PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23864105-7	2013	Comparative studies indicate that PHTPP derivatives fit well within the ATP binding cleft in CDK2, with the core heterocyclic ring overlapping significantly with the adenine group of ATP despite a small deflection.	Adenine	166-173	cyclin dependent kinase 2	Homo sapiens	93-97	
9030780-8	1997	The purine portion of the inhibitor binds to the adenine binding pocket of cdk2.	Adenine	49-56	cyclin dependent kinase 2	Homo sapiens	75-79	
7479711-5	1995	Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP.	Adenine	20-27	cyclin dependent kinase 2	Homo sapiens	82-86	
7479711-5	1995	Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP.	Adenine	56-63	cyclin dependent kinase 2	Homo sapiens	82-86	
7479711-5	1995	Both inhibitors are adenine derivatives and bind in the adenine binding pocket of CDK2, but in an unexpected and different orientation from the adenine of the authentic ligand ATP.	Adenine	56-63	cyclin dependent kinase 2	Homo sapiens	82-86	
8610110-6	1996	The aromatic portion of the inhibitor binds to the adenine-binding pocket of CDK2, and the position of the phenyl group of the inhibitor enables the inhibitor to make contacts with the enzyme not observed in the ATP complex structure.	Adenine	51-58	cyclin dependent kinase 2	Homo sapiens	77-81	
32210718-10	2020	Western blot analysis showed that adenine reduced expression of cyclin A/D1 and cyclin-dependent kinase (CDK)2 and upregulated p53, p21, Bax, PUMA, and NOXA in HepG2 cell.	Adenine	34-41	cyclin dependent kinase 2	Homo sapiens	80-110	
28827110-2	2017	A series of novel 6-aminopurine compounds was prepared for structure-activity relationship (SAR) studies of CDK2 and CDK5 inhibitors.	Adenine	18-31	cyclin dependent kinase 2	Homo sapiens	108-112	
28827110-4	2017	Here, we report the synthesis and evaluation of novel 6-aminopurine derivatives and present molecular docking models of compound 81 with CDK2 and CDK5.	Adenine	54-67	cyclin dependent kinase 2	Homo sapiens	137-141	
11170642-0	2001	Crystal structure of human cyclin-dependent kinase 2 in complex with the adenine-derived inhibitor H717.	Adenine	73-80	cyclin dependent kinase 2	Homo sapiens	27-52	
11377199-10	2001	CONCLUSIONS: The accuracy of monomeric CDK2 as an inhibitor design template is restricted to the adenine binding site.	Adenine	97-104	cyclin dependent kinase 2	Homo sapiens	39-43	
22927831-5	2012	That plasticity obscured a requirement for Cdk2 activity in proliferation of human cells, which we uncovered by replacement of wild-type Cdk2 with a mutant version sensitized to inhibition by bulky adenine analogs.	Adenine	198-205	cyclin dependent kinase 2	Homo sapiens	43-47	
22927831-5	2012	That plasticity obscured a requirement for Cdk2 activity in proliferation of human cells, which we uncovered by replacement of wild-type Cdk2 with a mutant version sensitized to inhibition by bulky adenine analogs.	Adenine	198-205	cyclin dependent kinase 2	Homo sapiens	137-141