| pubmed-article:10877824 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C1332731 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C1705561 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C0012888 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C0058594 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C1332732 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C1422411 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C1825299 | lld:lifeskim |
| pubmed-article:10877824 | lifeskim:mentions | umls-concept:C2003905 | lld:lifeskim |
| pubmed-article:10877824 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:10877824 | pubmed:dateCreated | 2000-9-5 | lld:pubmed |
| pubmed-article:10877824 | pubmed:abstractText | p12(DOC-1) is a growth suppressor identified and isolated from normal keratinocytes. Ectopic expression of p12(DOC-1) in squamous carcinoma cells led to the reversion of in vitro transformation phenotypes including anchorage independence, doubling time, and morphology. Here we report that p12(DOC-1) associates with DNA polymerase alpha/primase (pol-alpha:primase) in vitro and in cells. The pol-alpha:primase binding domain in p12(DOC-1) is mapped to the amino-terminal six amino acid (MSYKPN). The biological effect of p12(DOC-1) on pol-alpha:primase was examined using in vitro DNA replication assays. Using the SV40 DNA replication assay, p12(DOC-1) suppresses DNA replication, leveling at approximately 50%. Similar results were obtained using the M13 single-stranded DNA synthesis assay. Analysis of the DNA replication products revealed that p12(DOC-1) affects the initiation step, not the elongation phase. The p12(DOC-1) suppression of DNA replication is likely to be mediated either by a direct inhibitory effect on pol-alpha:primase or by its effect on cyclin-dependent kinase 2 (CDK2), a recently identified p12(DOC-1)-associated protein known to stimulate DNA replication by phosphorylating pol-alpha:primase. p12(DOC-1) suppresses CDK2-mediated phosphorylation of pol-alpha:primase. These data support a role of p12(DOC-1) as a regulator of DNA replication by direct inhibition of pol-alpha:primase or by negatively regulating the CDK2-mediated phosphorylation of pol-alpha:primase. | lld:pubmed |
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| pubmed-article:10877824 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10877824 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10877824 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10877824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10877824 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10877824 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10877824 | pubmed:issn | 0892-6638 | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:TsujiTT | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:OhyamaHH | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:ShintaniSS | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:WongD TDT | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:NagataEE | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:MatsuiAA | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:LermanMM | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:NakaharaYY | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:ToddRR | lld:pubmed |
| pubmed-article:10877824 | pubmed:author | pubmed-author:McBrideJJ | lld:pubmed |
| pubmed-article:10877824 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10877824 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:10877824 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10877824 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10877824 | pubmed:pagination | 1318-24 | lld:pubmed |
| pubmed-article:10877824 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10877824 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10877824 | pubmed:articleTitle | p12(DOC-1), a growth suppressor, associates with DNA polymerase alpha/primase. | lld:pubmed |
| pubmed-article:10877824 | pubmed:affiliation | Laboratory of Molecular Pathology, Division of Oral Pathology, and. Harvard University, School of Dental Medicine, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:10877824 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10877824 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10877824 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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