PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10512721-7	1999	When GroES was present, ATP as well as ADP and AMP-PNP were effective in reducing the affinity between GroEL and the refolding intermediate of alpha-lactalbumin.	Adenylyl Imidodiphosphate	47-54	heat shock protein family D (Hsp60) member 1	Homo sapiens	103-108	
10512721-8	1999	The affinity at a saturating concentration of ADP or AMP-PNP was about ten times lower than with GroEL alone.	Adenylyl Imidodiphosphate	53-60	heat shock protein family D (Hsp60) member 1	Homo sapiens	97-102	
8861908-3	1996	Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 A resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP.	Adenylyl Imidodiphosphate	203-210	heat shock protein family D (Hsp60) member 1	Homo sapiens	106-111	
10395457-6	1999	When ADP, ATP, or AMP-PNP were added to a solution of GroEL and Mg2+, C138 incorporated approximately 0.8 labels, while C458 incorporated approximately 0.1 labels.	Adenylyl Imidodiphosphate	18-25	heat shock protein family D (Hsp60) member 1	Homo sapiens	54-59	
9407071-4	1997	Electron microscopy, image processing, and biochemical analysis of GroEL, a single-ring mutant (SR1) and a inter-ring communication affected mutant (A126V), in the presence of ATP and adenylyl imidodiphosphate, have allowed the identification of a conformational change in the apical domains that is strictly dependent on the communication between the two GroEL rings.	Adenylyl Imidodiphosphate	184-209	heat shock protein family D (Hsp60) member 1	Homo sapiens	67-72	
9054367-7	1997	The inability of the nonhydrolyzable ATP analog, AMP-PNP, to cause a similar effect is explained by the interaction of bisANS with a transient conformational state of GroEL formed consequent to ATP hydrolysis.	Adenylyl Imidodiphosphate	49-56	heat shock protein family D (Hsp60) member 1	Homo sapiens	167-172	
9087913-2	1997	Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution.	Adenylyl Imidodiphosphate	276-283	heat shock protein family D (Hsp60) member 1	Homo sapiens	197-202	
9087913-2	1997	Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution.	Adenylyl Imidodiphosphate	276-283	heat shock protein family D (Hsp60) member 1	Homo sapiens	197-202	
9087913-3	1997	Both AMP-PNP and ATP induce similar conformational shifts in the apical domains of GroEL.	Adenylyl Imidodiphosphate	5-12	heat shock protein family D (Hsp60) member 1	Homo sapiens	83-88	
9914513-1	1999	The conformational properties of the molecular chaperone GroEL in the presence of ATP, its non-hydrolyzable analog 5"-adenylimidodiphosphate (AMP-PNP), and ADP have been analyzed by differential scanning calorimetry (DSC), Fourier-transform infra-red (FT-IR) and fluorescence spectroscopy.	Adenylyl Imidodiphosphate	142-149	heat shock protein family D (Hsp60) member 1	Homo sapiens	57-62	
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.	Adenylyl Imidodiphosphate	318-325	heat shock protein family D (Hsp60) member 1	Homo sapiens	249-254	
9087913-5	1997	At the RR state for AMP-PNP and ATP, both GroEL rings undergo conformational changes, albeit of different magnitude, giving rise to a structurally asymmetric particle (one ring in the "open" state, while the other is in an "intermediate" state).	Adenylyl Imidodiphosphate	20-27	heat shock protein family D (Hsp60) member 1	Homo sapiens	42-47	
8861908-3	1996	Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 A resolution for GroEL and GroEL-GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP.	Adenylyl Imidodiphosphate	203-210	heat shock protein family D (Hsp60) member 1	Homo sapiens	116-121	
12736270-0	2003	Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.	Adenylyl Imidodiphosphate	32-38	heat shock protein family D (Hsp60) member 1	Homo sapiens	53-58