The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins
about
Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiPIntegration of UPRER and oxidative stress signaling in the control of intestinal stem cell proliferationFormation and intracellular transport of a heterodimeric viral spike protein complexGene therapy for hemophiliaLoss of BiP/GRP78 function blocks translocation of secretory proteins in yeastA3 domain region 1803-1818 contributes to the stability of activated factor VIII and includes a binding site for activated factor IXDefining 'full-length' recombinant factor VIII: a comparative structural analysis.Expression and characterization of a codon-optimized blood coagulation factor VIII.Transient transfection of serum-free suspension HEK 293 cell culture for efficient production of human rFVIII.Molecular cloning of a mouse 47-kDa heat-shock protein (HSP47), a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells.Comparison of factor VIII transgenes bioengineered for improved expression in gene therapy of hemophilia AProtein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levelsAdvancements in gene transfer-based therapy for hemophilia A.Eukaryotic coupled translation of tandem cistrons: identification of the influenza B virus BM2 polypeptide.Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum.BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complexSuppression of inhibitor formation against FVIII in a murine model of hemophilia A by oral delivery of antigens bioencapsulated in plant cellsThe role of cis dimerization of signal regulatory protein alpha (SIRPalpha) in binding to CD47How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.Most factor VIII B domain missense mutations are unlikely to be causative mutations for severe hemophilia A: implications for genotyping.Enhanced biosynthesis of coagulation factor VIII through diminished engagement of the unfolded protein response.The future of recombinant coagulation factors.Bioengineered coagulation factor VIII enables long-term correction of murine hemophilia A following liver-directed adeno-associated viral vector delivery.Bioengineering of coagulation factor VIII for efficient expression through elimination of a dispensable disulfide loopSimilarity of nucleotide interactions of BiP and GTP-binding proteins.Dissociation of glucose-regulated protein Grp78 and Grp78-IgE Fc complexes by ATP.Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP).Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface.The G protein of vesicular stomatitis virus has free access into and egress from the smooth endoplasmic reticulum of UT-1 cells.Conversion of a class II integral membrane protein into a soluble and efficiently secreted protein: multiple intracellular and extracellular oligomeric and conformational forms.Quality control in the endoplasmic reticulum: folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro.Transgene-host cell interactions mediate significant influences on the production, stability, and function of recombinant canine FVIIIStable high-level expression of factor VIII in Chinese hamster ovary cells in improved elongation factor-1 alpha-based systemA peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock familyParticipation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process.Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum.Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperone, BiP.Regulated export of a secretory protein from the ER of the hepatocyte: a specific binding site retaining C-reactive protein within the ER is downregulated during the acute phase response.
P2860
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P2860
The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins
description
1987 nî lūn-bûn
@nan
1987 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
The relationship of N-linked g ...... the secretion of glycoproteins
@ast
The relationship of N-linked g ...... the secretion of glycoproteins
@en
The relationship of N-linked g ...... the secretion of glycoproteins
@en-gb
The relationship of N-linked g ...... the secretion of glycoproteins
@nl
type
label
The relationship of N-linked g ...... the secretion of glycoproteins
@ast
The relationship of N-linked g ...... the secretion of glycoproteins
@en
The relationship of N-linked g ...... the secretion of glycoproteins
@en-gb
The relationship of N-linked g ...... the secretion of glycoproteins
@nl
prefLabel
The relationship of N-linked g ...... the secretion of glycoproteins
@ast
The relationship of N-linked g ...... the secretion of glycoproteins
@en
The relationship of N-linked g ...... the secretion of glycoproteins
@en-gb
The relationship of N-linked g ...... the secretion of glycoproteins
@nl
P2093
P2860
P921
P3181
P356
P1476
The relationship of N-linked g ...... the secretion of glycoproteins
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.105.6.2665
P407
P433
P577
1987-12-01T00:00:00Z