pubmed-article:1698613 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1698613 | lifeskim:mentions | umls-concept:C0012888 | lld:lifeskim |
pubmed-article:1698613 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:1698613 | lifeskim:mentions | umls-concept:C0038973 | lld:lifeskim |
pubmed-article:1698613 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:1698613 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:1698613 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:1698613 | pubmed:dateCreated | 1990-11-15 | lld:pubmed |
pubmed-article:1698613 | pubmed:abstractText | Purified SV40 large T antigen and purified DNA polymerase alpha-primase form a complex detectable by ELISA and by a modified immunoblotting technique. The interaction is specific for the large catalytic subunit of polymerase alpha. The amino terminal 83 amino acids of T antigen are both necessary and sufficient for binding to the polymerase. However, antibody epitopes located in the carboxy terminal ATPase domain of T antigen are masked in the polymerase-T antigen complex, and complex formation is inhibited by an antibody directed against the carboxy terminus of T antigen, suggesting that this region of T antigen, though not required for binding, is in close proximity to the bound polymerase. The affinity of human DNA polymerase alpha for T antigen is approximately 10-fold greater than that of polymerase alpha from calf thymus, consistent with the interpretation that polymerase alpha is at least in part responsible for the primate-specific replication of SV40 DNA in vivo and in vitro. The results suggest that specific protein-protein interaction between DNA polymerase alpha and T antigen plays an important role in viral DNA replication. | lld:pubmed |
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pubmed-article:1698613 | pubmed:language | eng | lld:pubmed |
pubmed-article:1698613 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1698613 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1698613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1698613 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1698613 | pubmed:month | Oct | lld:pubmed |
pubmed-article:1698613 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:1698613 | pubmed:author | pubmed-author:FanningEE | lld:pubmed |
pubmed-article:1698613 | pubmed:author | pubmed-author:DornreiterII | lld:pubmed |
pubmed-article:1698613 | pubmed:author | pubmed-author:HöslHH | lld:pubmed |
pubmed-article:1698613 | pubmed:author | pubmed-author:ArthurA KAK | lld:pubmed |
pubmed-article:1698613 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1698613 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:1698613 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1698613 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1698613 | pubmed:pagination | 3329-36 | lld:pubmed |
pubmed-article:1698613 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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