PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28430446-2	2017	Here we have employed an approach combining amide backbone hydrogen/deuterium exchange coupled with mass spectrometry, fluorescence spectroscopy, and molecular simulations to characterize allosteric patterns of chaperonin GroEL, an ~800 kDa tetradecamer from E. coli.	Amides	44-49	GroEL	Escherichia coli	222-227	
9299328-2	1997	We examined the exchange of amide protons of cyclophilin A (CypA) interacting with GroEL, using NMR spectroscopy.	Amides	28-33	GroEL	Escherichia coli	83-88	
9299328-5	1997	This allowed the calculation of protection factors (PF) for the backbone amide protons in the GroEL-bound substrate protein.	Amides	73-78	GroEL	Escherichia coli	94-99	
7908413-4	1994	Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin.	Amides	169-174	GroEL	Escherichia coli	117-122	
7908413-4	1994	Here we use nuclear magnetic resonance techniques to show that the interaction of the small protein cyclophilin with GroEL is reversible by temperature changes, and all amide protons in GroEL-bound cyclophilin are exchanged with the solvent, although this exchange does not occur in free cyclophilin.	Amides	169-174	GroEL	Escherichia coli	186-191