Results 11 to 20 of about 83,408 (297)
Compact conformations of human protein disulfide isomerase. [PDF]
PLoS ONE, 2014 Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum.
Shang Yang +8 more
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Protein Disulfide Isomerase and Host-Pathogen Interaction [PDF]
The Scientific World Journal, 2011 Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways ...
Beatriz S. Stolf +7 more
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The human protein disulfide isomerase gene family [PDF]
Human Genomics, 2012 Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known ...
Galligan James J, Petersen Dennis R
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Emerging roles of protein disulfide isomerase in cancer
BMB Reports, 2017 The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine-based redox reactions and assist the quality control of client proteins ...
Eun-Yup Lee, Do Hee Lee
semanticscholar +5 more sources
Inhibition of Protein Disulfide Isomerase in Thrombosis. [PDF]
Basic & Clinical Pharmacology & Toxicology, 2016 This 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.
Roelof H. Bekendam, R. Flaumenhaft
semanticscholar +4 more sources
Protein disulfide isomerase a multifunctional protein with multiple physiological roles [PDF]
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
doaj +3 more sources
Reversal of Alpha-Synuclein Fibrillization by Protein Disulfide Isomerase [PDF]
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
doaj +3 more sources
von Willebrand factor is dimerized by protein disulfide isomerase. [PDF]
Blood, 2016 Multimeric von Willebrand factor (VWF) is essential for primary hemostasis. The biosynthesis of VWF high-molecular-weight multimers requires spatial separation of each step because of varying pH value requirements.
Svenja Lippok +16 more
semanticscholar +5 more sources
Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy [PDF]
Scientific Reports, 2015 Protein disulfide isomerase (PDI) family members including PDI and ERp57 emerge as novel targets for anti-thrombotic treatments, but chemical agents with selectivity remain to be explored.
G. Cui +13 more
semanticscholar +3 more sources
Selective Inhibition of Protein Disulfide Isomerase by Estrogens
Journal of Biological Chemistry, 1989 Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
John C.M. Tsibris +5 more
openalex +4 more sources