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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/118656
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dc.contributor.authorZwick, V.-
dc.contributor.authorChatzivasileiou, A.-O.-
dc.contributor.authorDeschamps, N.-
dc.contributor.authorRoussaki, M.-
dc.contributor.authorSimões-Pires, C.A.-
dc.contributor.authorNurisso, A.-
dc.contributor.authorDenis, I.-
dc.contributor.authorBlanquart, C.-
dc.contributor.authorMartinet, N.-
dc.contributor.authorCarrupt, P.-A.-
dc.contributor.authorDetsi, A.-
dc.contributor.authorCuendet, M.-
dc.date.issued2014-
dc.identifier.citationBioorganic and Medicinal Chemistry Letters, 2014; 24(23):5497-5501-
dc.identifier.issn0960-894X-
dc.identifier.issn1464-3405-
dc.identifier.urihttp://hdl.handle.net/2440/118656-
dc.description.abstractIn this study, a total of 22 flavonoids were tested for their HDAC inhibitory activity using fluorimetric and BRET-based assays. Four aurones were found to be active in both assays and showed IC50 values below 20 μM in the enzymatic assay. Molecular modelling revealed that the presence of hydroxyl groups was responsible for good compound orientation within the isoenzyme catalytic site and zinc chelation.-
dc.description.statementofresponsibilityVincent Zwick, Alkiviadis-Orfefs Chatzivasileiou, Nathalie Deschamps, Marina Roussaki, Claudia A. Simões-Pires ... Iza Denis ... et al.-
dc.language.isoen-
dc.publisherElsevier-
dc.rights© 2014 Elsevier Ltd. All rights reserved.-
dc.source.urihttp://dx.doi.org/10.1016/j.bmcl.2014.10.019-
dc.subjectHistone deacetylase; structure activity relationship; docking; aurone-
dc.titleAurones as histone deacetylase inhibitors: identification of key features-
dc.typeJournal article-
dc.identifier.doi10.1016/j.bmcl.2014.10.019-
pubs.publication-statusPublished-
dc.identifier.orcidDenis, I. [0000-0002-2882-4306]-
Appears in Collections:Aurora harvest 4
Medicine publications

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