Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.
about
Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease ACompact conformations of human protein disulfide isomeraseBiP and PDI cooperate in the oxidative folding of antibodies in vitroCatalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulinEndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factorIs protein disulfide isomerase a redox-dependent molecular chaperone?Oligomerization properties of ERp29, an endoplasmic reticulum stress proteinProtein disulfide isomerase acts as a molecular chaperone during the assembly of procollagenThiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assemblyVascular thiol isomerases.Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.Protein targets of monocrotaline pyrrole in pulmonary artery endothelial cells.Disulfide-dependent folding and export of Escherichia coli DsbC.The metallopeptide antibiotic bacitracin inhibits interleukin-12 alphabeta and beta2 secretion.Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution.The protein disulphide-isomerase family: unravelling a string of folds.Protein disulfide isomerase in thrombosis and vascular inflammationProfiling the venom gland transcriptomes of Costa Rican snakes by 454 pyrosequencing.Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.Glycoprotein folding in the endoplasmic reticulum.Glucose-stimulated translation regulation of insulin by the 5' UTR-binding proteins.Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation.A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding.Human retinal pigment epithelium proteome changes in early diabetesBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Versatility of the endoplasmic reticulum protein folding factory.Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitorBoth PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway.DsbA-L is a versatile player in adiponectin secretion.The redox switch that regulates molecular chaperones.ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexinInhibition of Protein Disulfide Isomerase in Thrombosis.Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.Enzymes as chaperones and chaperones as enzymes.The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.Dependence of the anti-chaperone activity of protein disulphide isomerase on its chaperone activity.Human pancreas-specific protein disulfide-isomerase (PDIp) can function as a chaperone independently of its enzymatic activity by forming stable complexes with denatured substrate proteins.Thermodynamics of the folding of D-glyceraldehyde-3-phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry.
P2860
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P2860
Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@ast
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@en
type
label
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@ast
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@en
prefLabel
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@ast
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@en
P2093
P2860
P356
P1433
P1476
Both the isomerase and chapero ...... tured acidic phospholipase A2.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/16.3.651
P407
P577
1997-02-01T00:00:00Z