Inhibition of Protein Disulfide Isomerase in Thrombosis [PDF]
Basic & Clinical Pharmacology & Toxicology, 2016 AbstractThis MiniReview addresses our current understanding of the mechanisms by which protein disulfide isomerase (PDI) mediates thrombus formation and discusses the potential of blocking thrombosis by targeting PDI. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic reticulum (ER) where they serve a critical role ...
Roelof H, Bekendam, Robert, Flaumenhaft
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Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans. [PDF]
, 2007 Protein disulfide isomerase (PDI) is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum.
Page, Antony P. +5 more
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Substrate recognition by the protein disulfide isomerases [PDF]
The FEBS Journal, 2007 Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Hatahet Feras, Ruddock Lloyd
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The physiological functions of mammalian endoplasmic oxidoreductin 1: on disulfides and more [PDF]
, 2012 Significance: The oxidative process of disulfide-bond formation is essential for the folding of most secretory and membrane proteins in the endoplasmic reticulum (ER).
Ramming, Thomas +1 more
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The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses
BMC Plant Biology, 2021 Background Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response.
Ying Lu +6 more
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Interaction of Calreticulin with Protein Disulfide Isomerase [PDF]
Journal of Biological Chemistry, 1995 We report here that calreticulin interacts with protein disulfide isomerase (PDI). The PDI-calreticulin complex can be dissociated by Zn(2+)-iminodiacetate-substituted Sepharose-agarose chromatography, suggesting that these interactions may be Zn2+-dependent.
S, Baksh +3 more
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Endoplasmic reticulum H₂O₂ : Ero1-driven generation and GPx-mediated detoxification [PDF]
, 2014 Endoplasmic reticulum (ER) oxidoreductin 1 alpha (Ero1alpha) is an ER-resident oxidase, which utilizes molecular oxygen (O2) as terminal electron acceptor to produce disulfide bonds and hydrogen peroxide (H2O2).
Ramming, Thomas
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A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion
Cell Reports, 2019 Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe +6 more
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Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase
Frontiers in Cell and Developmental Biology, 2020 Aggregates of α-synuclein contribute to the etiology of Parkinson’s Disease. Protein disulfide isomerase (PDI), a chaperone and oxidoreductase, blocks the aggregation of α-synuclein.
Albert Serrano +7 more
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A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding. [PDF]
PLoS ONE, 2014 Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI).
Li Zhu +4 more
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