(Q43909898)

28 November 2017

title

Protein disulfide isomerase as an enzyme and a chaperone in protein folding (English)

1 reference

28 November 2017

0 references

0 references

Chih-Chen Wang

1

1 reference

28 November 2017

language of work or name

English

0 references

publication date

1 January 2002

1 reference

28 November 2017

published in

Methods in Enzymology

1 reference

28 November 2017

volume

348

1 reference

28 November 2017

page(s)

66-75

1 reference

Protein disulphide isomerase: building bridges in protein folding

28 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Contributions of protein disulfide isomerase domains to its chaperone activity

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

The protein disulphide-isomerase family: unravelling a string of folds

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Thermophilic fungal protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Protein disulfide isomerase is both an enzyme and a chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Chaperone-Like Activity of Protein Disulfide-Isomerase in the Refolding Of Rhodanese

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

The enzymatic and non-enzymatic roles of protein-disulfide isomerase in apolipoprotein B secretion

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Procollagen binds to both prolyl 4-hydroxylase/protein disulfide isomerase and HSP47 within the endoplasmic reticulum in the absence of ascorbate

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Effects of non-nucleoside inhibitors of human immunodeficiency virus type 1 in cell-free recombinant reverse transcriptase assays

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Factors affecting the folding and association of flounder muscle glyceraldehyde-3-phosphate dehydrogenase, in vitro

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

A stable cold folding intermediate of rabbit muscle D-glyceraldehyde 3-phosphate dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Does DsbA have chaperone-like activity?

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Conformational and activity changes during guanidine denaturation of D-glyceraldehyde-3-phosphate dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

The general concept of molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Do molecular chaperones have to be proteins?

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Interaction of phospholipase A2 and its zymogen with divalent metal ions.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Tissue sulfhydryl groups

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Assay for enzyme activity by following the absorbance change of pH-indicators.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Isolation and characterization of two phospholipase as from the venom of Agkistrodon halys blomhoffii

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Oxidized redox state of glutathione in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

A mutant truncated protein disulfide isomerase with no chaperone activity

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Chaperone activity of DsbC

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

DsbG, a protein disulfide isomerase with chaperone activity

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Protein-disulfide isomerase activity of elongation factor EF-Tu

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

Effects of macromolecular crowding on protein folding and aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2802%2948627-2

7 January 2021

10.1016/S0076-6879(02)48627-2

Identifiers

DOI

1 reference

28 November 2017

1 reference