BiP and PDI cooperate in the oxidative folding of antibodies in vitro
about
ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressInteractions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulinJPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifspERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulinAge-enhanced endoplasmic reticulum stress contributes to increased Atg9A inhibition of STING-mediated IFN-β production during Streptococcus pneumoniae infectionHierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase.Efficient production of human bivalent and trivalent anti-MUC1 Fab-scFv antibodies in Pichia pastorisComprehensive engineering of Escherichia coli for enhanced expression of IgG antibodiesRole of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.A peptidic unconjugated GRP78/BiP ligand modulates the unfolded protein response and induces prostate cancer cell deathBeyond transcription--new mechanisms for the regulation of molecular chaperones.Modulation of conotoxin structure and function is achieved through a multienzyme complex in the venom glands of cone snails.Decreased enzyme activities of chaperones PDI and BiP in aged mouse livers.Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitorERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway.The activities and function of molecular chaperones in the endoplasmic reticulum.Protein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor.Targeting antibodies to the cytoplasm.Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae.Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates.Cysteines in CH1 underlie retention of unassembled Ig heavy chains.Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.Roles of silkworm endoplasmic reticulum chaperones in the secretion of recombinant proteins expressed by baculovirus system.Engineering toward a bacterial "endoplasmic reticulum" for the rapid expression of immunoglobulin proteins.Culture temperature modulates aggregation of recombinant antibody in cho cells.Molecular docking and molecular dynamics studies reveal structural basis of inhibition and selectivity of inhibitors EGCG and OSU-03012 toward glucose regulated protein-78 (GRP78) overexpressed in glioblastoma.An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.Protein disulfide isomerase family proteins involved in soybean protein biogenesis.Characterization of an A-Site Selective Protein Disulfide Isomerase A1 Inhibitor.Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system.The nucleotide exchange factor SIL1 is required for glucose-stimulated insulin secretion from mouse pancreatic beta cells in vivo
P2860
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P2860
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@ast
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@en
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@nl
type
label
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@ast
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@en
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@nl
prefLabel
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@ast
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@en
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@nl
P2093
P2860
P356
P1476
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
@en
P2093
P2860
P304
P356
10.1074/JBC.M002655200
P407
P577
2000-09-22T00:00:00Z