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http://purl.uniprot.org/citations/37171222http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37171222http://www.w3.org/2000/01/rdf-schema#comment"Death-associated protein kinase 1 (DAPK1), a Ca2+/calmodulin-regulated serine/threonine kinase, regulates cell apoptosis and autophagy and has been implicated in the pathogenesis of Alzheimer's disease (AD). Targeting DAPK1 may be a promising approach for treating AD. In our previous study, we found that a natural polyphenol, resveratrol (1), is a moderate DAPK1 inhibitor. In the present study, we investigated the interactions between natural and synthetic derivatives of 1 and DAPK1. Binding assays including intrinsic fluorescence quenching, protein thermal shift and isothermal titration calorimetry indicated that oxyresveratrol (3), a hydroxylated derivative, and pinostilbene (5), a methoxylated derivative, bind to DAPK1 with comparable affinity to 1. The enzymatic assay showed that 3 more effectively inhibits the intrinsic ATPase activity of DAPK1 compared with 1. Crystallographic analysis revealed that the binding modes of the methoxylated derivatives were different from those of 1 and 3, resulting in a unique interaction. Our results suggest that 3 may be helpful in treating AD and provide a clue for the development of promising DAPK1 inhibitors."xsd:string
http://purl.uniprot.org/citations/37171222http://purl.org/dc/terms/identifier"doi:10.1111/febs.16817"xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/author"Yokoyama T."xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/author"Kusaka K."xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/name"FEBS J"xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/pages"4465-4479"xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/title"Characterization of the molecular interactions between resveratrol derivatives and death-associated protein kinase 1."xsd:string
http://purl.uniprot.org/citations/37171222http://purl.uniprot.org/core/volume"290"xsd:string
http://purl.uniprot.org/citations/37171222http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37171222
http://purl.uniprot.org/citations/37171222http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37171222
http://purl.uniprot.org/uniprot/#_P53355-mappedCitation-37171222http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37171222
http://purl.uniprot.org/uniprot/P53355http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/37171222