PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	geminin DNA replication inhibitor	Homo sapiens	75-82	
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	geminin DNA replication inhibitor	Homo sapiens	79-86	
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	geminin DNA replication inhibitor	Homo sapiens	79-86	
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	geminin DNA replication inhibitor	Homo sapiens	51-58	
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	geminin DNA replication inhibitor	Homo sapiens	147-154	
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	geminin DNA replication inhibitor	Homo sapiens	96-103