OrganismsChemicals and DrugsPhenomena and ProcessesInformation Science
GlutaredoxinsOxidoreductasesProtein Disulfide Reductase (Glutathione)ThioredoxinsThioredoxin-Disulfide ReductaseGlutathioneIron-Sulfur ProteinsOxidation-ReductionSulfhydryl CompoundsGlutathione DisulfideDisulfidesProteinsEscherichia coliCysteineIronSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeAmino Acid SequenceMolecular Sequence Data
ThioredoxinOxidoreductaseThioredoxinsGLRXGeneProteinsMacrophagesGlutathioneEnzymeMiceBackgroundEffectPrimaryHumanPeroxiredoxinMonothiol glutaredoxinsThioredoxin reductaseProteinThioltransferaseSuperoxide dismutaseGrx3MitochondrialGlutathione-dependentDisulfide bondArabidopsisReductaseClusterEquivalentsEncodesElectronSystemFunctionsType
Thioredoxin6
  • In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. (wikipedia.org)
  • Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulfide bond. (wikipedia.org)
  • The thioredoxin family consists of a small group of redox proteins present in all organisms and composed of thioredoxins (TRXs), glutaredoxins (GLRXs) and peroxiredoxins (PRDXs) which are found in the extracellular fluid, the cytoplasm, the mitochondria and in the nucleus with functions that include antioxidation, signaling and transcriptional control, among others. (curefa.org)
  • Redox post-translational modifications of proteins** In addition to performing structure-function analyses of thioredoxin (TRX) and glutaredoxin (GRX) family members which control most of the reversible oxidative modifications of protein cysteinyl residues, we are characterizing proteins of unknown function possessing one or several conserved CXXC motifs known to be particularly suited for disulfide bond formation but also other redox modifications. (hal.science)
  • Increased antioxidant gene expression, including superoxide dismutase, glutaredoxin and thioredoxin was also noted, indicating that oxidative stress may be driving the antimicrobial activity of zeolite silver nanoparticle supports. (cdc.gov)
  • More specifically, redox homeostasis broadly affects cellular metabolism and proliferation, with major contributions by thiol/disulfide oxidoreductase systems, in particular, the Thioredoxin Reductase Thioredoxin (TrxR/Trx) and the Glutathione Reductase-Glutathione-Glutaredoxin (GR/GSH/Grx) systems. (uni-muenchen.de)
Oxidoreductase3
  • Here, we provide biochemical and biophysical evidence that the oxidoreductase glutaredoxin 2 inhibits peroxynitrite formation by transforming nitric oxide into dinitrosyl-diglutathionyl-iron-complexes. (amsterdamumc.org)
  • Of note, glutaredoxin 2-mediated protection is not linked to its enzymatic activity as oxidoreductase, but to the disassembly of its uniquely coordinated iron-sulfur cluster using glutathione as non-protein ligand. (amsterdamumc.org)
  • Our group recently observed that male mice containing a deletion for the gene encoding the thiol oxidoreductase glutaredoxin-2 (GRX2) were protected from diet-induced obesity (DIO) and the development of related disorders (e.g. fatty liver disease). (mun.ca)
Thioredoxins2
  • Redox regulation, thioredoxins, and glutaredoxins in retrograde signalling and gene transcription. (bvsalud.org)
  • Redox regulation is an important point of control in protein structure, interactions, cellular location , and function, with thioredoxins (TRXs) and glutaredoxins (GRXs) being key players in the maintenance of cellular redox homeostasis . (bvsalud.org)
GLRX1
  • Glutaredoxin-1 (Glrx) enzymatically catalyzes the removal of S-glutathione adducts, conferring reversible signaling dynamics toproteins with redox-sensitive cysteines. (aston.ac.uk)
Gene2
  • Combining gene expression data, re-sequencing and re- annotation of one of these genomic regions identified a glutaredoxin-encoding gene PgGRXC9 as the candidate stress resilience root growth regulator. (sciety.org)
  • Functional characterization of its closest Arabidopsis homolog AtROXY19 revealed a novel role for this glutaredoxin (GRX) gene clade in regulating cell elongation. (sciety.org)
Proteins1
  • Since mitochondria are a major source of ROS and a number of their proteins are susceptible to protein-S-glutathionylation, we examined if overexpression of mitochondrial thioltranferase glutaredoxin 2a (Grx2a) in macrophages of dyslipidemic atherosclerosis-prone mice would prevent mitochondrial dysfunction and protect against atherosclerotic lesion formation. (ox.ac.uk)
Macrophages2
  • Glutaredoxin 2a overexpression in macrophages promotes mitochondrial dysfunction but has little or no effect on atherogenesis in LDL-receptor null mice. (ox.ac.uk)
  • Weinberg EO, Ferran B, Tsukahara Y, Hatch MMS, Han J, Murdoch CE, Matsui R. IL-33 induction and signaling are controlled by glutaredoxin-1 in mouse macrophages. (bu.edu)
Glutathione5
  • Glutaredoxins (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. (wikipedia.org)
  • Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. (wikipedia.org)
  • Instead, glutaredoxins are reduced by the oxidation of glutathione. (wikipedia.org)
  • Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. (wikipedia.org)
  • The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation" (PDF). (wikipedia.org)
Enzyme1
  • A mutant of the glutaredoxin enzyme that has one free cysteine was expressed in E. coli and covalently linked to a Grubbs-type olefin metathesis catalyst through a judiciously positioned-bromo ester electrophile. (europa.eu)
Mice1
