| pubmed-article:16474403 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16474403 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:16474403 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:16474403 | lifeskim:mentions | umls-concept:C1819424 | lld:lifeskim |
| pubmed-article:16474403 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16474403 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16474403 | pubmed:dateCreated | 2006-3-6 | lld:pubmed |
| pubmed-article:16474403 | pubmed:abstractText | Helicases unwind dsDNA during replication, repair and recombination in an ATP-dependent reaction. The mechanism for helicase activity can be studied using oligonucleotide substrates to measure formation of single-stranded (ss) DNA from double-stranded (ds) DNA. This assay provides an 'all-or-nothing' readout because partially unwound intermediates are not detected. We have determined conditions under which an intermediate in the reaction cycle of Dda helicase can be detected by trapping a partially unwound substrate. The appearance of this intermediate supports a model in which each ssDNA product interacts with the helicase after unwinding has occurred. Kinetic analysis indicates that the intermediate appears during a slow step in the reaction cycle that is flanked by faster steps for unwinding. These observations demonstrate a complex mechanism containing nonuniform steps for a monomeric helicase. The potential biological significance of such a mechanism is discussed. | lld:pubmed |
| pubmed-article:16474403 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16474403 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16474403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16474403 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16474403 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16474403 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:16474403 | pubmed:author | pubmed-author:RaneyKevin... | lld:pubmed |
| pubmed-article:16474403 | pubmed:author | pubmed-author:EoffRobert... | lld:pubmed |
| pubmed-article:16474403 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16474403 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:16474403 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16474403 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16474403 | pubmed:pagination | 242-9 | lld:pubmed |
| pubmed-article:16474403 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:meshHeading | pubmed-meshheading:16474403... | lld:pubmed |
| pubmed-article:16474403 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16474403 | pubmed:articleTitle | Intermediates revealed in the kinetic mechanism for DNA unwinding by a monomeric helicase. | lld:pubmed |
| pubmed-article:16474403 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham St. Slot 516, Little Rock, Arkansas 72205, USA. | lld:pubmed |
| pubmed-article:16474403 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16474403 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16474403 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:1258784 | entrezgene:pubmed | pubmed-article:16474403 | lld:entrezgene |
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