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- W2080432046 endingPage "451" @default.
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- W2080432046 abstract "Replication protein A (RAP) is a eukaryotic single-stranded DNA binding protein involved in DNA replication, repair, and recombination. Recent studies indicate that RPA preferentially binds the damaged sites rather than the undamaged sites. Therefore, RPA is thought to be a member of repair factories or a sensor of lesion on DNA. To obtain further information of behavior of RPA against the oxidized lesion, we studied the binding affinity of RPA for the single-stranded DNA containing 5-formyluracil, a major lesion of thymine base yielded by the oxidation, using several synthetic oligonucleotides. The affinity of RPA for oligonucleotides was determined by gel shift assay. Results suggest that the surrounding sequence of 5-formyluracil may affect the affinity for RPA, and that the 5-formyluracil on the purine stretch but not the pyrimidine stretch increases the affinity for RPA. Results of affinity labeling experiment of RPA with the oligonucleotides containing 5-formyluracil indicate that RPA1 subunit may directly recognize and bind to the 5-formyluracil on the single-stranded DNA." @default.
- W2080432046 created "2016-06-24" @default.
- W2080432046 creator A5049681206 @default.
- W2080432046 creator A5056249214 @default.
- W2080432046 creator A5067928470 @default.
- W2080432046 date "2006-06-01" @default.
- W2080432046 modified "2023-09-27" @default.
- W2080432046 title "Recognition of Oxidized Thymine Base on the Single-Stranded DNA by Replication Protein A" @default.
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- W2080432046 doi "https://doi.org/10.1080/01457630600684138" @default.
- W2080432046 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16838837" @default.
- W2080432046 hasPublicationYear "2006" @default.
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