Thioredoxins
Mostrando 1-12 de 51 artigos, teses e dissertações.
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1. Structural studies of the proteins Q4DV70 from Trypanosoma cruzi and mesothelin from Homo sapiens / Estudos estruturais das proteinas Q4DV70 de Trypanosoma cruzi e mesotelina de Homo sapiens
In this work we carried out studies with two proteins, Q4DV70 from Trypanosoma cruzi and mesothelin from Homo sapiens. The aim was to help the understanding of the function of these proteins which possibly are important to Chagas disease and cancer, respectively. Q4DV70 protein was annotated in T. cruzi genome as a conserved hypothetical protein. In our stud
Publicado em: 2009
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2. In silico analysis of Eucalyptus thioredoxins
The Eucalyptus Genome Sequencing Project (FORESTs), an initiative from the Brazilian ONSA consortium (Organization for Nucleotide Sequencing and Analysis), has achieved the sequencing of 123.889 EST clones from 18 different cDNA libraries. We have investigated the FORESTs data set to identify EST clusters potentially encoding thioredoxins (TRX). Two types of
Genetics and Molecular Biology. Publicado em: 2005
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3. Presença e atividade da proteína quiescina sulfidril oxidase em sorofetal e neonatal
Production of reactive oxygen and nitrogen species during embryonic and fetal development has been demonstrated in the last few years. Among these species, superoxide radical anion, hydrogen peroxide and nitric oxide radical, enzymatically produced, have been considered. Their tightly controlled production provides the adequate concentrations necessary for t
Publicado em: 2005
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4. In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae
Whereas vertebrates possess only two thioredoxin genes, higher plants present a much greater diversity of thioredoxins. For example, Arabidopsis thaliana has five cytoplasmic thioredoxins (type h) and at least as many chloroplastic thioredoxins. The abundance of plant thioredoxins leads to the question whether the various plant thioredoxins play a similar ro
The National Academy of Sciences.
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5. Thioredoxin from Brugia malayi: Defining a 16-Kilodalton Class of Thioredoxins from Nematodes
Thioredoxins are a family of small redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase. This results in a supply of reducing equivalents that cells use in a wide variety of biological reactions, which include maintaining reduced forms of the enzymes important for protection against damage from high-energy oxygen radicals, the regul
American Society for Microbiology.
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6. Proteomics gives insight into the regulatory function of chloroplast thioredoxins
Thioredoxins are small multifunctional redox active proteins widely if not universally distributed among living organisms. In chloroplasts, two types of thioredoxins (f and m) coexist and play central roles in regulating enzyme activity. Reduction of thioredoxins in chloroplasts is catalyzed by an iron-sulfur disulfide enzyme, ferredoxin-thioredoxin reductas
The National Academy of Sciences.
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7. Spinach thioredoxin m inhibits DNA synthesis in fertilized Xenopus eggs.
A role for thioredoxin in metazoan DNA synthesis has been assessed by injecting rapidly dividing Xenopus eggs with purified heterologous thioredoxins, which might act as inhibitors if they were to replace resident thioredoxins in some but not all reaction steps. Of 10 tested proteins, spinach chloroplast thioredoxin m is the most potent inhibitor. Eggs cleav
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8. Thioredoxins and the redox modulation of glucose-6-phosphate dehydrogenase in Anabaena sp. strain PCC 7120 vegetative cells and heterocysts.
Glucose-6-phosphate dehydrogenase (G6PDH) was isolated from heterocysts and vegetative cells of Anabaena sp. strain PCC 7120. Both enzyme preparations proved to be more active in their oxidized than in their reduced forms. At least one protein with thioredoxin activity was found in Anabaena sp. which, if reduced with dithiothreitol, deactivated the G6PDH pre
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9. Evidence for five divergent thioredoxin h sequences in Arabidopsis thaliana.
Five different clones encoding thioredoxin homologues were isolated from Arabidopsis thaliana cDNA libraries. On the basis of the sequences they encode divergent proteins, but all belong to the cytoplasmic thioredoxins h previously described in higher plants. The five proteins obtained by overexpressing the coding sequences in Escherichia coli present typica
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10. 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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11. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure.
An expression system has been established for the incorporation of selenomethionine into recombinant proteins produced from plasmids in Escherichia coli. Replacement of methionine by selenomethionine is demonstrated at the level of 100% for both T4 and E. coli thioredoxins. The natural recombinant proteins and the selenomethionyl variants of both thioredoxin
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12. Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120.
Thioredoxin is a small redox protein that functions as a reducing agent and modulator of enzyme activity. A gene for an unusual thioredoxin was previously isolated from the cyanobacterium Anabaena sp. strain PCC 7120 and cloned and expressed in Escherichia coli. However, the protein could not be detected in Anabaena cells (J. Alam, S. Curtis, F. K. Gleason,