Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin (Q28203834)

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Robert B Freedman

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Hauke Lilie

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Rainer Rudolph

Journal of Biological Chemistry

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language of work or name

English

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publication date

4 January 2002

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published in

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volume

277

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page(s)

310-7

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issue

1

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cites work

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

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

21 January 2018

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

21 January 2018

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

21 January 2018

1 reference

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

21 January 2018

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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.

21 January 2018

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

21 January 2018

1 reference

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The refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein

21 January 2018

1 reference

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Assisted refolding of recombinant prochymosin with the aid of protein disulphide isomerase

21 January 2018

1 reference

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Formation of native insulin from the scrambled molecule by protein disulphide-isomerase

21 January 2018

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Studies on the function of yeast protein disulfide isomerase in renaturation of proteins

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Discrimination between native and non-native disulfides by protein-disulfide isomerase

21 January 2018

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

21 January 2018

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

21 January 2018

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An Improved method for the purification of tRNA by chromatography on dlhydroxyboryl substituted cellulose

21 January 2018

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

21 January 2018

1 reference

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

21 January 2018

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Activation of partially folded mitochondrial malate dehydrogenase by thioredoxin.

21 January 2018

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Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

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

21 January 2018

1 reference

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Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding.

21 January 2018

1 reference

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Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro

21 January 2018

1 reference

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Putative folding pathway of insulin-like growth factor-I.

21 January 2018

1 reference

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release_eokg2oupnbcwxjev2eriddbuue

21 January 2018

Identifiers

DOI

10.1074/JBC.M107832200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/eokg2oupnbcwxjev2eriddbuue