{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Glanzer JG"],"funding":["NCRR NIH HHS"],"pagination":["2589-95"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3399738"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(8)"],"pubmed_abstract":["The pharmacological suppression of the DNA damage response and DNA repair can increase the therapeutic indices of conventional chemotherapeutics. Replication Protein A (RPA), the major single-stranded DNA binding protein in eukaryotes, is required for DNA replication, DNA repair, DNA recombination, and DNA damage response signaling. Through the use of high-throughput screening of 1500 compounds, we have identified a small molecule inhibitor, 15-carboxy-13-isopropylatis-13-ene-17,18-dioic acid (NSC15520), that inhibited both the binding of Rad9-GST and p53-GST fusion proteins to the RPA N-terminal DNA binding domain (DBD), interactions that are essential for robust DNA damage signaling. NSC15520 competitively inhibited the binding of p53-GST peptide with an IC(50) of 10 μM. NSC15520 also in"],"journal":["Bioorganic & medicinal chemistry"],"pubmed_title":["Small molecule inhibitor of the RPA70 N-terminal protein interaction domain discovered using in silico and in vitro methods."],"pmcid":["PMC3399738"],"funding_grant_id":["P20 RR018759","P20-RR01875"],"pubmed_authors":["Oakley GG","Glanzer JG","Liu S"],"additional_accession":[]},"is_claimable":false,"name":"Small molecule inhibitor of the RPA70 N-terminal protein interaction domain discovered using in silico and in vitro methods.","description":"The pharmacological suppression of the DNA damage response and DNA repair can increase the therapeutic indices of conventional chemotherapeutics. Replication Protein A (RPA), the major single-stranded DNA binding protein in eukaryotes, is required for DNA replication, DNA repair, DNA recombination, and DNA damage response signaling. Through the use of high-throughput screening of 1500 compounds, we have identified a small molecule inhibitor, 15-carboxy-13-isopropylatis-13-ene-17,18-dioic acid (NSC15520), that inhibited both the binding of Rad9-GST and p53-GST fusion proteins to the RPA N-terminal DNA binding domain (DBD), interactions that are essential for robust DNA damage signaling. NSC15520 competitively inhibited the binding of p53-GST peptide with an IC(50) of 10 μM. NSC15520 also in","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Apr","modification":"2026-04-29T06:50:09.996Z","creation":"2026-04-14T03:07:03.993Z"},"accession":"S-EPMC3399738","cross_references":{"pubmed":["21459001"],"doi":["10.1016/j.bmc.2011.03.012"]}}