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Browsing Research Output by Author "Petzer, Anél"

Boloka/Manakin Repository

Browsing Research Output by Author "Petzer, Anél"

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  • Van der Walt, Mietha; Terre’Blanche, Gisella; Petzer, Anél; Lourens, Anna C. U.; Petzer, Jacobus P. (ELSEVIER, 2013)
    The adenosine A2A receptor is considered to be an important target for the development of new therapies for Parkinson’s disease. Several antagonists of the A2A receptor have entered clinical trials for this purpose and ...
  • Meiring, Letitia; Petzer, Jacobus Petrus; Petzer, Anél (ELSEVIER, 2013)
    In the present study, a series of 3,4-dihydro-2(1H)-quinolinone derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The 3,4-dihydro-2(1H)- quinolinone derivatives ...
  • Bergh, Jacobus Johannes; Mentz, Wayne; Mostert, Samantha; Petzer, Jacobus Petrus; Petzer, Anél (Elsevier, 2012)
    In a previous study we have investigated the monoamine oxidase (MAO) inhibitory properties of a series of 8-sulfanylcaffeine analogues. Among the compounds studied, 8-[(phenylethyl)sulfanyl]caffeine (IC50 = 0.223 lM) was ...
  • Bergh, Jacobus Johannes; Okaecwe, Thokozile Audrey Dorcas; Petzer, Jacobus Petrus; Swanepoel, Abraham Johannes; Petzer, Anél (Elsevier, 2012)
    A recent study has reported that a series of 8-benzyloxycaffeines are potent and reversible inhibitors of both human monoamine oxidase (MAO) isoforms, MAO-A and -B. In an attempt to discover additional caffeine derivatives ...
  • Legoabe, Lesetja Jan; Petzer, Jacobus Petrus; Kruger, Johann; Petzer, Anél; Bergh, Jacobus J. (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 ...
  • Bergh, Jacobus Johannes; Kruger, Johann; Legoabe, Lesetja Jan; Petzer, Jacobus Petrus; Petzer, Anél (Elsevier, 2011)
    A series of anilide derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The most potent inhibitors among the derivatives that were initially evaluated were ...
  • Petzer, Jacobus Petrus; Petzer, Anél; Terre'Blanche, Gisella; Van der Walt, Mietha Magdalena (Elsevier, 2012)
    Monoamine oxidase (MAO) plays an essential role in the catabolism of neurotransmitter amines. The two isoforms of this enzyme, MAO-A and -B, are considered to be drug targets for the therapy of depression and neurodegenerative ...
  • Legoabe, Lesetja Jan; Petzer, Jacobus Petrus; Petzer, Anél (Elsevier, 2012)
    A series of C7-substituted chromone (1-benzopyran-4-one) derivatives were synthesized and evaluated as inhibitors of recombinant human monoamine oxidase (MAO) A and B. The chromones are structurally related to a series of ...
  • Legoabe, Lesetja Jan; Petzer, Jacobus Petrus; Petzer, Anél (Elsevier, 2012)
    A previous study has shown that a series of C6-benzyloxy substituted chromones exhibit high binding affinities for human monoamine oxidase (MAO) B. In an attempt to discover additional chromones with potent and selective ...
  • Robinson, Sarel J.; Petzer, Jacobus P.; Petzer, Anél; Bergh, Jacobus J.; Lourens, Anna C. U. (ELSEVIER, 2013)
    The validity of the chalcone scaffold for the design of inhibitors of monoamine oxidase has previously been illustrated. In a systematic attempt to investigate the effect of heterocyclic substitution on the monoamine ...
  • Lourens, Anna Catharina; Petzer, Jacobus Petrus; Van der Walt, Mietha Magdalena; Terre'Blanche, Gisella; Petzer, Anél (Elsevier, 2012)
    It has recently been reported that nitrile containing compounds frequently act as potent monoamine oxidase B (MAO-B) inhibitors. Modelling studies suggest that this high potency inhibition may rely, at least in part, on ...
  • Bergh, Jacobus Johannes; Booysen, Hermanus Perold; Moraal, Christina Maria; Petzer, Jacobus Petrus; Petzer, Anél; Terre'Blanche, Gisella (Elsevier, 2011)
    In a recent study it was shown that 8-benzyloxycaffeine analogues act as potent reversible inhibitors of human monoamine oxidase (MAO) A and B. Although the benzyloxy side chain appears to be particularly favorable for ...

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