PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14701904-3	2004	Unfolding of labeled tetra-Cys CRABP I is accompanied by enhancement of FlAsH fluorescence, which made it possible to determine the free energy of unfolding of this protein by urea titration in cells and to follow in real time the formation of inclusion bodies by a slow-folding, aggregationprone mutant (FlAsH-labeled P39A tetra-Cys CRABP I).	Urea	176-180	cellular retinoic acid binding protein 1	Homo sapiens	31-38	
8286330-2	1994	Urea unfolding-refolding of CRABP is a highly cooperative process that can be approximated by a two-state model.	Urea	0-4	cellular retinoic acid binding protein 1	Homo sapiens	28-33	
30252171-3	2018	We report that several sequence regions of a beta-barrel protein, cellular retinoic acid-binding protein 1 (CRABP1), populate native-like secondary structure to a significant extent in the denatured state in 8 M urea.	Urea	212-216	cellular retinoic acid binding protein 1	Homo sapiens	66-106	
30252171-3	2018	We report that several sequence regions of a beta-barrel protein, cellular retinoic acid-binding protein 1 (CRABP1), populate native-like secondary structure to a significant extent in the denatured state in 8 M urea.	Urea	212-216	cellular retinoic acid binding protein 1	Homo sapiens	108-114