PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21291269-5	2011	In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography.	8-anilino-1-naphthalenesulfonic acid	130-163	cyclin dependent kinase 2	Homo sapiens	181-185	
21291269-5	2011	In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography.	8-anilino-1-naphthalenesulfonic acid	165-168	cyclin dependent kinase 2	Homo sapiens	181-185	
21291269-6	2011	ANS interacts with free CDK2 in a saturation-dependent manner with an apparent K(d) of 37 muM, and cyclin A displaced ANS from CDK2 with an EC(50) value of 0.6 muM.	8-anilino-1-naphthalenesulfonic acid	0-3	cyclin dependent kinase 2	Homo sapiens	24-28	
21291269-6	2011	ANS interacts with free CDK2 in a saturation-dependent manner with an apparent K(d) of 37 muM, and cyclin A displaced ANS from CDK2 with an EC(50) value of 0.6 muM.	8-anilino-1-naphthalenesulfonic acid	118-121	cyclin dependent kinase 2	Homo sapiens	127-131	
21291269-8	2011	Binding of ANS is accompanied by substantial structural changes in CDK2, resulting in a C-helix conformation that is incompatible for cyclin A association.	8-anilino-1-naphthalenesulfonic acid	11-14	cyclin dependent kinase 2	Homo sapiens	67-71	
21291269-9	2011	These findings indicate the potential of the ANS binding pocket as a new target site for allosteric inhibitors disrupting the interaction of CDKs and cyclins.	8-anilino-1-naphthalenesulfonic acid	45-48	cyclin dependent kinase 2	Homo sapiens	141-145