pubmed-article:10625495 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0012935 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0678536 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0456389 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
pubmed-article:10625495 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
pubmed-article:10625495 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10625495 | pubmed:dateCreated | 2000-1-28 | lld:pubmed |
pubmed-article:10625495 | pubmed:abstractText | Using a fluorescent sensor for inorganic phosphate, the kinetics of ATP hydrolysis by PcrA helicase were measured in the presence of saturating concentrations of oligonucleotides of various lengths. There is a rapid phase of inorganic phosphate release that is equivalent to several turnovers of the ATPase, followed by slower steady-state ATP hydrolysis. The magnitude of the rapid phase is governed by the length of single-stranded DNA, while the slow phase is independent of its length. A kinetic model is presented in which the rapid phase is associated with translocation along single-stranded DNA, after the PcrA binds randomly along the DNA. There is a linear relationship between the length of single-stranded DNA and both the duration and amplitude of the rapid phase. These data suggest that the translocation activity occurs at 50 bases/s in unidirectional single-base steps, each requiring the hydrolysis of 1 ATP molecule. | lld:pubmed |
pubmed-article:10625495 | pubmed:language | eng | lld:pubmed |
pubmed-article:10625495 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10625495 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10625495 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10625495 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10625495 | pubmed:month | Jan | lld:pubmed |
pubmed-article:10625495 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:10625495 | pubmed:author | pubmed-author:WebbM RMR | lld:pubmed |
pubmed-article:10625495 | pubmed:author | pubmed-author:WigleyD BDB | lld:pubmed |
pubmed-article:10625495 | pubmed:author | pubmed-author:DillinghamM... | lld:pubmed |
pubmed-article:10625495 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10625495 | pubmed:day | 11 | lld:pubmed |
pubmed-article:10625495 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:10625495 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10625495 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10625495 | pubmed:pagination | 205-12 | lld:pubmed |
pubmed-article:10625495 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10625495 | pubmed:meshHeading | pubmed-meshheading:10625495... | lld:pubmed |
pubmed-article:10625495 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10625495 | pubmed:articleTitle | Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. | lld:pubmed |
pubmed-article:10625495 | pubmed:affiliation | Sir William Dunn School of Pathology, University of Oxford, United Kingdom. | lld:pubmed |
pubmed-article:10625495 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10625495 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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