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 (Q28212078)

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scientific article (publication date: November 1992)

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English	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	scientific article (publication date: November 1992)

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14 September 2019

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 (English)

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14 September 2019

endoplasmic reticulum

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Spodoptera frugiperda

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Spodoptera frugiperda

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K. Vuori

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14 September 2022

T. Pihlajaniemi

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14 September 2022

R. Myllylä

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14 September 2022

K. I. Kivirikko

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14 September 2022

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1 November 1992

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14 September 2019

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14 September 2022

https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/1327760/?tool=EBI

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14 September 2022

https://europepmc.org/articles/PMC556932

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14 September 2022

https://europepmc.org/articles/PMC556932?pdf=render

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14 September 2022

The EMBO Journal

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14 September 2019

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14 September 2019

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14 September 2019

4213-4217

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14 September 2019

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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20 March 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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20 March 2017

ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase

1 reference

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20 March 2017

The ERD2 gene determines the specificity of the luminal ER protein retention system

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ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway

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

1 reference

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

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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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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

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A C-terminal signal prevents secretion of luminal ER proteins

1 reference

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Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase

1 reference

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Control of protein exit from the endoplasmic reticulum

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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29 September 2017

Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins

1 reference

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29 September 2017

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

1 reference

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Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER.

1 reference

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29 September 2017

The retention signal for soluble proteins of the endoplasmic reticulum

1 reference

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29 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=556932

29 September 2017

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

1 reference

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29 September 2017

Mechanism of the Prolyl Hydroxylase Reaction. 2. Kinetic Analysis of the Reaction Sequence

1 reference

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29 September 2017

Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase

1 reference

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29 September 2017

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

1 reference

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Secretion of the extracellular domain of the human insulin receptor from insect cells by use of a baculovirus vector

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The catalytic mechanism of the hydroxylation reaction of peptidyl proline and lysine does not require protein disulphide-isomerase activity

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Role of protein disulphide-isomerase in the expression of native proteins

1 reference

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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

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1 reference

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1 reference

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Molecular biology of prolyl 4-hydroxylase

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/J.1460-2075.1992.TB05515.X

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14 September 2019

PMC publication ID

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14 September 2019

PubMed publication ID

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1327760%20AND%20SRC:MED&resulttype=core&format=json

14 September 2019

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