RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11741547http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11741547http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11741547http://www.w3.org/2000/01/rdf-schema#comment"The human Rad50 protein, classified as a structural maintenance of chromosomes (SMC) family member, is complexed with Mre11 (R/M) and has important functions in at least two distinct double-strand break repair pathways. To find out what the common function of R/M in these pathways might be, we investigated its architecture. Scanning force microscopy showed that the complex architecture is distinct from the described SMC family members. R/M consisted of two highly flexible intramolecular coiled coils emanating from a central globular DNA binding domain. DNA end-bound R/M oligomers could tether linear DNA molecules. These observations suggest that a unified role for R/M in multiple aspects of DNA repair and chromosome metabolism is to provide a flexible, possibly dynamic, link between DNA ends."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00381-1"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(01)00381-1"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Wyman C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Wyman C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Kanaar R."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Kanaar R."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"van Gent D.C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"van Gent D.C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"van Noort J."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"van Noort J."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Dekker C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"Dekker C."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"de Jager M."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/author"de Jager M."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/pages"1129-1135"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/pages"1129-1135"xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/title"Human Rad50/Mre11 is a flexible complex that can tether DNA ends."xsd:string
http://purl.uniprot.org/citations/11741547http://purl.uniprot.org/core/title"Human Rad50/Mre11 is a flexible complex that can tether DNA ends."xsd:string