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
doaj +1 more source
Inhibition of Protein Disulfide Isomerase in Thrombosis [PDF]
Basic & Clinical Pharmacology & Toxicology, 2016 AbstractThis 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. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic reticulum (ER) where they serve a critical role ...
Roelof H, Bekendam, Robert, Flaumenhaft
openaire +2 more sources
Genes and Diseases, 2018 Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family.
Hedy A. Chawsheen +3 more
doaj +1 more source
Soluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification. [PDF]
PLoS ONE, 2013 Human leukemia inhibitory factor (hLIF) is a multifunctional cytokine that is essential for maintaining the pluripotency of embryonic stem cells. hLIF may be also be useful in aiding fertility through its effects on increasing the implantation rate of ...
Jung-A Song +12 more
doaj +1 more source
Protein disulfide isomerase plays a crucial role in mediating chemically-induced, glutathione depletion-associated hepatocyte injury in vitro and in vivo. [PDF]
Cell Commun SignalZhu YY, Zhang Q, Jia YC, Hou MJ, Zhu BT.
europepmc +3 more sources
Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms [PDF]
, 2006 Substrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. Three of them, Asp, Glu, and (oxidized) Cys, function through their conjugation to Arg, one of destabilizing N-terminal residues that are recognized directly by
Brower, Christopher S. +7 more
core +2 more sources
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
doaj +1 more source
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
core +1 more source
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
openaire +2 more sources
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