A. Gustafsson

Hybridization of alpha class subunits generating a functional glutathione transferase A1-4 heterodimer.

B. Mannervik, A. Gustafsson, L. O. Nilsson, 2002, Journal of molecular biology.

Benzoic acid derivatives induce recovery of catalytic activity in the partially inactive Met208Lys mutant of human glutathione transferase A1-1.

B. Mannervik, A. Gustafsson, 1999, Journal of molecular biology.

Lowering of tumoral interstitial fluid pressure by prostaglandin E1 is paralleled by an increased uptake of 51Cr‐EDTA

R. Reed, M. Sjöquist, K. Rubin, 2000, International journal of cancer.

Human Glutathione Transferase A1-1 Demonstrates Both Half-of-the-sites and All-of-the-sites Reactivity*

B. Mannervik, S. Lien, A. Gustafsson, 2001, The Journal of Biological Chemistry.

Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.

B. Mannervik, A. Gustafsson, L. O. Nilsson, 2000, Proceedings of the National Academy of Sciences of the United States of America.

An evolutionary approach to the design of glutathione-linked enzymes.

P. Jemth, L. Hansson, B. Mannervik, 1998, Chemico-biological interactions.

New crystal structures of human glutathione transferase A1-1 shed light on glutathione binding and the conformation of the C-terminal helix.

G. Kleywegt, B. Mannervik, M. Novotný, 2006, Acta crystallographica. Section D, Biological crystallography.

Role of the glutamyl alpha-carboxylate of the substrate glutathione in the catalytic mechanism of human glutathione transferase A1-1.

P. Jemth, B. Mannervik, L. Grehn, 2001, Biochemistry.

The C-terminal region of human glutathione transferase A1-1 affects the rate of glutathione binding and the ionization of the active-site Tyr9.

P. Jemth, B. Mannervik, A. Gustafsson, 1999, Biochemistry.