Localization of the large subunit of replication factor C near the 5? end of DNA primers (original) (raw)
Subunits of human replication protein A are crosslinked by photoreactive primers synthesized by DNA polymerases
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Nucleic Acids Research, 1998
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ø29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates
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Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains
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Human Replication Protein A. THE C-TERMINAL RPA70 AND THE CENTRAL RPA32 DOMAINS ARE INVOLVED IN THE INTERACTIONS WITH THE 3'-END OF A PRIMER-TEMPLATE DNA
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Journal of Biological Chemistry, 2003
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Initiation of phi 29 DNA replication occurs at the second 3' nucleotide of the linear template: a sliding-back mechanism for protein-primed DNA replication
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Proceedings of the National Academy of Sciences, 1992
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The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA
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DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C
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Photoreactive DNA as a Tool to study Replication Protein A Functioning in DNA Replication and Repair
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29 DNA Polymerase Residue Leu384, Highly Conserved in Motif B of Eukaryotic Type DNA Replicases, Is Involved in Nucleotide Insertion Fidelity
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