{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sterner JM"],"funding":["NCI NIH HHS"],"pagination":["2748-57"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC110654"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(5)"],"pubmed_abstract":["A yeast two-hybrid screen was employed to identify human proteins that specifically bind the amino-terminal 400 amino acids of the retinoblastoma (Rb) protein. Two independent cDNAs resulting from this screen were found to encode the carboxy-terminal 137 amino acids of MCM7, a member of a family of proteins that comprise replication licensing factor. Full-length Rb and MCM7 form protein complexes in vitro, and the amino termini of two Rb-related proteins, p107 and p130, also bind MCM7. Protein complexes between Rb and MCM7 were also detected in anti-Rb immunoprecipitates prepared from human cells. The amino-termini of Rb and p130 strongly inhibited DNA replication in an MCM7-dependent fashion in a Xenopus in vitro DNA replication assay system. These data provide the first evidence that Rb "],"journal":["Molecular and cellular biology"],"pubmed_title":["Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7."],"pmcid":["PMC110654"],"funding_grant_id":["CA53248"],"pubmed_authors":["Sterner JM","Dew-Knight S","Horowitz JM","Musahl C","Kornbluth S"],"additional_accession":[]},"is_claimable":false,"name":"Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7.","description":"A yeast two-hybrid screen was employed to identify human proteins that specifically bind the amino-terminal 400 amino acids of the retinoblastoma (Rb) protein. Two independent cDNAs resulting from this screen were found to encode the carboxy-terminal 137 amino acids of MCM7, a member of a family of proteins that comprise replication licensing factor. Full-length Rb and MCM7 form protein complexes in vitro, and the amino termini of two Rb-related proteins, p107 and p130, also bind MCM7. Protein complexes between Rb and MCM7 were also detected in anti-Rb immunoprecipitates prepared from human cells. The amino-termini of Rb and p130 strongly inhibited DNA replication in an MCM7-dependent fashion in a Xenopus in vitro DNA replication assay system. These data provide the first evidence that Rb ","dates":{"release":"1998-01-01T00:00:00Z","publication":"1998 May","modification":"2025-04-05T07:08:43.751Z","creation":"2019-03-27T00:17:01Z"},"accession":"S-EPMC110654","cross_references":{"pubmed":["9566894"],"doi":["10.1128/MCB.18.5.2748"]}}