Differential expression of islet glutaredoxin 1 and 5 with high reactive oxygen species production in a mouse model of diabesity. [PDF]
The onset and progression of diabetes mellitus type 2 is highly contingent on the amount of functional beta-cell mass. An underlying cause of beta-cell decay in diabetes is oxidative stress, which markedly affects the insulin producing pancreatic cells ...
Sebastian Friedrich Petry +3 more
doaj +2 more sources
The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins where they function as ...
Heba Al Khamici +11 more
doaj +2 more sources
A Prognostic Activity of Glutaredoxin 1 Protein (Grx1) in Colon Cancer. [PDF]
Glutaredoxin 1 (Grx1) is an essential enzyme that regulates redox signal transduction and repairs protein oxidation by reversing S-glutathionylation, an oxidative modification of protein cysteine residues. Grx1 removes glutathione from proteins to restore their reduced state (protein-SH) and regulate protein-SSG levels in redox signaling networks. Thus,
Brzozowa-Zasada M +6 more
europepmc +3 more sources
Corrigendum to “Glutaredoxin 1 deficiency promotes intestinal epithelial cell copper toxicity in inflammatory bowel disease” [Redox Biology 93 (2026) 104164] [PDF]
Tiantian Zhang +11 more
doaj +2 more sources
Redox Regulation via Glutaredoxin-1 and Protein S-Glutathionylation. [PDF]
Significance: Over the past several years, oxidative post-translational modifications of protein cysteines have been recognized for their critical roles in physiology and pathophysiology.
Matsui R +7 more
europepmc +4 more sources
Evaluation of a dithiocarbamate derivative as an inhibitor of human glutaredoxin-1. [PDF]
Glutaredoxins (GRX) are involved in the regulation of thiol redox state. GRX-1 is a cytosolic enzyme responsible for the catalysis of deglutathionylation of proteins. To date, very few inhibitors of GRX-1 have been reported.The objective of this paper is to report 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethyl-sulfanylthiocarbonylamino ...
Sadhu SS +4 more
europepmc +4 more sources
Glutaredoxin 1 Downregulation in the Substantia Nigra Leads to Dopaminergic Degeneration in Mice [PDF]
AbstractBackgroundParkinson's disease (PD) is characterized by a severe loss of the dopaminergic (DA) neurons in the substantia nigra pars compacta (SNpc). Perturbation of protein thiol redox homeostasis has been shown to play a role in the dysregulation of cell death and cell survival signaling pathways in these neurons.
Aditi Verma +7 more
openaire +3 more sources
The oxidizability of cysteine residues is exploited in redox chemistry and as a source of stabilizing disulfide bonds, but it also raises the possibility that these side chains will be oxidized when they should not be.
Stefanie S. Eben, James A. Imlay
doaj +1 more source
Regulation of DJ-1 by Glutaredoxin 1 in Vivo: Implications for Parkinson's Disease. [PDF]
Parkinson's disease (PD) is the second most common neurodegenerative disease worldwide, caused by the degeneration of the dopaminergic neurons in the substantia nigra. Mutations in PARK7 (DJ-1) result in early onset autosomal recessive PD, and oxidative modification of DJ-1 has been reported to regulate the protective activity of DJ-1 in vitro ...
Johnson WM +15 more
europepmc +4 more sources
Mechanism of 1-Cys type methionine sulfoxide reductase Aregeneration by glutaredoxin
1-Cys MsrA; Disulfide bond; Glutaredoxin; Glutathionylation ...
이공주
core +1 more source

