| pubmed-article:17350265 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17350265 | lifeskim:mentions | umls-concept:C0041427 | lld:lifeskim |
| pubmed-article:17350265 | lifeskim:mentions | umls-concept:C1325592 | lld:lifeskim |
| pubmed-article:17350265 | lifeskim:mentions | umls-concept:C0012892 | lld:lifeskim |
| pubmed-article:17350265 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:17350265 | lifeskim:mentions | umls-concept:C0376706 | lld:lifeskim |
| pubmed-article:17350265 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17350265 | pubmed:dateCreated | 2007-4-9 | lld:pubmed |
| pubmed-article:17350265 | pubmed:abstractText | Chromosomal replicases are multicomponent machines that copy DNA with remarkable speed and processivity. The organization of the replisome reveals a twin DNA polymerase design ideally suited for concurrent synthesis of leading and lagging strands. Recent structural and biochemical studies of Escherichia coli and eukaryotic replication components provide intricate details of the organization and inner workings of cellular replicases. In particular, studies of sliding clamps and clamp-loader subunits elucidate the mechanisms of replisome processivity and lagging strand synthesis. These studies demonstrate close similarities between the bacterial and eukaryotic replication machineries. | lld:pubmed |
| pubmed-article:17350265 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17350265 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17350265 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17350265 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17350265 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17350265 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17350265 | pubmed:issn | 0966-842X | lld:pubmed |
| pubmed-article:17350265 | pubmed:author | pubmed-author:O'DonnellMike... | lld:pubmed |
| pubmed-article:17350265 | pubmed:author | pubmed-author:PomerantzRich... | lld:pubmed |
| pubmed-article:17350265 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17350265 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:17350265 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17350265 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17350265 | pubmed:pagination | 156-64 | lld:pubmed |
| pubmed-article:17350265 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17350265 | pubmed:meshHeading | pubmed-meshheading:17350265... | lld:pubmed |
| pubmed-article:17350265 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17350265 | pubmed:articleTitle | Replisome mechanics: insights into a twin DNA polymerase machine. | lld:pubmed |
| pubmed-article:17350265 | pubmed:affiliation | Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:17350265 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17350265 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17350265 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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