| pubmed-article:9129153 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0079183 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9129153 | lifeskim:mentions | umls-concept:C0762677 | lld:lifeskim |
| pubmed-article:9129153 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:9129153 | pubmed:dateCreated | 1997-5-13 | lld:pubmed |
| pubmed-article:9129153 | pubmed:abstractText | DNA polymerase alpha-primase is the only known eukaryotic enzyme that can start DNA replication de novo. In this study, we investigated the regulation of DNA replication by phosphorylation of DNA polymerase alpha-primase. The p180 and the p68 subunits of DNA polymerase alpha-primase were phosphorylated using Cyclin A-, B- and E- dependent kinases. This phosphorylation did not influence its DNA polymerase activity on activated DNA, but slightly stimulated primase activity using poly(dT) single-stranded DNA (ssDNA) without changing the product length of primers. In contrast, site-specific initiation of replication on plasmid DNA containing the SV40 origin is affected: Cyclin A-Cdk2 and Cyclin A-Cdc2 inhibited initiation of SV40 DNA replication in vitro, Cyclin B-Cdc2 had no effect and Cyclin E-Cdk2 stimulated the initiation reaction. DNA polymerase alpha-primase that was pre-phosphorylated by Cyclin A-Cdk2 was completely unable to initiate the SV40 DNA replication in vitro; Cyclin B-Cdc2-phosphorylated enzyme was moderately inhibited, while Cyclin E-Cdk2-treated DNA polymerase alpha-primase remained fully active in the initiation reaction. | lld:pubmed |
| pubmed-article:9129153 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9129153 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9129153 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9129153 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9129153 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9129153 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9129153 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9129153 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9129153 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9129153 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9129153 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:9129153 | pubmed:author | pubmed-author:FanningEE | lld:pubmed |
| pubmed-article:9129153 | pubmed:author | pubmed-author:NasheuerH PHP | lld:pubmed |
| pubmed-article:9129153 | pubmed:author | pubmed-author:Voitenleitner... | lld:pubmed |
| pubmed-article:9129153 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9129153 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9129153 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:9129153 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9129153 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9129153 | pubmed:pagination | 1611-5 | lld:pubmed |
| pubmed-article:9129153 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9129153 | pubmed:meshHeading | pubmed-meshheading:9129153-... | lld:pubmed |
| pubmed-article:9129153 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9129153 | pubmed:articleTitle | Phosphorylation of DNA polymerase alpha-primase by cyclin A-dependent kinases regulates initiation of DNA replication in vitro. | lld:pubmed |
| pubmed-article:9129153 | pubmed:affiliation | Institut für Biochemie, LMU München, Germany. | lld:pubmed |
| pubmed-article:9129153 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9129153 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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