Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli.

Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli.

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http://www.wikidata.org/entity/Q54599822
MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress responseStrategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase.Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function.Formation and transfer of disulphide bonds in living cells.Drug-eluting stents: a mechanical and pharmacologic approach to coronary artery disease.Arabidopsis protein disulfide isomerase-8 is a type I endoplasmic reticulum transmembrane protein with thiol-disulfide oxidase activity.Strategies for achieving high-level expression of genes in Escherichia coli.Expression of active human tissue-type plasminogen activator in Escherichia coli.Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organismsMurine Wnt-1 with an internal c-myc tag recombinantly produced in Escherichia coli can induce intracellular signaling of the canonical Wnt pathway in eukaryotic cells.Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold.Novel protein-disulfide isomerases from the early-diverging protist Giardia lamblia.Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells.
P2860

Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli.

Item
http://www.wikidata.org/entity/Q54599822
description
1995 nî lūn-bûn
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1995年の論文
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1995年学术文章
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1995年学术文章
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1995年学术文章
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name
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@en
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@nl
type
label
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@en
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@nl
prefLabel
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@en
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P356
P1433
P1476
Human protein disulfide isomer ...... e lyase C in Escherichia coli.
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P921