Inhibition of protein disulfide isomerase induces differentiation of acute myeloid leukemia cells
Haematologica, 2018 A cute myeloid leukemia is a malignant disease of immature myeloid cells. Despite significant therapeutic effects of differentiation-inducing agents in some acute myeloid leukemia subtypes, the disease remains incurable in a large fraction of patients ...
Justyna Chlebowska-Tuz +22 more
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Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]
, 2017 The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J. +3 more
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Protein disulfide isomerase a multifunctional protein with multiple physiological roles
Frontiers in Chemistry, 2014 Protein disulfide isomerase (PDI), is a member of the thioredoxin superfamily of redox proteins. PDI has three catalytic activities including, thiol-disulfide oxireductase, disulfide isomerase and redox-dependent chaperone.
Hyder eAli Khan, Bulent eMutus
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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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Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]
, 2017 Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio +1 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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Influence of ellagitannins extracted by pomegranate fruit on disulfide isomerase PDIA3 activity [PDF]
, 2019 Pomegranate fruit is a functional food of high interest for human health due to its wide range of phytochemicals with antioxidant properties are implicated in the prevention of inflammation and cancer. Ellagitannins, such as punicalagin and ellagic acid,
Altieri, Fabio +6 more
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Multiple protein disulfide isomerases support thrombosis [PDF]
Current Opinion in Hematology, 2018 Purpose of review The present review provides an overview of recent findings on new members of the protein disulfide isomerase (PDI) family required for thrombosis. Recent findings Twenty years ago PDI was shown to mediate platelet aggregation, and 10 years ago PDI was shown to ...
David W, Essex, Yi, Wu
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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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