The back cover picture shows a 3D model of the tumor-relevant, homodimeric form of human gluta- thione transferase P1 (GSTP1, PDB: 5GSS) and inhibition of its enzymatic activity by a synthetic 1,2,4-triox- ane. This compound and analogous derivatives are able to interact with the glutathione binding site of each GSTP1 monomer and often exhibit a parabolic competitive mode of inhibition where two molecules of inhibitor compete with one substrate molecule for binding. For further details, see the Full Paper by Markus Pietsch et al. on p. 629 ff.
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The back cover picture shows a 3D model of the tumor-relevant, homodimeric form of human gluta-thione transferase P1 (GSTP1, PDB: 5GSS) and inhibition of its enzymatic activity by a synthetic 1,2,4-triox-ane. This compound and analogous derivatives are able to interact with the glutathione binding site ofeach GSTP1 monomer and often exhibit a parabolic competitive mode of inhibition where two moleculesof inhibitor compete with one substrate molecule for binding. For further details, see the Full Paper byMarkus Pietsch et al. on p. 629 ff.
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