PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9860959-2	1998	In the absence of GroES and nucleotides, the rate of GroEL-mediated refolding of heat- and DTT-denatured mitochondrial malate dehydrogenase was extremely low, but some three times higher than the spontaneous rate.	Dithiothreitol	91-94	heat shock protein family D (Hsp60) member 1	Homo sapiens	53-58	
14577157-1	2003	The interaction of the molecular chaperonin GroEL with fluorescein-labeled lysozyme in the presence of high concentrations of thiol reagent--dithiothreitol (DTT) has been studied.	Dithiothreitol	139-155	heat shock protein family D (Hsp60) member 1	Homo sapiens	44-49	
14577157-1	2003	The interaction of the molecular chaperonin GroEL with fluorescein-labeled lysozyme in the presence of high concentrations of thiol reagent--dithiothreitol (DTT) has been studied.	Dithiothreitol	157-160	heat shock protein family D (Hsp60) member 1	Homo sapiens	44-49	
14577157-3	2003	It has been shown that in the presence of high concentrations of DTT and two-fold molar excess of GroEL the lysozyme tightly interacts with GroEL that essentially decreases the efficiency of its aggregation.	Dithiothreitol	65-68	heat shock protein family D (Hsp60) member 1	Homo sapiens	140-145	
12441378-3	2002	The reduction by dithiothreitol of the three intramolecular disulfide bonds of the fifth domain was accelerated in the presence of stoichiometric amounts of GroEL, indicating that the fifth domain was destabilized upon interaction with GroEL.	Dithiothreitol	17-31	heat shock protein family D (Hsp60) member 1	Homo sapiens	157-162	
12441378-3	2002	The reduction by dithiothreitol of the three intramolecular disulfide bonds of the fifth domain was accelerated in the presence of stoichiometric amounts of GroEL, indicating that the fifth domain was destabilized upon interaction with GroEL.	Dithiothreitol	17-31	heat shock protein family D (Hsp60) member 1	Homo sapiens	236-241	
11124034-6	2000	Although single minichaperones (residues 193-335 to 191-376 of GroEL) have certain chaperone activities in vitro and in vivo, they cannot refold heat and dithiothreitol-denatured mitochondrial malate dehydrogenase (mtMDH), a reaction that normally requires GroEL, its co-chaperonin GroES and ATP.	Dithiothreitol	154-168	heat shock protein family D (Hsp60) member 1	Homo sapiens	63-68