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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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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Oxidative protein folding in the mitochondrial intermembrane space [PDF]
, 2010 Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB +4 more
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Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase [PDF]
Journal of Biological Chemistry, 1999 Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic reticulum and is secreted by cells and associates with the cell surface. We examined the consequence of over- or underexpression of PDI in HT1080 fibrosarcoma cells for the redox state of cell-surface protein thiols/disulfides ...
Philip J. Hogg +3 more
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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.
Alan D. Winter +44 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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Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization. [PDF]
PLoS ONE, 2013 BACKGROUND: Tau protein is implicated in the pathogenesis of neurodegenerative disorders such as tauopathies including Alzheimer disease, and Tau fibrillization is thought to be related to neuronal toxicity. Physiological inhibitors of Tau fibrillization
Li-Rong Xu +3 more
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