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Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents

Bioorganic & medicinal chemistry letters, 2006-04, Vol.16 (8), p.2283-2292

2006

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Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue

FEBS letters, 1998-02, Vol.422 (3), p.311-314

1998

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Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds

The Journal of biological chemistry, 1998-08, Vol.273 (32), p.20096-20101

1998

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The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Proceedings of the National Academy of Sciences - PNAS, 1997-04, Vol.94 (8), p.3621-3626

1997

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Mechanism-Based Inactivation of Thioredoxin Reductase from Plasmodium falciparum by Mannich Bases. Implication for Cytotoxicity

Biochemistry (Easton), 2003-11, Vol.42 (45), p.13319-13330

2003

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Thioredoxin reductase two modes of catalysis have evolved

European journal of biochemistry, 2000-10, Vol.267 (20), p.6110-6117

2000

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Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme

The Journal of biological chemistry, 2000-12, Vol.275 (48), p.37317-37323

2000

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Role of Active Site Tyrosine Residues in Catalysis by Human Glutathione Reductase

Biochemistry (Easton), 1998-10, Vol.37 (40), p.13968-13977

1998

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Mixed Disulfide with Glutathione as an Intermediate in the Reaction Catalyzed by Glutathione Reductase from Yeast and as a Major Form of the Enzyme in the Cell

Biochemistry (Easton), 2000-04, Vol.39 (16), p.4711-4721

2000

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The Relationship of the Redox Potentials of Thioredoxin and Thioredoxin Reductase from Drosophila melanogaster to the Enzymatic Mechanism: Reduced Thioredoxin Is the Reductant of Glutathione in Drosophila

Biochemistry (Easton), 2007-07, Vol.46 (26), p.7875-7885

2007

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Thioredoxin Reductase from Plasmodium falciparum: Evidence for Interaction between the C-Terminal Cysteine Residues and the Active Site Disulfide−Dithiol

Biochemistry (Easton), 1999-03, Vol.38 (10), p.3187-3196

1999

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Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD+/NADH Redox Couple: Enzyme Forms Active in Catalysis

Biochemistry (Easton), 1998-11, Vol.37 (44), p.15575-15582

1998

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Active Sites of Thioredoxin Reductases: Why Selenoproteins?

Proceedings of the National Academy of Sciences - PNAS, 2003-10, Vol.100 (22), p.12618-12623

2003

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Amino Acid Sequence Homology between Pig Heart Lipoamide Dehydrogenase and Human Erythrocyte Glutathione Reductase

Proceedings of the National Academy of Sciences - PNAS, 1982-04, Vol.79 (7), p.2199-2201

1982

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Reductive and Oxidative Half-Reactions of Glutathione Reductase from Escherichia coli

Biochemistry (Easton), 1994-11, Vol.33 (46), p.13888-13895

1994

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Failure of bromocriptine therapy to control juvenile mammary hypertrophy

British journal of plastic surgery, 2001-12, Vol.54 (8), p.720-723

2001

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Studies of an active site mutant of the selenoprotein thioredoxin reductase: The Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme

Free radical biology & medicine, 2006-08, Vol.41 (4), p.649-656

2006

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The Mechanism of High M r Thioredoxin Reductase from Drosophila melanogaster

The Journal of biological chemistry, 2003-08, Vol.278 (35), p.33020-33028

2003

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The oxidative and reductive half reactions of subunit interface mutants of Escherichia coli glutathione reductase

Biochemical Society transactions, 1996-02, Vol.24 (1), p.9S

1996

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The Mechanism of High M sub(r) Thioredoxin Reductase from Drosophila melanogaster

The Journal of biological chemistry, 2003-08, Vol.278 (35), p.33020-33028

2003

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Properties of Lipoamide Dehydrogenase and Thioredoxin Reductase from Escherichia coli Altered by Site-Directed Mutagenesis

Annals of the New York Academy of Sciences, 1989, Vol.573 (1), p.55-65

1989

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Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD super(+)/NADH Redox Couple: Enzyme Forms Active in Catalysis

Biochemistry (Easton), 1998-11, Vol.37 (44), p.15575-15582

1998

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Lipoamide Dehydrogenase, Glutathione Reductase, Thioredoxin Reductase, and Thioredoxin

The Journal of biological chemistry, 1967-11, Vol.242 (22), p.5226-5231

1967

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Chemical burns as assault injuries in Jamaica

BURNS, 1996-03, Vol.22 (2), p.154-155

1996

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Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase

BBA - Enzymology, 1974-11, Vol.370 (1), p.26-38

1974

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Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents

Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue

Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Mechanism-Based Inactivation of Thioredoxin Reductase from Plasmodium falciparum by Mannich Bases. Implication for Cytotoxicity

Thioredoxin reductase two modes of catalysis have evolved

Kinetic characterization of glutathione reductase from the malarial parasite Plasmodium falciparum. Comparison with the human enzyme

Role of Active Site Tyrosine Residues in Catalysis by Human Glutathione Reductase

Mixed Disulfide with Glutathione as an Intermediate in the Reaction Catalyzed by Glutathione Reductase from Yeast and as a Major Form of the Enzyme in the Cell

The Relationship of the Redox Potentials of Thioredoxin and Thioredoxin Reductase from Drosophila melanogaster to the Enzymatic Mechanism: Reduced Thioredoxin Is the Reductant of Glutathione in Drosophila

Thioredoxin Reductase from Plasmodium falciparum: Evidence for Interaction between the C-Terminal Cysteine Residues and the Active Site Disulfide−Dithiol

Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD+/NADH Redox Couple: Enzyme Forms Active in Catalysis

Active Sites of Thioredoxin Reductases: Why Selenoproteins?

Amino Acid Sequence Homology between Pig Heart Lipoamide Dehydrogenase and Human Erythrocyte Glutathione Reductase

Reductive and Oxidative Half-Reactions of Glutathione Reductase from Escherichia coli

Failure of bromocriptine therapy to control juvenile mammary hypertrophy

Studies of an active site mutant of the selenoprotein thioredoxin reductase: The Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme

The Mechanism of High M r Thioredoxin Reductase from Drosophila melanogaster

The oxidative and reductive half reactions of subunit interface mutants of Escherichia coli glutathione reductase

The Mechanism of High M sub(r) Thioredoxin Reductase from Drosophila melanogaster

Properties of Lipoamide Dehydrogenase and Thioredoxin Reductase from Escherichia coli Altered by Site-Directed Mutagenesis

Redox Potentials for Yeast, Escherichia coli and Human Glutathione Reductase Relative to the NAD super(+)/NADH Redox Couple: Enzyme Forms Active in Catalysis

Lipoamide Dehydrogenase, Glutathione Reductase, Thioredoxin Reductase, and Thioredoxin

Chemical burns as assault injuries in Jamaica

Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase

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