B Mannervik

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Glutathione transferases--structure and catalytic activity.

B. Mannervik, B. Ketterer, B Mannervik, 1988, CRC critical reviews in biochemistry.

Crystal structure of human glyoxalase I—evidence for gene duplication and 3D domain swapping

T A Jones, A D Cameron, B. Mannervik, 1997, The EMBO journal.

Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.

A D Cameron, B. Mannervik, A. Cameron, 1999, Structure.

Random pathway mechanism involving parallel one- and two- substrate branches for glyoxalase I from yeast.

B Mannervik, T Bartfai, B Górna-Hall, 1974, The Journal of biological chemistry.

Discrimination between steady-state kinetic models of the Mechanism of action of yeast glyoxalase I.

T. Bártfai, B. Mannervik, B Mannervik, 1973, Biochemistry.

The steady-state kinetics of glyoxalase I from porcine erythrocytes. Evidence for a random-pathway mechanism involving one- and two-substrate branches.

T. Bártfai, B. Mannervik, B Mannervik, 1973, European journal of biochemistry.

Nonlinear regression methods in design of experiments and mathematical modelling. Applications to the analysis of the steady-state kinetics of glutathione reductase.

B. Mannervik, B Mannervik, 1975, Bio Systems.

A steady-state-kinetic model for formaldehyde dehydrogenase from human liver. A mechanism involving NAD+ and the hemimercaptal adduct of glutathione and formaldehyde as substrates and free glutathione as an allosteric activator of the enzyme.

B. Mannervik, L. Uotila, B Mannervik, 1979, The Biochemical journal.

Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate.

T A Jones, A D Cameron, B. Mannervik, 1995, Structure.

The stereochemical configuration of the lactoyl group of S-lactoylglutathionine formed by the action of glyoxalase I from porcine erythrocytes and yeast.

B. Mannervik, B Mannervik, K Ekwall, 1973, Biochimica et biophysica acta.

The effect of ethanol on the steady‐state kinetics of glutathione S‐transferase a from rat liver

B. Mannervik, M. Warholm, B Mannervik, 1979, FEBS letters.

Molecular and catalytic properties of glutathione transferase mu from human liver: an enzyme efficiently conjugating epoxides.

B. Mannervik, M. Warholm, B Mannervik, 1983, Biochemistry.

Absence of a ping‐pong pathway in the kinetic mechanism of glutathione S‐transferase a from rat liver. Evidence based on quantitative comparison of the asymptotic properties of experimental data and alternative rate equations

B. Mannervik, B Mannervik, P Askelöf, 1975, FEBS letters.

X-ray absorption studies of the Zn2+ site of glyoxalase I.

B Chance, B. Chance, A. Mildvan, 1984, Biochemistry.

A steady-state kinetic model of butyrylcholinesterase from horse plasma.

T. Bártfai, B. Mannervik, B Mannervik, 1974, The Biochemical journal.

Human Glutathione Transferase A3-3, a Highly Efficient Catalyst of Double-bond Isomerization in the Biosynthetic Pathway of Steroid Hormones*

B. Mannervik, B Mannervik, A. Johansson, 2001, The Journal of Biological Chemistry.

Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.

A D Cameron, B. Mannervik, A. Cameron, 1999, Biochemistry.

Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties.

H. Jörnvall, B. Mannervik, M. Warholm, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Binding of the competitive inhibitor S‐(p‐bromobenzyl)‐glutathione to glyoxalase I from yeast

B. Mannervik, B Mannervik, E Marmstal, 1979, FEBS letters.

Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products.

J. Tainer, B. Mannervik, I. Hubatsch, 1999, Journal of molecular biology.

Purification and characterization of the flavoenzyme glutathione reductase from rat liver.

B. Mannervik, B Mannervik, I. Carlberg, 1975, The Journal of biological chemistry.

Multiple inhibition of glutathione S-transferase A from rat liver by glutathione derivatives: kinetic analysis supporting a steady-state random sequential mechanism.

B Mannervik, I Jakobson, M Warholm, 1979, The Biochemical journal.

Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling.

L. Hansson, B. Mannervik, B Mannervik, 1999, Journal of molecular biology.

A steady-state-kinetic random mechanism for glutathione S-transferase A from rat liver. A model involving kinetically significant enzyme-product complexes in the forward reaction.

B. Mannervik, M. Warholm, B Mannervik, 1977, European journal of biochemistry.

Acquired resistance to cisplatin and doxorubicin in a small cell lung cancer cell line is correlated to elevated expression of glutathione-linked detoxification enzymes.

J. Bergh, U. Hellman, O. Brodin, 1994, Carcinogenesis.