Browsing Research Output by Subject "Competitive inhibition"

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 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 ...

    • Inhibition of monoamine oxidase by selected C6-substituted chromone derivatives 

      Legoabe, Lesetja J.; Petzer, Anél; Petzer, Jacobus P. (Elsevier, 2012)
      Chromone has been reported to be a useful scaffold for the design of monoamine oxidase (MAO) inhibitors. In an attempt to discover highly potent MAO inhibitors and to contribute to the known structureeactivity relationships ...

    • Structure-activity relationships in the inhibition of monoamine oxidase B by 1-methyl-3-phenylpyrroles 

      Ogunrombi, Modupe O.; Malan, Sarel F.; Terre'Blanche, Gisella; Bergh, Jacobus J.; Petzer, Jacobus P. (Elsevier, 2008)
      1-Methyl-3-phenyl-3-pyrrolines are structural analogues of the neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and like MPTP are selective substrates of monoamine oxidase B (MAO-B). As part of an ongoing ...