Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin - sprookjes - yvandenbroek - TriplyDB

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

http://www.wikidata.org/entity/Q28203834

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Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A Scorpion toxins specific for potassium (K+) channels: a historical overview of peptide bioengineering Mechanism of insulin chain combination. Asymmetric roles of A-chain alpha-helices in disulfide pairing Design of an Active Ultrastable Single-chain Insulin Analog: SYNTHESIS, STRUCTURE, AND THERAPEUTIC IMPLICATIONS Solution Structure of Proinsulin: CONNECTING DOMAIN FLEXIBILITY AND PROHORMONE PROCESSING Is protein disulfide isomerase a redox-dependent molecular chaperone?Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain Deciphering a molecular mechanism of neonatal diabetes mellitus by the chemical synthesis of a protein diastereomer, [D-AlaB8]human proinsulin.Substrate recognition by the protein disulfide isomerases.Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes.Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates Beyond 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.The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.Disulfide Mispairing During Proinsulin Folding in the Endoplasmic Reticulum.Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.Generating an unfoldase from thioredoxin-like domains Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Redox-regulated export of the major histocompatibility complex class I-peptide complexes from the endoplasmic reticulum Inhibition of Protein Disulfide Isomerase in Thrombosis.Maternal caffeine exposure impairs insulin secretion by pancreatic β-cells and increases the risk of type II diabetes mellitus in offspring.GRP78, but Not Protein-disulfide Isomerase, Partially Reverses Hyperglycemia-induced Inhibition of Insulin Synthesis and Secretion in Pancreatic {beta}-Cells.Role of the connecting peptide in insulin biosynthesis.Behavior in the eukaryotic secretory pathway of insulin-containing fusion proteins and single-chain insulins bearing various B-chain mutations.Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation.Emerging roles of protein disulfide isomerase in cancer.Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding 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.In vitro refolding of human proinsulin. Kinetic intermediates, putative disulfide-forming pathway folding initiation site, and potential role of C-peptide in folding process.Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells.Protein Folding in the Presence of Water-Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities.Dietary soy isoflavones increased hepatic protein disulfide isomerase content and suppressed its enzymatic activity in rats.

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P2860

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

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description

2002 nî lūn-bûn

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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2002 թվականի հունվարին հրատարակված գիտական հոդված

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2002年の論文

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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Catalytic activity and chapero ...... icient refolding of proinsulin

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P1433

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P356

P1433

Journal of Biological Chemistry

P1476

Catalytic activity and chapero ...... icient refolding of proinsulin

@en

P2093

Hauke Lilie

http://www.w3.org/2001/XMLSchema#string

Jeannette Winter

http://www.w3.org/2001/XMLSchema#string

Peter Klappa

http://www.w3.org/2001/XMLSchema#string

Rainer Rudolph

http://www.w3.org/2001/XMLSchema#string

Robert B Freedman

http://www.w3.org/2001/XMLSchema#string

P2860

Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

BiP and PDI cooperate in the oxidative folding of antibodies in vitro

Reversible formation of on-pathway macroscopic aggregates during the folding of maltose binding protein

Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA.

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum.

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation.

An improved method for the purification of tRNA by chromatography on dihydroxyboryl substituted cellulose

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310-7

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scholarly article

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10.1074/JBC.M107832200

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P433

1

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P478

277

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P577

2002-01-04T00:00:00Z

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P698

11694508

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P921

molecular chaperones