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Bengt Mannervik, Ph.D.

Professor Adjunct
Department of Molecular Medicine
California Campus
Scripps VIVO Scientific Profile
(858) 784-8636

Professional Experience

2016-2017 Professor Adjunct, Chemical Physiology, The Scripps Research Institute

Selected References

All Publications

Abdalla, A. M., Bruns, C. M., Tainer, J. A., Mannervik, B. & Stenberg, G. Design of a monomeric human glutathione transferase gstp1, a structurally stable but catalytically inactive protein. (2002). Protein Engineering, 15(10), 827-834.

Bruns, C. M., Hubatsch, I., Ridderstrom, M., Mannervik, B. & Tainer, J. A. Human glutathione transferase a4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. (1999). Journal of Molecular Biology, 288(3), 427-439.

Thorson, J. S., Shin, I., Chapman, E., Stenberg, G., Mannervik, B. & Schultz, P. G. Analysis of the role of the active site tyrosine in human glutathione transferase A1-1 by unnatural amino acid mutagenesis. (1998). Journal of the American Chemical Society, 120(2), 451-452.

Augustinsson, K. B., Bartfai, T. & Mannervik, B. A steady-state kinetic model of butyrylcholinesterase from horse plasma. (1974). Biochemical Journal, 141(3), 825-834. PMCID: PMC1168188.

Mannervik, B., Bartfai, T. & Gorna-Hall, B. Random pathway mechanism involving parallel one- and two- substrate branches for glyoxalase i from yeast. (1974). Journal of Biological Chemistry, 249(3), 901-903.

Bartfai, T. & Mannervik, B. Application of weight factors in the discrimination between mathematical models of enzyme kinetics. (1973). FEBS Letters, 32(1), 179-183.

Mannervik, B. & Bartfai, T. Discrimination between mathematical models of biological systems exemplified by enzyme steady state kinetics. (1973). Acta Biologica Et Medica Germanica, 31(2), 203-215.

Bartfai, T., Ekwall, K. & Mannervik, B. Discrimination between steady-state kinetic models of the mechanism of action of yeast glyoxalase I. (1973). Biochemistry, 12(3), 387-391.

Mannervik, B., Gorna-Hall, B. & Bartfai, T. The steady-state kinetics of glyoxalase I from porcine erythrocytes. Evidence for a random-pathway mechanism involving one- and two-substrate branches. (1973). European Journal of Biochemistry, 37(2), 270-281.

Bartfai, T. & Mannervik, B. A procedure based on statistical criteria for discrimination between steady state kinetic models. (1972). FEBS Letters, 26(1), 252-256.