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http://purl.uniprot.org/citations/23393192http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23393192http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23393192http://www.w3.org/2000/01/rdf-schema#comment"DNA repair helicases function in the cell to separate DNA duplexes or remodel nucleoprotein complexes. These functions are influenced by sensing and signaling; the cellular pool of a DNA helicase may contain subpopulations of enzymes carrying different post-translational modifications and performing distinct biochemical functions. Here, we report a novel experimental strategy, single-molecule sorting, which overcomes difficulties associated with comprehensive analysis of heterologously modified pool of proteins. This methodology was applied to visualize human DNA helicase F-box-containing DNA helicase (FBH1) acting on the DNA structures resembling a stalled or collapsed replication fork and its interactions with RAD51 nucleoprotein filament. Individual helicase molecules isolated from human cells with their native post-translational modifications were analyzed using total internal reflection fluorescence microscopy. Separation of the activity trajectories originated from ubiquitylated and non-ubiquitylated FBH1 molecules revealed that ubiquitylation affects FBH1 interaction with the RAD51 nucleoprotein filament, but not its translocase and helicase activities."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkt056"xsd:string
http://purl.uniprot.org/citations/23393192http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkt056"xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Spies M."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Spies M."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Seo Y.S."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Seo Y.S."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Hoang T."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Hoang T."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Chen L.F."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Chen L.F."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Masuda-Ozawa T."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/author"Masuda-Ozawa T."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/name"Nucleic Acids Res."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/pages"3576-3587"xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/pages"3576-3587"xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/title"Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/title"Single-molecule sorting reveals how ubiquitylation affects substrate recognition and activities of FBH1 helicase."xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/23393192http://purl.uniprot.org/core/volume"41"xsd:string