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http://purl.uniprot.org/citations/21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21496642http://www.w3.org/2000/01/rdf-schema#comment"Human exonuclease 1 (hExo1) plays important roles in DNA repair and recombination processes that maintain genomic integrity. It is a member of the 5' structure-specific nuclease family of exonucleases and endonucleases that includes FEN-1, XPG, and GEN1. We present structures of hExo1 in complex with a DNA substrate, followed by mutagenesis studies, and propose a common mechanism by which this nuclease family recognizes and processes diverse DNA structures. hExo1 induces a sharp bend in the DNA at nicks or gaps. Frayed 5' ends of nicked duplexes resemble flap junctions, unifying the mechanisms of endo- and exonucleolytic processing. Conformational control of a mobile region in the catalytic site suggests a mechanism for allosteric regulation by binding to protein partners. The relative arrangement of substrate binding sites in these enzymes provides an elegant solution to a complex geometrical puzzle of substrate recognition and processing."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2011.03.005"xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Orans J."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Hellinga H.W."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Beese L.S."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Modrich P."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Hast M.A."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"Iyer R.R."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/author"McSweeney E.A."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/pages"212-223"xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/title"Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family."xsd:string
http://purl.uniprot.org/citations/21496642http://purl.uniprot.org/core/volume"145"xsd:string
http://purl.uniprot.org/citations/21496642http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21496642
http://purl.uniprot.org/citations/21496642http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21496642
http://purl.uniprot.org/uniprot/#_P52701-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P54278-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_A8K5H6-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P15927-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P12004-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P20585-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P27694-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642
http://purl.uniprot.org/uniprot/#_P35244-mappedCitation-21496642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21496642