PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9914513-3	1999	In addition, ATP induces a conformational change in GroEL characterized by (a) the appearance of a reversible low temperature endotherm in the DSC profiles of the protein, and (b) an enhanced binding of the hydrophobic probe 8-anilino-naphthalene-1-sulfonate (ANS), which strictly depends on ATP hydrolysis.	8-anilino-1-naphthalenesulfonic acid	225-258	heat shock protein family D (Hsp60) member 1	Homo sapiens	52-57	
9914513-3	1999	In addition, ATP induces a conformational change in GroEL characterized by (a) the appearance of a reversible low temperature endotherm in the DSC profiles of the protein, and (b) an enhanced binding of the hydrophobic probe 8-anilino-naphthalene-1-sulfonate (ANS), which strictly depends on ATP hydrolysis.	8-anilino-1-naphthalenesulfonic acid	260-263	heat shock protein family D (Hsp60) member 1	Homo sapiens	52-57	
9914513-4	1999	The similar sensitivity to K+ of the temperature range where activation of the GroEL ATPase activity, the low temperature endotherm, and the increase of the ANS fluorescence are abserved strongly indicates the existence of a conformational state of GroEL during ATP hydrolysis, different from that generated on ADP or AMP-PNP binding.	8-anilino-1-naphthalenesulfonic acid	157-160	heat shock protein family D (Hsp60) member 1	Homo sapiens	249-254