  • In line, brain lesions of mice suffering from experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis, show decreased glutaredoxin 2 expression and increased nitrotyrosine formation indicating that this type of protection is missing in the inflamed central nervous system. (amsterdamumc.org)
Background1
  • For confocal microscopy, β-actin immunolabelling of ectoplasmic specializations was studied over the background of either prosaposin or glutaredoxin immunolabelling of the Sertoli cytoplasm. (techscience.com)
Effect1
  • The protective effect of glutaredoxin 2 is connected to decreased protein carbonylation and nitration. (amsterdamumc.org)
Primary1
  • Glutaredoxin 2 levels influence both survival rates of primary oligodendrocyte progenitor cells and preservation of myelin structure in cerebellar organotypic slice cultures challenged with activated microglia or nitric oxide donors. (amsterdamumc.org)
Human1
  • Human Glutaredoxin 3 Forms [2Fe-2S]-bridged Complexes with Human BolA2" by H. Li, D. T. Mapolelo et al. (sc.edu)
Peroxiredoxin2
  • Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. (prospecbio.com)
  • In collaboration with Dr Ché Pillay from the University of KwaZulu-Natal in Pietermaritzburg, I am developing kinetic models of redoxin networks (thioredoxin, glutaredoxin, peroxiredoxin) in Escherichia coli and Mycobacterium tuberculosis . (sun.ac.za)
Monothiol glutaredoxins2
  • Herein we describe an investigation of the cluster exchange reactivity of holo BOLA3-GLRX complexes using two different monothiol glutaredoxins, H.s. (nih.gov)
  • In fungi, monothiol glutaredoxins are central regulators of key cellular functions such as iron homeostasis, cell wall integrity and redox status via their interactions with other proteins as well as iron-sulfur clusters and glutathione. (ubc.ca)
Thioredoxin reductase3
  • In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. (wikipedia.org)
  • Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. (harvard.edu)
  • Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. (t3db.ca)
Protein5
  • On the basis of extensive sequence similarity, it has been proposed that Vaccinia virus protein O2L is, it seems, a glutaredoxin. (wikipedia.org)
  • We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. (harvard.edu)
  • We observe that a 1 : 1 mixture of apo BOLA3 and glutaredoxin protein is able to accept a cluster from donors such as ISCU and a [2Fe-2S](GS)4 complex, with preferential formation of the cluster-bridged heterodimer over the plausible holo homodimeric glutaredoxin. (nih.gov)
  • Using a EGSH biosensor, comprising human glutaredoxin-1 linked to a redox sensitive green fluorescent protein (hGrx1-roGFP2), the basal cytosolic EGSH as well as the antimalarial drug-induced changes in EGSH were determined in drug-sensitive (3D7) and resistant (Dd2) strains of P. falciparum. (shaker.de)
  • This gene encodes a protein containing a glutaredoxin domain, which functions in protein S-glutathionylation. (nih.gov)
Thioltransferase1
  • Glutaredoxins (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. (wikipedia.org)
Superoxide dismutase1
  • Increased antioxidant gene expression, including superoxide dismutase, glutaredoxin and thioredoxin was also noted, indicating that oxidative stress may be driving the antimicrobial activity of zeolite silver nanoparticle supports. (cdc.gov)
Grx32
  • Cluster exchange and calorimetry experiments resulted in a very similar behavior for yeast Grx3 (cytosolic) and human GLRX5 (mitochondrial), indicating conservation across the monothiol glutaredoxin family for interactions with BOLA3 and supporting a functional role for the BOLA3-GLRX5 heterocomplex relative to the previously proposed BOLA3-NFU1 interaction. (nih.gov)
  • Function of glutaredoxin 3 (Grx3) in oxidative stress response caused by iron homeostasis disorder in Candida albicans. (medscape.com)
Mitochondrial1
  • Human mitochondrial glutaredoxin 2 (Grx2) is a glutathione-dependent oxidoreductase (active site: Cys-Ser-Tyr-Cys) that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. (elsevierpure.com)
Glutathione-dependent1
  • Glutaredoxins function as electron carriers in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. (wikipedia.org)
Disulfide bond1
  • Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active centre disulfide bond. (wikipedia.org)
Arabidopsis1
  • Recent studies have shown that the Arabidopsis gene for monothiol glutaredoxin, named AtGRXS17, is a critical mediator of heat stress. (univation.co)
Reductase1
Cluster1
  • A single monothiol glutaredoxin (GRX) is involved in Fe-S cluster assembly in mitochondria of yeast and mammals. (strath.ac.uk)
Equivalents1
  • Arsenate reductases require reducing equivalents such as GLUTAREDOXIN or AZURIN. (bvsalud.org)
Encodes1
  • From NCBI Gene: This gene encodes a member of the glutaredoxin family. (nih.gov)
Electron1
  • In particular, the main reductive pathways are the glutaredoxin (Grx) and thioredoxin (Trx) systems, both of which share NADPH as their final electron donor. (gla.ac.uk)
System1
  • Dynamics of the glutathione/glutaredoxin system. (ukzn.ac.za)
Functions1
  • The role of glutathione in photosynthetic organisms: emerging functions for glutaredoxins and glutathionylation" (PDF). (wikipedia.org)
Type1
  • A very rare non-syndromic autosomal recessive pyridoxine-refractory sideroblastic anemia due to a splice defect of glutaredoxin-5 (GLRX5) described in a single patient with adult onset microcytic hypochromic anemia with liver iron overload and type 2 diabetes. (cdc.gov)