PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1680001-6	1991	The complex between GroEL and denatured LDH is destabilized by the binding of magnesium/ATP (Mg/ATP) or by the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP).	Magnesium	78-87	GroEL	Escherichia coli	20-25	
18230606-1	2008	The chaperonin GroEL assists protein folding in the presence of ATP and magnesium through substrate protein capsulation in combination with the cofactor GroES.	Magnesium	72-81	GroEL	Escherichia coli	15-20	
1680001-7	1991	From our initial kinetic data, we propose that GroEL exists in two interconvertible forms, one of which is stabilized by the binding of Mg/ATP but associates weakly with the unfolded protein.	Magnesium	136-138	GroEL	Escherichia coli	47-52	
10548063-2	1999	In this paper, we investigate the effects of potassium, magnesium, and MgADP on the release of the EcDHFR late folding intermediate from GroEL.	Magnesium	56-65	GroEL	Escherichia coli	137-142	
10548063-4	1999	In the absence of potassium, magnesium, and ADP, approximately 80-90% of GroEL resides in the form with the faster rate of release.	Magnesium	29-38	GroEL	Escherichia coli	73-78	
10548063-5	1999	Magnesium and potassium both shift the distribution of GroEL forms toward the form with the slower release rate, though cooperativity for the magnesium-induced transition is observed only in the presence of potassium.	Magnesium	0-9	GroEL	Escherichia coli	55-60	
10548063-5	1999	Magnesium and potassium both shift the distribution of GroEL forms toward the form with the slower release rate, though cooperativity for the magnesium-induced transition is observed only in the presence of potassium.	Magnesium	142-151	GroEL	Escherichia coli	55-60	
10548063-8	1999	In the presence of saturating magnesium, potassium, and MgADP, the apparent rate constant for the release of EcDHFR from wild-type GroEL at 22 degrees C reaches a limiting value of 0.014 s(-1).	Magnesium	30-39	GroEL	Escherichia coli	131-136	
1680001-6	1991	The complex between GroEL and denatured LDH is destabilized by the binding of magnesium/ATP (Mg/ATP) or by the nonhydrolyzable analogue adenylyl imidodiphosphate (AMP-PNP).	Magnesium	93-95	GroEL	Escherichia coli	20-25