Protein Disulfide Isomerases Function as the Missing Link Between Diabetes and Cancer. [PDF]
Jiang H +5 more
europepmc +1 more source
Oxidative protein folding in the mitochondrial intermembrane space [PDF]
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
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by neuromuscular connectivity decline followed by motoneuron loss.
Martin Sepulveda +15 more
doaj +1 more source
Critical roles of protein disulfide isomerases in balancing proteostasis in the nervous system. [PDF]
Medinas DB, Rozas P, Hetz C.
europepmc +1 more source
Identifying Interaction Partners of Yeast Protein Disulfide Isomerases Using a Small Thiol-Reactive Cross-Linker: Implications for Secretory Pathway Proteostasis. [PDF]
Freije BJ +8 more
europepmc +1 more source
Selective Inhibition of Protein Disulfide Isomerase by Estrogens
Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
J C, Tsibris +5 more
openaire +2 more sources
Protein disulfide isomerases (PDIs) negatively regulate ebolavirus structural glycoprotein expression in the endoplasmic reticulum (ER) via the autophagy-lysosomal pathway. [PDF]
Wang B +10 more
europepmc +1 more source
Molecular cloning and characterization of protein disulfide isomerase of Brugia malayi, a human lymphatic filarial parasite [PDF]
Lymphatic filariasis results in an altered lymphatic system and the abnormal enlargement of body parts, causing pain, serious disability and social stigma.
Doharey, Pawan Kumar +5 more
core +1 more source
Environmental stressors disrupt secretory protein folding and proteostasis in the endoplasmic reticulum (ER), leading to ER stress. The unfolded protein response (UPR) senses ER stress and restores proteostasis by increasing the expression of ER-resident
Rina Carrillo +4 more
doaj +1 more source

