L. Arscott

发表

Glutathione reductase from yeast. Differential reactivity of the nascent thiols in two-electron reduced enzyme and properties of a monoalkylated derivative.

C. Thorpe, C. Williams, L. Arscott, 1981, Biochemistry.

Two modes of catalysis have evolved

R. Schirmer, K. Becker, Pan-Fen Wang, 2000 .

Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase.

G. Schulz, C. Williams, L. Arscott, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis.

R. Matthews, K. Wilkinson, C. Thorpe, 1979, Methods in enzymology.

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.

R. Schirmer, K. Becker, S. Gromer, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity.

G. L. Kenyon, R. Schirmer, K. Becker, 2003, Biochemistry.

Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin.

G. Zanetti, C. Williams, L. Arscott, 1967, The Journal of biological chemistry.

Human Placenta Thioredoxin Reductase

R. Schirmer, K. Becker, S. Gromer, 1998, The Journal of Biological Chemistry.

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

R. Matthews, C. Williams, L. Arscott, 1974, Biochimica et biophysica acta.

Thioredoxin reductase two modes of catalysis have evolved.

R. Schirmer, K. Becker, S. Müller, 2000, European journal of biochemistry.

Mechanistic Studies on a Novel, Highly Potent Gold-Phosphole Inhibitor of Human Glutathione Reductase*

K. Fritz-Wolf, K. Becker, E. Davioud‐Charvet, 2005, Journal of Biological Chemistry.

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.

Elias S. J. Arnér, D. Ballou, L. Johansson, 2006, Free radical biology & medicine.

Active sites of thioredoxin reductases: Why selenoproteins?

R. Schirmer, H. Bauer, S. Gromer, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol.

S. Müller, T. Gilberger, C. Williams, 1999, Biochemistry.

The Mechanism of High Mr Thioredoxin Reductase from Drosophila melanogaster*

R. Schirmer, H. Bauer, D. Ballou, 2003, Journal of Biological Chemistry.

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

L. Sahlman, J. Guest, A. Prongay, 1989, Annals of the New York Academy of Sciences.

Reductive and oxidative half-reactions of glutathione reductase from Escherichia coli.

N. Scrutton, R. Perham, A. Berry, 1994, Biochemistry.

Inactivation-reactivation of two-electron reduced Escherichia coli glutathione reductase involving a dimer-monomer equilibrium.

C. Williams, L. Arscott, D. M. Drake, 1989, Biochemistry.

Kinetic Characterization of Glutathione Reductase from the Malarial Parasite Plasmodium falciparum

R. Schirmer, K. Becker, L. Arscott, 2000, The Journal of Biological Chemistry.

Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD+/NADH redox couple: enzyme forms active in catalysis.

C. Williams, L. Arscott, D. M. Veine, 1998, Biochemistry.

Identification of Acid-Base Catalytic Residues of High-Mr Thioredoxin Reductase from Plasmodium falciparum*

K. Becker, S. Müller, P. McMillan, 2006, Journal of Biological Chemistry.

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

R. Schirmer, K. Becker, L. Arscott, 1998, FEBS letters.

Sequence around the Active Center Cystine of Lipoamide Dehydrogenase from Pig Heart, Comparison with the E. coli Enzyme

C. Williams, L. Arscott, 1972, Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie.

Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents.

C. Nickel, G. L. Kenyon, K. Becker, 2006, Bioorganic & medicinal chemistry letters.

Role of active site tyrosine residues in catalysis by human glutathione reductase.

R. Schirmer, R. Krauth-Siegel, C. Williams, 1998, Biochemistry.

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.

C. Williams, L. Arscott, D. M. Veine, 2000, Biochemistry.

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.

Charles H Williams, Zhiyong Cheng, D. Ballou, 2007, Biochemistry.

Post-Macondo Focus on Safety

L. Arscott, Roland Moreau, 2020 .

Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.

D. Ballou, L. Arscott, C. Williams, 2008, Biochemistry.