Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process.
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Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulumA luminal flavoprotein in endoplasmic reticulum-associated degradationCotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoformsA single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseasesMammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylationCrucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function.Selective protein degradation in the yeast exocytic pathway.Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulumEndoplasmic reticulum: a dynamic patchwork of specialized subregionsSEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartmentAssembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.O-glycosylation of intact and truncated ribophorins in brefeldin A-treated cells: newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases.The alpha subunit of the Saccharomyces cerevisiae oligosaccharyltransferase complex is essential for vegetative growth of yeast and is homologous to mammalian ribophorin I.Degradation of aggrecan precursors within a specialized subcompartment of the chicken chondrocyte endoplasmic reticulum.How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.Non-lysosomal degradation of misfolded human lysozymes with and without an asparagine-linked glycosylation site.Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response.Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control.Posttranscriptional Regulation of Glycoprotein Quality Control in the Endoplasmic Reticulum Is Controlled by the E2 Ub-Conjugating Enzyme UBC6e.N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation.Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation.Disruption of disulfide bonds is responsible for impaired secretion in human complement factor H deficiency.Selective fast degradation of cytochrome P-450 2E1 in serum-deprived hepatoma cells by a mechanism sensitive to inhibitors of vesicular transport.Degradation of distinct assembly forms of immunoglobulin M occurs in multiple sites in permeabilized B cells.The endoplasmic reticulum degradation pathway for mutant secretory proteins alpha1-antitrypsin Z and S is distinct from that for an unassembled membrane protein.A neuroendocrine-specific protein localized to the endoplasmic reticulum by distal degradation.A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum.Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.A signal for endoplasmic reticulum retention located at the carboxyl terminus of the plasma membrane Ca(2+)-ATPase isoform 4CI.Protein interaction screening for the ankyrin repeats and suppressor of cytokine signaling (SOCS) box (ASB) family identify Asb11 as a novel endoplasmic reticulum resident ubiquitin ligase.Degradation of apolipoprotein B in cultured rat hepatocytes occurs in a post-endoplasmic reticulum compartment.An uncleaved glycosylphosphatidylinositol signal mediates Ca(2+)-sensitive protein degradationProteolytic cleavage of haptoglobin occurs in a subcompartment of the endoplasmic reticulum: evidence from membrane fusion in vitro.Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2alpha kinase.Quality control of glycosylphosphatidylinositol anchor attachment in mammalian cells: a biochemical study.Activation of the Ras-cAMP signal transduction pathway inhibits the proteasome-independent degradation of misfolded protein aggregates in the endoplasmic reticulum lumen.
P2860
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P2860
Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Carboxy terminally truncated f ...... y a calcium-dependent process.
@ast
Carboxy terminally truncated f ...... y a calcium-dependent process.
@en
type
label
Carboxy terminally truncated f ...... y a calcium-dependent process.
@ast
Carboxy terminally truncated f ...... y a calcium-dependent process.
@en
prefLabel
Carboxy terminally truncated f ...... y a calcium-dependent process.
@ast
Carboxy terminally truncated f ...... y a calcium-dependent process.
@en
P2093
P2860
P356
P1476
Carboxy terminally truncated f ...... y a calcium-dependent process.
@en
P2093
D D Sabatini
G Kreibich
N E Ivessa
P2860
P356
10.1083/JCB.116.1.57
P407
P577
1992-01-01T00:00:00Z