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	
18029098-4	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	
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