Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum. [PDF]
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
Atomic Sulfur: An Element for Adaptation to an Oxidative Environment
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
Evidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandii. [PDF]
Clostridium oremlandii MsrA (CoMsrA) is a natively selenocysteine-containing methionine-S-sulfoxide reductase and classified into a 1-Cys type MsrA. CoMsrA exists as a monomer in solution.
Eun Hye Lee +6 more
doaj +1 more source
Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System
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
Increased glutaredoxin-1 and decreased proteinS-glutathionylation in sputum of asthmatics [PDF]
To the Editor: Total reduced glutathione (GSH), the main pulmonary antioxidant, is increased in asthma patients and, in some studies, increased amounts of oxidised glutathione (GSSG) were also found. In addition, enzymes that regulate the GSH redox cycle are altered in asthmatics (reviewed in [1]).
Kuipers, Ine +8 more
openaire +3 more sources
Glutaredoxin-1 overexpression enhances neovascularization and diminishes ventricular remodeling in chronic myocardial infarction. [PDF]
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
Knockdown of cytosolic glutaredoxin 1 leads to loss of mitochondrial membrane potential: implication in neurodegenerative diseases. [PDF]
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
Photo-labelling of glutaredoxin from Escherichia coli
N,N′-bis (4-azidobenzoyl) glutathione disulphide (1) was a strong inhibitor of glutaredoxin in the dark. The presence of 1 caused the velocity versus glutathione concentration curves of the glutaredoxin activity as assayed by E.
D'Silva, Claudius +7 more
core +1 more source
The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803 [PDF]
Arsenic resistance in Synechocystis sp. strain PCC 6803 is mediated by an operon of three genes in which arsC codes for an arsenate reductase with unique characteristics.
Reyes, José C. +7 more
core +1 more source
Glutathione and Glutaredoxin—Key Players in Cellular Redox Homeostasis and Signaling
This Special Issue of Antioxidants on Glutathione (GSH) and Glutaredoxin (Grx) was designed to collect review articles and original research studies focused on advancing the current understanding of the roles of the GSH/Grx system in cellular homeostasis
Yuh-Cherng Chai, John J. Mieyal
doaj +1 more source

