Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. [PDF]
, 2008 Sulfatase modifying factor 1 (SUMF1) encodes for the formylglicine generating enzyme, which activates sulfatases by modifying a key cysteine residue within their catalytic domains. SUMF1 is mutated in patients affected by multiple sulfatase deficiency, a
Annunziata F. +10 more
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Protein disulfide isomerase as an antithrombotic target [PDF]
Trends in Cardiovascular Medicine, 2013 Protein disulfide isomerase (PDI) is a ubiquitously expressed oxidoreductase required for proper protein folding. It is highly concentrated in the endoplasmic reticulum, but can also be released into the extracellular environment. Several in vivo thrombosis models have demonstrated that vascular PDI secreted by platelets and endothelial cells is ...
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Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm
Animals, 2021 Epididymal maturation can be defined as a scope of changes occurring during epididymal transit that prepare spermatozoa to undergo capacitation. One of the most common post-translational modifications involved in the sperm maturation process and their ...
Katarzyna Dyrda +3 more
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The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis [PDF]
, 2015 Mitochondria are fundamental intracellular organelles with key roles in important cellular processes like energy production, Fe/S cluster biogenesis, and homeostasis of lipids and inorganic ions.
Mordas, Amelia, Tokatlidis, Konstantinos
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Functional Differences in Yeast Protein Disulfide Isomerases [PDF]
The Journal of Cell Biology, 2001 PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to
P, Nørgaard +5 more
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A functionalized hydroxydopamine quinone links thiol modification to neuronal cell death
Redox Biology, 2020 Recent findings suggest that dopamine oxidation contributes to the development of Parkinson's disease (PD); however, the mechanistic details remain elusive.
Ali Farzam +6 more
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Molecules, 2021 Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues.
Shunsuke Okada +3 more
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Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]
, 2016 Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio +7 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
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Oxidative Protein-Folding Systems in Plant Cells
International Journal of Cell Biology, 2013 Plants are unique among eukaryotes in having evolved organelles: the protein storage vacuole, protein body, and chloroplast. Disulfide transfer pathways that function in the endoplasmic reticulum (ER) and chloroplasts of plants play critical roles in the
Yayoi Onda
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