Intracellular degradation of unassembled asialoglycoprotein receptor subunits: a pre-Golgi, nonlysosomal endoproteolytic cleavage.
about
Calumenin, a Ca2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEFAssembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acidsCab45, a novel (Ca2+)-binding protein localized to the Golgi lumenType XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovaryInhibition by acidic phospholipids of protein degradation by ER-60 protease, a novel cysteine protease, of endoplasmic reticulumUltrastructure of inclusion bodies in annulus cells in the degenerating human intervertebral disc.Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function.Decreased in vivo glucose uptake but normal expression of GLUT1 and GLUT4 in skeletal muscle of diabetic rats.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 reticulumHepatic cytochrome P450 degradation: mechanistic diversity of the cellular sanitation brigade.Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fateOligomeric structure of the human asialoglycoprotein receptor: nature and stoichiometry of mutual complexes containing H1 and H2 polypeptides assessed by fluorescence photobleaching recovery.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.Nonlysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor subunits: a TLCK- and TPCK-sensitive cleavage within the ER.Distinct intracellular fates of membrane and secretory immunoglobulin heavy chains in a pre-B cell lineA permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation.Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process.The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment.A non-autophagic pathway for diversion of ER secretory proteins to lysosomes.Two pathways for the degradation of the H2 subunit of the asialoglycoprotein receptor in the endoplasmic reticulum.Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval.In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using beta-lactamase gene fusionsN-glycan structure dictates extension of protein folding or onset of disposal.How early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.Endocytosis by the asialoglycoprotein receptor is independent of cytoplasmic serine residues.Unfolded protein response in filamentous fungi-implications in biotechnology.H2, the minor subunit of the human asialoglycoprotein receptor, trafficks intracellularly and forms homo-oligomers, but does not bind asialo-orosomucoid.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.A novel quality control compartment derived from the endoplasmic reticulumRole of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin.Overexpression of calsequestrin in L6 myoblasts: formation of endoplasmic reticulum subdomains and their evolution into discrete vacuoles where aggregates of the protein are specifically accumulated.Degradation of T-cell receptor chains in the endoplasmic reticulum is inhibited by inhibitors of cysteine proteases.The transmembrane anchor of the T-cell antigen receptor beta chain contains a structural determinant of pre-Golgi proteolysis.gamma-secretase cleavage is distinct from endoplasmic reticulum degradation of the transmembrane domain of the amyloid precursor protein.A complex of the soluble interleukin-6 receptor and interleukin-6 is internalized via the signal transducer gp130.Degradation of distinct assembly forms of immunoglobulin M occurs in multiple sites in permeabilized B cells.Blocking intracellular degradation of the erythropoietin and asialoglycoprotein receptors by calpain inhibitors does not result in the same increase in the levels of their membrane and secreted forms.Overexpression of the Bcl-2 protein increases the half-life of p21Bax.
P2860
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P2860
Intracellular degradation of unassembled asialoglycoprotein receptor subunits: a pre-Golgi, nonlysosomal endoproteolytic cleavage.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@ast
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@en
type
label
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@ast
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@en
prefLabel
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@ast
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@en
P2860
P356
P1476
Intracellular degradation of u ...... omal endoproteolytic cleavage.
@en
P2093
G Lederkremer
P2860
P304
P356
10.1083/JCB.109.6.3315
P407
P433
P577
1989-12-01T00:00:00Z