Now showing items 1-4 of 4

    • Inhibition of monoamine oxidase B by N-methyl-2-phenylmaleimides 

      Manley-King, Clarina I.; Terre'blanche, Gisella; Bergh, Jacobus J.; Petzer, Jacobus P.; Castagnoli, Neal (Elsevier, 2009)
      Based on a recent report that 1-methyl-3-phenylpyrrolyl analogues are moderately potent reversible inhibitors of the enzyme monoamine oxidase B (MAO-B), a series of structurally related N-methyl-2-phenylmaleimidyl analogues ...
    • Inhibition of monoamine oxidase by C5-substituted phthalimide analogues 

      Manley-King, Clarina I.; Bergh, Jacobus J.; Petzer, Jacobus P. (Elsevier, 2011)
      Literature reports that isatin as well as C5- and C6-substituted isatin analogues are reversible inhibitors of human monoamine oxidase (MAO) A and B. In general, C5- and C6-substitution of isatin leads to enhanced binding ...
    • Inhibition of monoamine oxidase by selected C5- and C6-substituted isatin analogues 

      Manley-King, Clarina I.; Bergh, Jacobus J.; Petzer, Jacobus P. (Elsevier, 2011)
      Previous studies have shown that (E)-5-styrylisatin and (E)-6-styrylisatin are reversible inhibitors of human monoamine oxidase (MAO) A and B. Both homologues are reported to exhibit selective binding to the MAO-B isoform ...
    • Monoamine oxidase inhibition by C4-substituted phthalonitriles 

      Manley-King, Clarina I.; Bergh, Jacobus J.; Petzer, Jacobus P. (Elsevier, 2012)
      It was recently reported that a series of C5-substituted phthalimides are remarkably potent reversible inhibitors of recombinant human monoamine oxidase (MAO) B. Modeling studies suggested that the phthalimide ring forms ...