| pubmed-article:17032657 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C1414091 | lld:lifeskim |
| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C1254042 | lld:lifeskim |
| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C1704973 | lld:lifeskim |
| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C1979975 | lld:lifeskim |
| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:17032657 | lifeskim:mentions | umls-concept:C0069390 | lld:lifeskim |
| pubmed-article:17032657 | pubmed:issue | 50 | lld:pubmed |
| pubmed-article:17032657 | pubmed:dateCreated | 2006-12-12 | lld:pubmed |
| pubmed-article:17032657 | pubmed:abstractText | The Dna2 protein is a multifunctional enzyme with 5'-3' DNA helicase, DNA-dependent ATPase, 3' exo/endonuclease, and 5' exo/endonuclease. The enzyme is highly specific for structures containing single-stranded flaps adjacent to duplex regions. We report here two novel activities of both the yeast and human Dna2 helicase/nuclease protein: single strand annealing and ATP-independent strand exchange on short duplexes. These activities are independent of ATPase/helicase and nuclease activities in that mutations eliminating either nuclease or ATPase/helicase do not inhibit strand annealing or strand exchange. ATP inhibits strand exchange. A model rationalizing the multiple catalytic functions of Dna2 and leading to its coordination with other enzymes in processing single-stranded flaps during DNA replication and repair is presented. | lld:pubmed |
| pubmed-article:17032657 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032657 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17032657 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17032657 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17032657 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17032657 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17032657 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17032657 | pubmed:author | pubmed-author:CampbellJudit... | lld:pubmed |
| pubmed-article:17032657 | pubmed:author | pubmed-author:PolaczekPiotr... | lld:pubmed |
| pubmed-article:17032657 | pubmed:author | pubmed-author:Masuda-SasaTa... | lld:pubmed |
| pubmed-article:17032657 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17032657 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17032657 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:17032657 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17032657 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17032657 | pubmed:pagination | 38555-64 | lld:pubmed |
| pubmed-article:17032657 | pubmed:dateRevised | 2008-7-24 | lld:pubmed |
| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
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| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
| pubmed-article:17032657 | pubmed:meshHeading | pubmed-meshheading:17032657... | lld:pubmed |
| pubmed-article:17032657 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17032657 | pubmed:articleTitle | Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation. | lld:pubmed |
| pubmed-article:17032657 | pubmed:affiliation | Braun Laboratories, California Institute of Technology, Pasadena, CA 91125, USA. | lld:pubmed |
| pubmed-article:17032657 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17032657 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17032657 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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