PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18029098-10 2008 Using three-dimensional computer modeling analysis, CoQ(10) was considered to interact with the geminin interaction interface on Cdt1, and was assumed to make hydrogen bonds with the residue of Arg243 of Cdt1. coenzyme Q10 52-59 chromatin licensing and DNA replication factor 1 Homo sapiens 129-133 18029098-10 2008 Using three-dimensional computer modeling analysis, CoQ(10) was considered to interact with the geminin interaction interface on Cdt1, and was assumed to make hydrogen bonds with the residue of Arg243 of Cdt1. coenzyme Q10 52-59 chromatin licensing and DNA replication factor 1 Homo sapiens 204-208 18029098-4 2008 Using this system, we found that coenzyme Q(10) (CoQ(10)) can inhibit Cdt1-geminin interaction in vitro. coenzyme Q10 49-52 chromatin licensing and DNA replication factor 1 Homo sapiens 70-74 18029098-6 2008 CoQ(10), having a longer isoprenoid chain, was the strongest inhibitor of Cdt1-geminin binding in the tested CoQs, with 50% inhibition observed at concentrations of 16.2 muM. coenzyme Q10 0-3 chromatin licensing and DNA replication factor 1 Homo sapiens 74-78 18029098-6 2008 CoQ(10), having a longer isoprenoid chain, was the strongest inhibitor of Cdt1-geminin binding in the tested CoQs, with 50% inhibition observed at concentrations of 16.2 muM. coenzyme Q10 109-113 chromatin licensing and DNA replication factor 1 Homo sapiens 74-78 18029098-7 2008 Surface plasmon resonance analysis demonstrated that CoQ(10) bound selectively to Cdt1, but did not interact with geminin. coenzyme Q10 53-60 chromatin licensing and DNA replication factor 1 Homo sapiens 82-86 18029098-9 2008 These results suggested that CoQ(10) inhibits Cdt1-geminin complex formation by binding to Cdt1 and thereby could liberate Cdt1 from inhibition by geminin. coenzyme Q10 29-36 chromatin licensing and DNA replication factor 1 Homo sapiens 46-50 18029098-9 2008 These results suggested that CoQ(10) inhibits Cdt1-geminin complex formation by binding to Cdt1 and thereby could liberate Cdt1 from inhibition by geminin. coenzyme Q10 29-36 chromatin licensing and DNA replication factor 1 Homo sapiens 91-95 18029098-9 2008 These results suggested that CoQ(10) inhibits Cdt1-geminin complex formation by binding to Cdt1 and thereby could liberate Cdt1 from inhibition by geminin. coenzyme Q10 29-36 chromatin licensing and DNA replication factor 1 Homo sapiens 91-95