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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2007-8-13
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pubmed:abstractText |
Replication protein A (RPA) is a stable heterotrimeric complex consisting of p70, p32 and p14 subunits. The protein plays a crucial role in SV40 minichromosome replication. Peptides of p70 representing interaction sites for the smaller two subunits, DNA as well as the viral initiator protein large T-antigen (Tag) and the cellular DNA polymerase alpha-primase (Pol) all interfered with the replication process indicating the importance of the different p70 activities in this process. Inhibition by the peptide disrupting protein-protein interactions was observed only during the pre-initiation stage prior to primer synthesis, suggesting the formation of a stable initiation complex between RPA, Tag and Pol at the primer end.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-10233951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-10449415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-10747950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-11139606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-11157767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-11479296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-11927569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-1311258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-14960720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-15279788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-15793585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-16935876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-1885001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-2159011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-2406247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-2550804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-2841119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-2994044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-7876222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8196638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8380896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8454588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8611550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8804316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-8990123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-9214288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-9242902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17673209-9461578
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral, Tumor,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA polymerase alpha-primase,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein A,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3973-8
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17673209-Antigens, Viral, Tumor,
pubmed-meshheading:17673209-Cell Line,
pubmed-meshheading:17673209-DNA, Viral,
pubmed-meshheading:17673209-DNA Polymerase I,
pubmed-meshheading:17673209-DNA Primase,
pubmed-meshheading:17673209-DNA Primers,
pubmed-meshheading:17673209-DNA Replication,
pubmed-meshheading:17673209-Humans,
pubmed-meshheading:17673209-Multiprotein Complexes,
pubmed-meshheading:17673209-Protein Binding,
pubmed-meshheading:17673209-Protein Subunits,
pubmed-meshheading:17673209-Replication Protein A,
pubmed-meshheading:17673209-Simian virus 40,
pubmed-meshheading:17673209-Viral Proteins,
pubmed-meshheading:17673209-Virus Replication
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pubmed:year |
2007
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pubmed:articleTitle |
Different activities of the largest subunit of replication protein A cooperate during SV40 DNA replication.
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pubmed:affiliation |
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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