(Q41997546)

English

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

scientific article published on January 1999

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Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

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 (English)

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

molecular chaperones

0 references

author name string

Koivunen P

1

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Pirneskoski A

2

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Karvonen P

3

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Ljung J

4

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Helaakoski T

5

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Notbohm H

6

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Kivirikko KI

7

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

language of work or name

0 references

publication date

1 January 1999

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

The EMBO Journal

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

18

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

1

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

65-74

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Does DsbA have chaperone-like activity?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Cell-free synthesis and assembly of prolyl 4-hydroxylase: the role of the beta-subunit (PDI) in preventing misfolding and aggregation of the alpha-subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Secondary structure prediction of all-helical proteins in two states.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Protein disulfide isomerase associates with misfolded human lysozyme in vivo.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Thioredoxin--a fold for all reasons

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

A 30-amino acid truncation of the microsomal triglyceride transfer protein large subunit disrupts its interaction with protein disulfide-isomerase and causes abetalipoproteinemia

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Collagens: molecular biology, diseases, and potentials for therapy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

The retention signal for soluble proteins of the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Site-directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4-hydroxylase in Spodoptera frugiperda insect cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

5 June 2018

Cloning, baculovirus expression, and characterization of the alpha subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This alpha subunit forms an active alpha beta dimer with the human protein disulfide isomerase/beta subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1171103

18 August 2018

Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifying and characterizing a structural domain of protein disulfide isomerase

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A mutant truncated protein disulfide isomerase with no chaperone activity

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein disulfide isomerase appears necessary to maintain the catalytically active structure of the microsomal triglyceride transfer protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein disulphide isomerase: building bridges in protein folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase

1 reference

https://pubmed.ncbi.nlm.nih.gov/9878051

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1093/EMBOJ/18.1.65

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 October 2017

ResearchGate publication ID

0 references

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