Results 81 to 90 of about 83,411 (273)
DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]
Journal of Biological Chemistry, 2000 DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
James C.A. Bardwell +3 more
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ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]
, 2013 ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke +4 more
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Conformational Resilience of Protein Disulfide Isomerase
The FASEB Journal, 2019 Protein disulfide isomerase (PDI) is a 57 kDa protein with both oxidoreductase and chaperone activities that is mainly localized to the endoplasmic reticulum. It is a U‐shaped protein with an abb'xa’ structural organization where the a and a′ domains have conserved CGHC active sites, the b and b′ domains are involved with substrate binding, and x is an
Jessica Guyette +3 more
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Identification of Protein-disulfide Isomerase Activity in Fibronectin [PDF]
Journal of Biological Chemistry, 1999 Assembly and degradation of fibronectin-containing extracellular matrices are dynamic processes that are up-regulated during wound healing, embryogenesis, and metastasis. Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers
Kurt J. Langenbach, Jane Sottile
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Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER [PDF]
, 2017 Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called non ...
Elias SJ Arnér +8 more
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Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]
, 2016 The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto +7 more
core +1 more source
Diabetes, Metabolic Syndrome and Obesity, 2020 Chunyan Liu, Yanan Hao, Fei Yin, Jianhui Liu Chongqing Key Laboratory of Medicinal Chemistry & Molecular Pharmacology, Chongqing University of Technology, Chongqing 400054, People’s Republic of ChinaCorrespondence: Jianhui Liu; Fei YinChongqing
Liu C, Hao Y, Yin F, Liu J
doaj
PLoS ONE, 2013 Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as
Roohi Vinaik +2 more
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Nature Communications, 2017 Protein disulfide isomerase (PDI), secreted by platelets and endothelial cells on vascular injury, is required for thrombus formation. Using PDI variants that form mixed disulfide complexes with their substrates, we identify by kinetic trapping multiple ...
semanticscholar +1 more source
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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