Glutaredoxin
Mostrando 1-12 de 51 artigos, teses e dissertações.
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1. An early stage in T4-induced hyperthyroidism is related to systemic oxidative stress but does not influence the pentose cycle in erythrocytes and systemic inflammatory status
ABSTRACT Objective Hyperthyroidism causes many injuries in its target organs and the consequences are reflected systemically. As systemic alterations in hyperthyroidism at earlier stages have received partial attention, this study aimed to investigate systemic redox and inflammatory status at an early stage of T4-induced hyperthyroidism. Materials and met
Arch. Endocrinol. Metab.. Publicado em: 25/04/2019
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2. Caracterização estrutural e funcional das glutarredoxinas ditiolicas de Saccharomyces cerevisiae
Glutarredoxinas (Grxs) são pequenas oxidorredutases que possuem pelo menos um resíduo de cisteína conservado em seus sítios ativos e têm atividade dissulfeto redutase dependente de tiol. Embora Grxs estejam envolvidas em diversos processos celulares, como enovelamento protéico e proteção contra espécies reativas de oxigênio, poucos substratos biol�
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 12/08/2009
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3. Thioredoxin/Glutaredoxin System of Chlorella1: CHLORELLA ADENOSINE 5′-PHOSPHOSULFATE SULFOTRANSFERASE CANNOT USE THIOREDOXIN OR GLUTAREDOXIN AS COFACTORS
Using the thioredoxin/glutaredoxin-dependent adenosine 3′-phosphate 5′-phosphosulfate reductase coupled assay system, the Chlorella thioredoxin/glutaredoxin system has been partially purified and characterized. A NADPH-thioredoxin reductase and two thioredoxin/glutaredoxin activities, designated as Chlorella thioredoxin/glutaredoxin protein I and II (CPI
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4. Isolation and characterization of an Escherichia coli K-12 mutant deficient in glutaredoxin.
Mutants of Escherichia coli K-12 deficient in glutaredoxin were isolated and partially characterized. The mutants have detectable but significantly reduced glutaredoxin activity in assays of whole cells made permeable with ether as well as in assays of crude extracts coupled to ribonucleotide reductase. In vivo, the mutants appear to be deficient in both sul
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5. Construction and characterization of glutaredoxin-negative mutants of Escherichia coli.
Deoxyribonucleotides, the precursors of DNA, are formed de novo by ribonucleotide reductase, and in vitro thioredoxin or glutathione plus glutaredoxin have been isolated as hydrogen donors. The in vivo hydrogen donor for ribonucleotide reductase is not known. To study this, the Escherichia coli glutaredoxin gene (255 base pairs) was inactivated by inserting
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6. Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.
Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups. Components of the thioredoxin/glutaredoxin system from cultured HeLa cells have been partially purified and characterized by using Escherichia coli adenosine 3'-phosphate 5'-phosphosulfate reductase, a thioredoxin/glu
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7. Assimilatory sulfate reduction in Escherichia coli: identification of the alternate cofactor for adenosine 3'-phosphate 5'-phosphosulfate reductase as glutaredoxin.
The alternate cofactor (7004 cofactor) for Escherichia coli adenosine 3'-phosphate 5'-phosphosulfate (PAPS) reductase originally discovered in an E. coli mutant (tsnC 7004) lacking thioredoxin activity has now been purified and characterized. The tryptic peptide map of the 7004 cofactor is totally different from that of thioredoxin, indicating that the two p
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8. Novel Glutaredoxin Activity of the Yeast Prion Protein Ure2 Reveals a Native-like Dimer within Fibrils*
Ure2 is the protein determinant of the Saccharomyces cerevisiae prion [URE3]. Ure2 has structural similarity to glutathione transferases, protects cells against heavy metal and oxidant toxicity in vivo, and shows glutathione-dependent peroxidase activity in vitro. Here we report that Ure2 (which has no cysteine residues) also shows thiol-disulfide oxido
American Society for Biochemistry and Molecular Biology.
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9. Conformational and functional similarities between glutaredoxin and thioredoxins.
The tertiary structures of thioredoxin from Escherichia coli and bacteriophage T4 have been compared and aligned giving a common fold of 68 C alpha atoms with a root mean square difference of 2.6 A. The amino acid sequence of glutaredoxin has been aligned to those of the thioredoxins assuming that glutaredoxin has the same common fold. A model of the glutare
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10. Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis.
We have shown previously that Escherichia coli cells constructed to lack both thioredoxin and glutaredoxin are not viable unless they also acquire an additional mutation, which we called X. Here we show that X is a cysA mutation. Our data suggest that the inviability of a trxA grx double mutant is due to the accumulation of 3'-phosphoadenosine 5'-phosphosulf
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11. Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.
Purified calf thymus ribonucleoside-diphosphate reductase (2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin 2'-oxidoreductase, EC 1.17.4.1), showed an absolute requirement for a dithiol as hydrogen donor, whereas the natural monothiol glutathione (GSH) was inactive per se. However, a protein partially purified from thymus coupled the oxidation of GSH
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12. Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.
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. This paper reports the purification and characterization of two proteins with glutaredoxin activity