Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity (Q41205782)

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scientific article published on April 1996

Language	Label	Description	Also known as
English	Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity	scientific article published on April 1996

Statements

scholarly article

1 reference

Europe PubMed Central

28 September 2017

Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity (English)

1 reference

Europe PubMed Central

28 September 2017

author name string

Veijola J

1

1 reference

Europe PubMed Central

28 September 2017

Pihlajaniemi T

2

1 reference

Europe PubMed Central

28 September 2017

Kivirikko KI

3

1 reference

Europe PubMed Central

28 September 2017

language of work or name

0 references

publication date

1 April 1996

1 reference

Europe PubMed Central

28 September 2017

Biochemical Journal

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Europe PubMed Central

28 September 2017

315 ( Pt 2)

1 reference

Europe PubMed Central

28 September 2017

613-618

1 reference

Europe PubMed Central

28 September 2017

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=1217240

28 September 2017

The use of baculoviruses as expression vectors

1 reference

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Protein disulfide isomerase associates with misfolded human lysozyme in vivo.

1 reference

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

1 reference

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28 September 2017

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

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Collagens: molecular biology, diseases, and potentials for therapy

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The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum

1 reference

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28 September 2017

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

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28 September 2017

A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase

1 reference

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Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryo

1 reference

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28 September 2017

Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts

1 reference

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

1 reference

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Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity

1 reference

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28 September 2017

Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217240

28 September 2017

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=1217240

28 September 2017

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=1217240

28 September 2017

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=1217240

28 September 2017

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=1217240

17 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=1217240

17 June 2018

The complete cDNA derived sequence of the rat prolyl 4-hydroxylase alpha subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217240

19 August 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=1217240

19 August 2018

Site-directed mutagenesis of the alpha subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1217240

19 August 2018

10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of the oligosaccharides of prolyl hydroxylase, a microsomal glycoprotein

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Recent developments in posttranslational modification: intracellular processing

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase beta-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular biology of prolyl 4-hydroxylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

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/8615837

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/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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/8615837

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/8615837

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/8615837

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/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Prolyl 4-hydroxylase: defective assembly of alpha-subunit mutants indicates that assembled alpha-subunits are intramolecularly disulfide bonded

1 reference

https://pubmed.ncbi.nlm.nih.gov/8615837

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/BJ3150613

1 reference

Europe PubMed Central

28 September 2017

release_uzw6agdu7jg33khjau6pcmc57y

1 reference

https://api.fatcat.wiki/v0/release/uzw6agdu7jg33khjau6pcmc57y

24 November 2022

based on heuristic

mapped directly with Wikidata item

1 reference

Europe PubMed Central

28 September 2017

1 reference

Europe PubMed Central

28 September 2017

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