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Molecular aspects of monoamine oxidase B

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PNP8887accepted11Feb2016.pdf (633.4Kb)
Date
01/08/2016
Author
Ramsay, Rona Ruth
Keywords
Monoamine oxidase B
Kinetics
Drug design
Neurotransmitter levels
Platelet
RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry
QH301 Biology
Biochemistry, Genetics and Molecular Biology(all)
Biological Psychiatry
Cellular and Molecular Neuroscience
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Abstract
Monoamine oxidases (MAO) influence the monoamine levels in brain by virtue of their role in neurotransmitter breakdown. MAO B is the predominant form in glial cells and in platelets. MAO B structure, function and kinetics are described as a background for the alterations in its activity on behavior. The need to inhibit MAO B to combat decreased brain amines continues to drive the search for new drugs. Reversible and irreversible inhibitors are now designed using data-mining, computational screening, docking and molecular dynamics. Multi-target ligands designed to combat the elevated activity of MAO B in Alzheimer’s and Parkinson’s Diseases incorporate MAO inhibition (usually irreversible) as well as iron chelation, antioxidant or neuroprotective properties. The main focus of drug design is the catalytic activity of MAO, but the imidazoline I2 site in the entrance cavity of MAO B is also a pharmacological target. Endogenous regulation of MAO B expression is discussed briefly in light of new studies measuring mRNA, protein, or activity in healthy and degenerative samples, including the effect of DNA methylation on the expression. Overall, this review focuses on examples of recent research on the molecular aspects of the expression, activity, and inhibition of MAO B.
Citation
Ramsay , R R 2016 , ' Molecular aspects of monoamine oxidase B ' , Progress in Neuro-Psychopharmacology & Biological Psychiatry , vol. 69 , pp. 81-89 . https://doi.org/10.1016/j.pnpbp.2016.02.005
Publication
Progress in Neuro-Psychopharmacology & Biological Psychiatry
Status
Peer reviewed
DOI
https://doi.org/10.1016/j.pnpbp.2016.02.005
ISSN
0278-5846
Type
Journal item
Rights
© 2016, Publisher / the Author(s). This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at www.sciencedirect.com / https://dx.doi.org/10.1016/j.pnpbp.2016.02.005
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/10312

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