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Pharmacokinetics of monoamine oxidase B inhibitors in Parkinson’s disease: current status

Expert Opinion on Drug Metabolism & Toxicology, 2019
Introduction: Brain function depends considerably on the neurotransmission of biogenic monoamines. Their metabolism employs monoamine oxidase-B in neuronal and glial cells. Inhibition of monoamine oxidase-B elevates biogenic amine levels.
T. Müller, Jan-Dominique Möhr
semanticscholar   +1 more source

Monoamine oxidase: To B or not to B?

Life Sciences, 1982
That the enzyme, monoamine oxidase (E.C. 1.4.3.4. amine: O2 oxidoreductase, MAO) exists in multiple forms was first suggested by Johnston (1) who studied the effects of the irreversible inhibitor clorgyline on MAO. It has been proposed that MAO can be classified into two types, A and B, according to their inhibitor sensitivity and substrate specificity.
openaire   +2 more sources

Monoamine oxidase A and B inhibitors

Expert Opinion on Therapeutic Patents, 1998
This patent update relates to monoamine oxidase inhibitors, covers the patent activity in this field for the last 3 - 5 years and focuses on the most relevant filings. Patents are classified according to the type of MAO inhibition: selective MAO-A and MAO-B inhibitors, and mixed and reversible MAO-A and MAO-B inhibitors.
Samir Jegham, Pascal George
openaire   +1 more source

Potent and highly selective dual‐targeting monoamine oxidase‐B inhibitors: Fluorinated chalcones of morpholine versus imidazole

Archiv der Pharmazie, 2019
Two series of fluorinated chalcones containing morpholine and imidazole‐based compounds (f1–f8) were synthesized and evaluated for recombinant human monoamine oxidase (MAO)‐A and ‐B as well as acetylcholinesterase inhibitory activities.
B. Mathew   +11 more
semanticscholar   +1 more source

Antiapoptotic Actions of Monoamine Oxidase B Inhibitors

1997
Publisher Summary R-Deprenyl is an irreversible inhibitor of monoamine oxidase (MAO) with selectivity for MAO-B and, believed to influence neuronal survival by preventing necrosis induced by oxidative radicals resulting from monoamine metabolism. There is accumulating evidence that R-deprenyl and certain other MAO-B inhibitors can prevent apoptotic ...
I A, Paterson, W G, Tatton
openaire   +2 more sources

Titration of human brain type-B monoamine oxidase

Neurochemical Research, 1980
The interaction of the substrate-selective irreversible inhibitor J-508 [N-methyl-N-propargyl-(1-indanyl)-ammonium hydrochloride] with the B form of human brain monoamine oxidase has been investigated, and the conditions necessary for this inhibitor to "titrate" the concentration of this enzyme form determined.
C J, Fowler   +3 more
openaire   +2 more sources

Platelet monoamine oxidase B: Use and misuse

Experientia, 1988
The human platelet in addition to having serotonin (5-HT) receptors, uptake carriers (receptor) and transmitter storage vesicles, primarily possesses mitochondrial monoamine oxidase (MAO) type B. Similar to the major form of MAO in the human brain, this enzyme actively oxidizes A-B and B substrates (tyramine, dopamine, phenylethylamine) as well as the ...
openaire   +2 more sources

Hydrogen tunneling in the flavoenzyme monoamine oxidase B

Biochemistry, 1994
Competitive kH/kT and kD/kT kinetic isotope effects on p-methoxybenzylamine oxidation by the 8 alpha-S-cysteinyl flavin adenine dinucleotide (FAD)-dependent enzyme monoamine oxidase B (MAO-B) have been measured as a function of temperature. At pH 7.5, exponents relating observed kH/kT and kD/kT isotope effects indicate the presence of a temperature ...
T, Jonsson, D E, Edmondson, J P, Klinman
openaire   +2 more sources

Molecular docking of inhibitors into monoamine oxidase B

Biochemical and Biophysical Research Communications, 2007
Monoamine oxidase B (MAO-B) functions in the deamination of monoamines, including dopamine and norepinephrine. The search for MAO-B inhibitors increased following the discovery that the enzyme may be responsible for generating neurotoxins from various endogenous or exogenous compounds.
William T, Harkcom, David R, Bevan
openaire   +2 more sources

A novel and selective monoamine oxidase B substrate

Bioorganic & Medicinal Chemistry, 2005
Cyclic five- and six-membered tertiary allylamines constitute a unique class of monoamine oxidase substrates that undergo a net two-electron alpha-carbon oxidation to form the cyclic, conjugated eniminium metabolites. The corresponding saturated pyrrolidinyl and piperidinyl systems are not substrates for this flavoenzyme system.
John M, Rimoldi   +5 more
openaire   +2 more sources

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