ArticleThe EMBO journal1999
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.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 58 citations in OpenAlex.
- Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.Molecular plant · 2021Article
- On the role of protein disulfide isomerase in the retrograde cell transport of secreted phospholipases A2.PloS one · 2015Article
- Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode Brugia malayi.The Journal of biological chemistry · 2013Article
- Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.PloS one · 2013Article
- Generating an unfoldase from thioredoxin-like domains.The Journal of biological chemistry · 2009Article
- The activities and function of molecular chaperones in the endoplasmic reticulum.Seminars in cell & developmental biology · 2007Review
- Identification of redox sensitive thiols of protein disulfide isomerase using isotope coded affinity technology and mass spectrometry.Journal of the American Society for Mass Spectrometry · 2007Article
- Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics.Antioxidants & redox signaling · 2003Review
- Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A.Protein science : a publication of the Protein Society · 2003Article
- Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding.The Biochemical journal · 2001Article
- Native disulfide bond formation in proteins.Current opinion in chemical biology · 2000Review
- Assignment of 1H, 13C and 15N resonances of the a' domain of protein disulfide isomerase.Journal of biomolecular NMR · 1999Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerase (PDI) is a multifunctional polypeptide that acts as a subunit in the animal prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding. We report here that deletion of PDI sequences corresponding to the entire C-terminal domain c, previously thought to be critical for chaperone activity, had no inhibitory effect on the assembly of recombinant prolyl 4-hydroxylase in insect cells or on the in vitro chaperone activity or disulfide isomerase activity of purified PDI. However, partially overlapping critical regions for all these functions were identified at the C-terminal end of the preceding thioredoxin-like domain a'. Point mutations introduced into this region identified several residues as critical for prolyl 4-hydroxylase assembly. Circular dichroism spectra of three mutants suggested that two of these mutations may have caused only local alterations, whereas one of them may have led to more extensive structural changes. The critical region identified here corresponds to the C-terminal alpha helix of domain a', but this is not the only critical region for any of these functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.