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.-Reference-Cited by-同舟云学术

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.

Published:1992-04 Issue:11 Volume:267 Page:7211-7214
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Vuori K,Myllylä R,Pihlajaniemi T,Kivirikko K.I.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference29 articles.

1. Experimental and Theoretical Aspects of Protein Folding

2. Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins

3. Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins

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

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

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