Thioredoxin‐interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress [PDF]
EMBO Molecular Medicine, 2014 The endoplasmic reticulum (ER) is responsible for protein folding, modification, and trafficking. Accumulation of unfolded or misfolded proteins represents the condition of ER stress and triggers the unfolded protein response (UPR), a key mechanism ...
Samuel Lee +10 more
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Non-Canonical, Strongly Selective Protein Disulfide Isomerases as Anticancer Therapeutic Targets [PDF]
BiomoleculesProtein Disulfide Isomerases (PDIs) are emerging targets in anticancer therapy, with several PDI inhibitors demonstrating anticancer efficacy in preclinical models.
Mary E. Law +9 more
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Multiple protein disulfide isomerases support thrombosis. [PDF]
Curr Opin Hematol, 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 ...
Essex DW, Wu Y.
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HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases [PDF]
Redox Biology, 2017 Protein disulfide isomerase (PDI) present at platelet surfaces has been considered to play an important role in the conformational change and activation of the integrin glycoprotein IIb/IIIa (GPIIb/IIIa) and thus enhances platelet aggregation.
Po-Hsiung Kung +5 more
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Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases. [PDF]
Biochem J, 2014 Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Shepherd C, Oka OB, Bulleid NJ.
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Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17 [PDF]
Scientific Reports, 2018 A Disintegrin and Metalloprotease 17 (ADAM17) can cause the fast release of growth factors and inflammatory mediators from the cell surface. Its activity has to be turned on which occurs by various stimuli.
Sebastian Krossa +3 more
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Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols [PDF]
AntioxidantsThiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
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Protein Disulfide Isomerases Regulate IgE-Mediated Mast Cell Responses and Their Inhibition Confers Protective Effects During Food Allergy [PDF]
Frontiers in Immunology, 2020 The thiol isomerase, protein disulfide isomerase (PDI), plays important intracellular roles during protein folding, maintaining cellular function and viability.
Dylan Krajewski +13 more
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Activity‐Based Protein Profiling Identifies Protein Disulfide‐Isomerases as Target Proteins of the Volatile Salinilactones [PDF]
Advanced ScienceThe salinilactones, volatile marine natural products secreted from Salinispora arenicola, feature a unique [3.1.0]‐lactone ring system and cytotoxic activities through a hitherto unknown mechanism.
Karoline Jerye +6 more
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Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development [PDF]
Thrombosis JournalVascular thiol isomerases (VTIs) encompass proteins such as protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERp5), ERp46, ERp57, ERp72, thioredoxin-related transmembrane protein 1 (TMX1), and TMX4, and play pivotal functions in ...
Longguang Jiang +3 more
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