P356
10.1038/SJ.EMBOJ.7600090
P407
P577
2004-01-29T00:00:00Z