Results 51 to 60 of about 135,439,936 (222)
Atomic Sulfur: An Element for Adaptation to an Oxidative Environment
Molecules, 2017 During the period of rising oxygen concentration in the Earth’s atmosphere (Figure 1), sulfur atoms were incorporated into proteins as redox-active cysteine residues [1] and antioxidant molecules such as thioredoxin, glutathione, and glutaredoxin ...
Noryuki Nagahara, Maria Wróbel
doaj +1 more source
Involvement of glutaredoxin-1 and thioredoxin-1 in β-amyloid toxicity and Alzheimer's disease [PDF]
Cell Death & Differentiation, 2005 Strong evidence indicates oxidative stress in the pathogenesis of Alzheimer's disease (AD). Amyloid beta (Abeta) has been implicated in both oxidative stress mechanisms and in neuronal apoptosis. Glutaredoxin-1 (GRX1) and thioredoxin-1 (TRX1) are antioxidants that can inhibit apoptosis signal-regulating kinase (ASK1).
S, Akterin +6 more
openaire +2 more sources
Journal of Chemical Physics, 2022 Glutaredoxins are small enzymes that catalyze the oxidation and reduction of protein disulfide bonds by the thiol-disulfide exchange mechanism. They have either one or two cysteines in their active site, resulting in different catalytic reaction cycles ...
Julian Böser +3 more
semanticscholar +1 more source
Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum. [PDF]
, 2009 The malarial parasite Plasmodium falciparum possesses a functional thioredoxin and glutathione system comprising the dithiol-containing redox proteins thioredoxin (Trx) and glutaredoxin (Grx), as well as plasmoredoxin (Plrx), which is exclusively found ...
Sturm, Nicole +23 more
core +2 more sources
Glutaredoxin-1 overexpression enhances neovascularization and diminishes ventricular remodeling in chronic myocardial infarction. [PDF]
PLoS ONE, 2012 Oxidative stress plays a critical role in the pathophysiology of cardiac failure, including the modulation of neovascularization following myocardial infarction (MI).
Ram Sudheer Adluri +9 more
doaj +1 more source
Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System
, 2020 Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing ...
Noriyuki Nagahara
core +1 more source
Biochemical and Biophysical Research Communications - BBRC, 2022 Thioredoxin (Trx) family proteins are key players in redox signaling. Here, we have analyzed glutaredoxin (Grx) 1 and Grx2 in age-related macular degeneration (AMD) and in retinal pigment epithelial (ARPE-19) cells.
E. Hanschmann +6 more
semanticscholar +1 more source
Glutaredoxin-1 levels in plasma can predict future events in patients with cardiovascular diseases.
Free Radical Biology & Medicine, 2021 Reactive oxygen species that increase during cardiovascular disease (CVD) react with protein cysteine residues to form a glutathione adduct by S-glutathionylation, which is selectively removed by glutaredoxin-1 (Glrx).
Yosuke Watanabe +10 more
semanticscholar +1 more source
Knockdown of cytosolic glutaredoxin 1 leads to loss of mitochondrial membrane potential: implication in neurodegenerative diseases. [PDF]
PLoS ONE, 2008 Mitochondrial dysfunction including that caused by oxidative stress has been implicated in the pathogenesis of neurodegenerative diseases. Glutaredoxin 1 (Grx1), a cytosolic thiol disulfide oxido-reductase, reduces glutathionylated proteins to protein ...
Uzma Saeed +5 more
doaj +1 more source
BMB Reports, 2021 Protein S-glutathionylation is a reversible post-translational modification on cysteine residues forming a mixed disulfide with glutathione. S-glutathionylation, not only protects proteins from oxidation but also regulates the functions of proteins ...
Sungwon Hwang +4 more
semanticscholar +1 more source