Results 11 to 20 of about 3,189 (173)
The significance of glutaredoxins for diabetes mellitus and its complications [PDF]
Redox BiologyDiabetes mellitus is a non-communicable metabolic disease hallmarked by chronic hyperglycemia caused by beta-cell failure. Diabetic complications affect the vasculature and result in macro- and microangiopathies, which account for a significantly ...
Mengmeng Zhou +4 more
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Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction [PDF]
Nature CommunicationsGlutaredoxins catalyze the reduction of disulfides and are key players in redox metabolism and regulation. While important insights were gained regarding the reduction of glutathione disulfide substrates, the mechanism of non-glutathione disulfide ...
Fabian Geissel +4 more
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Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates [PDF]
Nature CommunicationsClass I glutaredoxins (GRXs) are nearly ubiquitous proteins that catalyse the glutathione (GSH)-dependent reduction of mainly glutathionylated substrates. In land plants, a third class of GRXs has evolved (class III). Class III GRXs regulate the activity
Pascal Mrozek +6 more
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Glutaredoxin proteins from E. coli isoforms were compared in terms of energy frustration [PDF]
Brazilian Journal of Biology, 2023 Glutaredoxin (GRXs) protein plays a vital role inside the cell, including redox control of transcription to the cell's antioxidant defense, apoptosis, and cellular differentiation regulation.
A. Patel +7 more
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The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes
Antioxidants, 2023 From bacteria to plants and humans, the glutathione system plays a pleiotropic role in cell defense against metabolic, oxidative and metal stresses. Glutathione (GSH), the γ-L-glutamyl-L-cysteinyl-glycine nucleophile tri-peptide, is the central player of
Corinne Cassier-Chauvat +4 more
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Photosynthesis Research, 2006 Glutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Some monothiol GRXs exist with a single-Grx domain while others have a thioredoxin-like domain (Trx) and one or more Grx domains in tandem.
Herrero Perpiñán, Enrique +3 more
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One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx
Redox Biology, 2020 Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies.
Jannik Zimmermann +5 more
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G3: Genes, Genomes, Genetics, 2021 Monothiol glutaredoxins are important regulators of iron homeostasis that play conserved roles in the sensing and trafficking of iron-sulfur clusters.
Guanggan Hu +5 more
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Nuclear Monothiol Glutaredoxins of Saccharomyces cerevisiae Can Function as Mitochondrial Glutaredoxins [PDF]
Journal of Biological Chemistry, 2004 Glutaredoxins are thiol oxidoreductases that regulate protein redox state. In Saccharomyces cerevisiae, Grx1 and Grx2 are cytosolic dithiol glutaredoxins, whereas Grx3, Grx4, and Grx5 are monothiol glutaredoxins. Grx5 locates at the mitochondrial matrix and is needed for iron/sulfur cluster biogenesis. Its absence causes phenotypes such as inactivation
Molina Navarro, Maria Micaela +4 more
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Antioxidants, 2022 Soybean (Glycine max (L.) Merr.) establishes symbiosis with rhizobacteria, developing the symbiotic nodule, where the biological nitrogen fixation (BNF) occurs.
María Martha Sainz +5 more
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