| http://purl.uniprot.org/citations/15653697 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15653697 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15653697 | http://www.w3.org/2000/01/rdf-schema#comment | "The presence of DNA-unwinding elements (DUEs) at eukaryotic replicators has raised the question of whether these elements contribute to origin activity by their intrinsic helical instability, as protein-binding sites, or both. We used the human c-myc DUE as bait in a yeast one-hybrid screen and identified a DUE-binding protein, designated DUE-B, with a predicted mass of 23.4 kDa. Based on homology to yeast proteins, DUE-B was previously classified as an aminoacyl-tRNA synthetase; however, the human protein is approximately 60 amino acids longer than its orthologs in yeast and worms and is primarily nuclear. In vivo, chromatin-bound DUE-B localized to the c-myc DUE region. DUE-B levels were constant during the cell cycle, although the protein was preferentially phosphorylated in cells arrested early in S phase. Inhibition of DUE-B protein expression slowed HeLa cell cycle progression from G1 to S phase and induced cell death. DUE-B extracted from HeLa cells or expressed from baculovirus migrated as a dimer during gel filtration and co-purified with ATPase activity. In contrast to endogenous DUE-B, baculovirus-expressed DUE-B efficiently formed high molecular mass complexes in Xenopus egg and HeLa extracts. In Xenopus extracts, baculovirus-expressed DUE-B inhibited chromatin replication and replication protein A loading in the presence of endogenous DUE-B, suggesting that differential covalent modification of these proteins can alter their effect on replication. Recombinant DUE-B expressed in HeLa cells restored replication activity to egg extracts immunodepleted with anti-DUE-B antibody, suggesting that DUE-B plays an important role in replication in vivo."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m404754200"xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m404754200"xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Ghosh M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Ghosh M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Casper J.M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Casper J.M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Kemp M.G."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Kemp M.G."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Leffak M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Leffak M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Randall G.M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Randall G.M."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Vaillant A."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/author | "Vaillant A."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/pages | "13071-13083"xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/pages | "13071-13083"xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/title | "The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro."xsd:string |
| http://purl.uniprot.org/citations/15653697 | http://purl.uniprot.org/core/title | "The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro."xsd:string |