RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18922789http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18922789http://www.w3.org/2000/01/rdf-schema#comment"The Saccharomyces cerevisiae Mec1-Ddc2 protein kinase (human ATR-ATRIP) initiates a signal transduction pathway in response to DNA damage and replication stress to mediate cell cycle arrest. The yeast DNA damage checkpoint clamp Ddc1-Mec3-Rad17 (human Rad9-Hus1-Rad1: 9-1-1) is loaded around effector DNA and thereby activates Mec1 kinase. Dpb11 (Schizosaccharomyces pombe Cut5/Rad4 or human TopBP1) is an essential protein required for the initiation of DNA replication and has a role in checkpoint activation. In this study, we demonstrate that Dpb11 directly activates the Mec1 kinase in phosphorylating the downstream effector kinase Rad53 (human Chk1/2) and DNA bound RPA. However, DNA was not required for Dpb11 to function as an activator. Dpb11 and yeast 9-1-1 independently activate Mec1, but substantial synergism in activation was observed when both activators were present. Our studies suggest that Dpb11 and 9-1-1 may partially compensate for each other during yeast checkpoint function."xsd:string
http://purl.uniprot.org/citations/18922789http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m807435200"xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/author"Burgers P.M."xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/author"Navadgi-Patil V.M."xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/pages"35853-35859"xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/title"Yeast DNA replication protein Dpb11 activates the Mec1/ATR checkpoint kinase."xsd:string
http://purl.uniprot.org/citations/18922789http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18922789http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18922789
http://purl.uniprot.org/citations/18922789http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18922789
http://purl.uniprot.org/uniprot/P47027#attribution-D59EF76014CAB4F8216F72E03AB02B6Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/#_A0A8H4BTI5-mappedCitation-18922789http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/#_A0A8H4FAI8-mappedCitation-18922789http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/#_P38111-mappedCitation-18922789http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/#_P47027-mappedCitation-18922789http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/A0A8H4BTI5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/P38111http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/A0A8H4FAI8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18922789
http://purl.uniprot.org/uniprot/P47027http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18922789