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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.


thioltransferase, Grx2, Grx1, Grx
This gene encodes a member of the glutaredoxin family. The encoded protein is a cytoplasmic enzyme catalyzing the reversible reduction of glutathione-protein mixed disulfides. This enzyme highly contributes to the antioxidant defense system. It is crucial for several signalling pathways by controlling the S-glutathionylation status of signalling mediators. It is involved in beta-amyloid toxicity and Alzheimer's disease. Multiple alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: Thioredoxin, CAN, ACID, HAD, oxidoreductase
Papers using thioltransferase antibodies
Overexpression of thioredoxin1 in transgenic mice suppresses development of diabetic nephropathy.
Salloum Fadi N., In PLoS ONE, 2006
... Glutaredoxin 1 (Grx-1) transgenic mice carrying a human Grx-1 ...
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
Janssen-Heininger Yvonne M.W. et al., In The Journal of Cell Biology, 2002
... H (Lab Frontier), Grx1 (American Diagnostica Inc.), Trx1 (Santa Cruz ...
Papers on thioltransferase
Response of two rice cultivars differing in their sensitivity towards arsenic, differs in their expression of glutaredoxin and glutathione S transferase genes and antioxidant usage.
Mallick et al., Lucknow, India. In Ecotoxicol Environ Saf, Feb 2016
Embodied study investigates the role of GRX and associated antioxidant enzymes in the detoxification mechanism between arsenic (As) sensitive (Usar-3) and tolerant cultivar (Pant Dhan 11) of Oryza sativa against As(III) and As(V), under GSH enriched, and GSH deprived conditions.
Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.
Ferry et al., United States. In Biochemistry, Feb 2016
We report here the biochemical and structural properties of a GRX-like protein named methanoredoxin (MRX) from Methanosarcina acetivorans of the domain Archaea.
Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.
da Silva Neto et al., São Paulo, Brazil. In Free Radic Res, Feb 2016
Glutaredoxin (Grx) enzymes also contain the Trx fold, but they do not share amino acid sequence similarity with Trx.
Glutaredoxin S15 is involved in Fe-S cluster transfer in mitochondria influencing lipoic acid-dependent enzymes, plant growth and arsenic tolerance in Arabidopsis.
Millar et al., Perth, Australia. In Plant Physiol, Jan 2016
Our results show its exclusive mitochondrial localisation and we are concluding it is the major or only Grx in this subcellular location.
Why high cholesterol levels help hematological malignancies: role of nuclear lipid microdomains.
Albi et al., Perugia, Italy. In Lipids Health Dis, Dec 2015
Cholesterol does not change GRX2 expression but it overexpresses SOD1, SOD2, CCS, PRDX1, GSR, GSS, CAT and PNKP.
Bacterial thioredoxin and thioredoxin reductase as mediators for epigallocatechin 3-gallate-induced antimicrobial action.
Zhong et al., Beijing, China. In Febs J, Dec 2015
Thioredoxin (Trx) system and glutathione/glutaredoxin (Grx) system both support bacterial growth.
A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.
Salinas et al., Montevideo, Uruguay. In Antioxid Redox Signal, Nov 2015
In this study, we addressed the biochemical characterization of a new class of Trx-related protein (IsTRP) and a classical monothiol Grx (EgGrx5) from the human pathogen Echinococcus granulosus.
Plant-specific CC-type glutaredoxins: functions in developmental processes and stress responses.
Gatz et al., In Biol Chem, May 2015
Here we review recent research on a land plant-specific class of GRX-like proteins, which are characterized by the conserved CC motif in the active centre.
Physiological Function of Rac Prophage During Biofilm Formation and Regulation of Rac Excision in Escherichia coli K-12.
Wang et al., Guangzhou, China. In Sci Rep, 2014
In most E. coli strains, rac is integrated into the ttcA gene which encodes a tRNA-thioltransferase.
Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components.
Park et al., Manhattan, United States. In Hortic Res, 2014
Here, we report that tomato expressing Arabidopsis GRX gene AtGRXS17 conferred tolerance to chilling stress without adverse effects on growth and development.
The thioredoxin antioxidant system.
Holmgren et al., Stockholm, Sweden. In Free Radic Biol Med, 2014
In mammalian cells, the cytosolic and mitochondrial Trx systems, in which TrxRs are high molecular weight selenoenzymes, together with the glutathione-glutaredoxin (Grx) system (NADPH, glutathione reductase, GSH, and Grx) control the cellular redox environment.
Mono- and dithiol glutaredoxins in the trypanothione-based redox metabolism of pathogenic trypanosomes.
Bellanda et al., Montevideo, Uruguay. In Antioxid Redox Signal, 2013
In vitro, all three 1-C-Grxs as well as the cytosolic 2-C-Grx of Trypanosoma brucei can complex an iron-sulfur cluster.
Thioredoxin glutathione reductase-dependent redox networks in platyhelminth parasites.
Salinas et al., Chicago, United States. In Antioxid Redox Signal, 2013
Platyhelminth parasites possess a streamlined thiol-based redox system in which a single enzyme, thioredoxin glutathione reductase (TGR), a fusion of a glutaredoxin (Grx) domain to canonical thioredoxin reductase (TR) domains, supplies electrons to oxidized glutathione (GSSG) and thioredoxin (Trx).
In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
Rouhier et al., Vandœuvre-lès-Nancy, France. In Antioxid Redox Signal, 2013
No peroxidase activity was detected for Prx6, whereas both bacterioferritin comigratory proteins (BCPs) were regenerated by a NADH/thioredoxin reductase/glutaredoxin (Grx)-like system, constituting a unique peroxide removal system.
Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine.
Kim, Taegu, South Korea. In Acta Biochim Biophys Sin (shanghai), 2012
Data show that glutaredoxin acts as a reductant for methionine sulfoxide reductases A and B (MsrA and MsrB) with or without resolving cysteine.
Protective effect of the thioltransferase gene on in vivo UVR-300 nm-induced cataract.
Söderberg et al., Uppsala, Sweden. In Invest Ophthalmol Vis Sci, 2012
This result signifies that the presence of the gene allows a 1.3 times longer in vivo exposure to UVR, at equivalent irradiance, than the absence of the gene before early-onset.
Vertebrate-specific glutaredoxin is essential for brain development.
Berndt et al., Stockholm, Sweden. In Proc Natl Acad Sci U S A, 2012
Grx2 thiol redox regulation is essential for vertebrate embryonic development
Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells.
Lou et al., Lincoln, United States. In Free Radic Biol Med, 2012
Grx2 has a function that protects cells against H(2)O(2)-induced injury via its peroxidase and dethiolase activities; particularly, Grx2 prevents complex I inactivation and preserves mitochondrial function.
Glutaredoxin-1 overexpression enhances neovascularization and diminishes ventricular remodeling in chronic myocardial infarction.
Maulik et al., Farmington, United States. In Plos One, 2011
results are the first to demonstrate that Grx-1 induces angiogenesis and diminishes ventricular remodeling apparently through neovascularization mediated by Akt, VEGF, Ang-1 and NF-kappaB as well as Bcl-2 and survivin-mediated anti-apoptotic pathway
Thioredoxins and glutaredoxins: unifying elements in redox biology.
Reichheld et al., Perpignan, France. In Annu Rev Genet, 2008
Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function.
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