Results 61 to 70 of about 135,439,936 (222)
Proceedings of the National Academy of Sciences, 1994 Thioredoxin (Trx) and glutaredoxin (Grx1) are hydrogen donors for ribonucleotide reductase, the key enzyme for deoxyribonucleotide biosynthesis. The viability of a double mutant lacking both Trx and Grx1 implies the presence of a third, unknown hydrogen donor.
F, Aslund +4 more
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Activation of the glutaredoxin-1 gene by nuclear factor κB enhances signaling [PDF]
Free Radical Biology and Medicine, 2011 The transcription factor nuclear factor κB (NF-κB) is a critical regulator of inflammation and immunity and is negatively regulated via S-glutathionylation. The inhibitory effect of S-glutathionylation is overcome by glutaredoxin-1 (Grx1), which under physiological conditions catalyzes deglutathionylation and enhances NF-κB activation.
Aesif, S.W. +10 more
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Intrinsically Disordered Region Modulates Ligand Binding in Glutaredoxin 1 from Trypanosoma Brucei.
Journal of Physical Chemistry B, 2021 Glutaredoxins are small proteins that share a common well-conserved thioredoxin-fold and participate in a wide variety of biological processes. Among them, class II Grx are redox-inactive proteins involved in iron-sulfur (Fe-S) metabolism. In the present
G. Balatti +5 more
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Modulation of Glutaredoxin-1 Expression in a Mouse Model of Allergic Airway Disease [PDF]
American Journal of Respiratory Cell and Molecular Biology, 2007 Abstract Glutaredoxins (GRX) are antioxidant enzymes that preferentially catalyze the reduction of protein-glutathione mixed disulfides. The formation of mixed disulfides with GSH is known as S-glutathionylation, a post-translational modification that is emerging as an important mode of redox signaling.
Reynaert, N.L. +2 more
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Glutathione and Glutaredoxin—Key Players in Cellular Redox Homeostasis and Signaling
Antioxidants, 2023 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
Photo-labelling of glutaredoxin from Escherichia coli
, 1982 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
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The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803 [PDF]
, 2009 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
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OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli
Redox Biology, 2019 Sulfane sulfur species including hydrogen polysulfide and organic persulfide are newly recognized normal cellular components, and they participate in signaling and protect cells from oxidative stress.
Ningke Hou +7 more
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Molecules, 2021 Parkinson’s disease (PD) is characterized mainly by the loss of dopaminergic neurons in the substantia nigra (SN) mediated via oxidative stress. Although glutaredoxin-1 (GLRX1) is known as one of the antioxidants involved in cell survival, the effects of
Yeon Joo Choi +13 more
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Free Radical Biology & MedicineVascular senescence serves as a critical pathophysiological foundation for systemic organ aging in humans. Glutaredoxin 1 (Grx1), a key regulator of intracellular redox signaling, plays a critical role in modulating cellular senescence. In this study, we
Fang Li +9 more
semanticscholar +1 more source