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Coumarin versus Chromone Monoamine Oxidase B Inhibitors: Quo Vadis?

dc.contributor.authorFonseca A.
dc.contributor.authorReis J.
dc.contributor.authorSilva T.
dc.contributor.authorMatos M.J.
dc.contributor.authorBagetta D.
dc.contributor.authorOrtuso F.
dc.contributor.authorAlcaro S.
dc.contributor.authorUriarte E.
dc.contributor.authorBorges F.
dc.date.accessioned2020-09-02T22:17:54Z
dc.date.available2020-09-02T22:17:54Z
dc.date.issued2017
dc.identifier10.1021/acs.jmedchem.7b00918
dc.identifier.citation60, 16, 7206-7212
dc.identifier.issn00222623
dc.identifier.urihttps://hdl.handle.net/20.500.12728/4497
dc.descriptionBecause of the lack of significant disease-modifying drugs for neurodegenerative disorders, a pressing need for new chemical entities endowed with IMAO-B still exists. Within this framework, and for the first time, a study was performed to compare coumarin- and chomone-3-phenylcarboxamide scaffolds. Compounds 10a and 10b were the most potent, selective, and reversible noncompetitive IMAO-B. The benzopyrone sp2 oxygen atom was found to be position independent and a productive contributor for the ligand-enzyme complex stability. © 2017 American Chemical Society.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.titleCoumarin versus Chromone Monoamine Oxidase B Inhibitors: Quo Vadis?
dc.typeArticle


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