Results 41 to 50 of about 3,418,558 (223)
Cell Reports, 2018 Summary: Multiple sulfatase deficiency (MSD) is a fatal, inherited lysosomal storage disorder characterized by reduced activities of all sulfatases in patients.
Lars Schlotawa +6 more
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Mapping of the ligand-binding site on the b ' domain of human PDI: interaction with peptide ligands and the x-linker region [PDF]
, 2009 PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum. PDI consists of four thioredoxin-like domains, of which two contain redox-active catalytic sites (a and a'), and two ...
Freedman, R. B. +15 more
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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
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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
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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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Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell [PDF]
, 1995 We investigated the effect of protein disulfide isomerase (PDI) on in vivo protein folding of human lysozyme (h-LZM) in a specially constructed yeast coexpression system.
Hayano, Toshiya +2 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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High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]
, 2013 ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxin-fold domains homologous with the non-catalytic b and b' domains of
Freedman, R. B. +15 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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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 ...
openaire +2 more sources