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Free Radical Biology and Medicine, 2014
Glutaredoxins (Grxs) and thioredoxins (Trxs) play important roles in maintaining intracellular thiol-redox homeostasis by scavenging reactive oxygen species. However, few Grxs and Trxs have been functionally characterized in Apis cerana cerana. In this study, we identified three genes, AccGrx1, AccGrx2, and AccTrx1, and investigated their connection to
Pengbo, Yao +6 more
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Glutaredoxins (Grxs) and thioredoxins (Trxs) play important roles in maintaining intracellular thiol-redox homeostasis by scavenging reactive oxygen species. However, few Grxs and Trxs have been functionally characterized in Apis cerana cerana. In this study, we identified three genes, AccGrx1, AccGrx2, and AccTrx1, and investigated their connection to
Pengbo, Yao +6 more
openaire +2 more sources
Microbial Pathogenesis
Visceral leishmaniasis, caused by Leishmania, remains a global health concern with limited treatment options. Although the polyene drug Amphotericin-B has been considered effective, the emergence of drug resistance compromises its efficacy.
B. Priya, Afreen Nawaz, A. Rai, V. Ali
semanticscholar +1 more source
Visceral leishmaniasis, caused by Leishmania, remains a global health concern with limited treatment options. Although the polyene drug Amphotericin-B has been considered effective, the emergence of drug resistance compromises its efficacy.
B. Priya, Afreen Nawaz, A. Rai, V. Ali
semanticscholar +1 more source
Current molecular medicine
BACKGROUND Aerobic organisms continuously generate small amounts of Reactive Oxygen Species (ROS), which are involved in the oxidation of sensitive cysteine residues in proteins, leading to the formation of disulfide bonds.
Efthymios Poulios +4 more
semanticscholar +1 more source
BACKGROUND Aerobic organisms continuously generate small amounts of Reactive Oxygen Species (ROS), which are involved in the oxidation of sensitive cysteine residues in proteins, leading to the formation of disulfide bonds.
Efthymios Poulios +4 more
semanticscholar +1 more source
Glutaredoxin-1 regulates TRAF6 activation and the IL-1 receptor/TLR4 signalling
Biochemical and Biophysical Research Communications, 2010Glutaredoxin-1 (GRX-1) is a cytoplasmic enzyme that highly contributes to the antioxidant defense system. It catalyzes the reversible reduction of glutathione-protein mixed disulfides, a process called deglutathionylation. Here, we investigated the role of GRX-1 in the pathway triggered by interleukin-1/Toll-like receptor 4 (IL-1R/TLR4) by using RNA ...
Eleni, Chantzoura +4 more
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Expression of Glutaredoxin-1 in Nasal Polyps and Airway Epithelial Cells
American Journal of Rhinology & Allergy, 2009Background Glutaredoxins (GRX)-1 is glutathione-dependent oxidoreductase. However, the role of these enzymes remains unknown in airway inflammatory diseases. Therefore, we aimed to establish the expression pattern of GRX-1 in the nasal polyps (NPs) and to assess the regulatory mechanisms associated with GRX-1 ...
Hyun-Jae, Woo +5 more
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Abstract 21314: Glutaredoxin-1: An Endothelial Protector in Hyperlipidemia
Circulation, 2017Background: Hypercholesterolemia (HC) dominates the risk factors for atherosclerosis. Sustained oxidative stress is a central mechanism driving endothelial dysfunction (ED) in HC. But the underlying redox mechanism remains unclear.
Jingyan Han, Huijie Fan, Naomi Hamburg
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Biochemical and Biophysical Research Communications - BBRC, 2020
Glutaredoxin 1 (Grx1) is an important thiol transferase that catalyses the deglutathionylation of proteins through its active site. Deletion of Grx1 increases levels of glutathione-protein adducts and improves ischaemic revascularization.
Xuwei Liu +5 more
semanticscholar +1 more source
Glutaredoxin 1 (Grx1) is an important thiol transferase that catalyses the deglutathionylation of proteins through its active site. Deletion of Grx1 increases levels of glutathione-protein adducts and improves ischaemic revascularization.
Xuwei Liu +5 more
semanticscholar +1 more source
Glutaredoxin-1 control on liver fibrosis in aged mice
Free Radical Biology and Medicine, 2017Objective Glutaredoxin-1 (Glrx) is a cytosolic enzyme which removes glutathione (GSH) adducts of protein thiols (S-glutathionylation), and controls protein functions including cellular signaling and gene transcription. We previously showed that Glrx knockout middle-aged mice developed liver steatosis and Glrx replenishment by viral gene transfer ...
Yuko Tsukahara +4 more
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Comparative Biochemistry and Physiology Part B Comparative Biochemistry, 2020
Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis.
Rajamanthrilage Kasun Madusanka +4 more
semanticscholar +1 more source
Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis.
Rajamanthrilage Kasun Madusanka +4 more
semanticscholar +1 more source
In vivo quantitative measurement of oxidation repair of glutaredoxin‐1
Acta Ophthalmologica, 2010Abstract Purpose Quantitative determination of the impact of glutaredoxin‐1 on sensitivity to oxidative stress induced by in vivo exposure to ultraviolet radiation in the 300 nm wavelength region. Methods Altogether, 20 glutredoxin‐1 knockout mice (Grx1 ‐/‐) and 20 wild type C57BL/6, bred on the same background were in vivo exposed unilaterally to ...
PG SÖDERBERG +3 more
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