PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8508806-0	1993	Biochemical bases of the interaction of human basic fibroblast growth factor with glycosaminoglycans.	Glycosaminoglycans	82-100	fibroblast growth factor 2	Homo sapiens	46-76	
8508806-2	1993	In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution.	Glycosaminoglycans	154-172	fibroblast growth factor 2	Homo sapiens	111-141	
8508806-2	1993	In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution.	Glycosaminoglycans	154-172	fibroblast growth factor 2	Homo sapiens	143-147	
8508806-2	1993	In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution.	Glycosaminoglycans	174-178	fibroblast growth factor 2	Homo sapiens	111-141	
8508806-2	1993	In the present study we have attempted a characterization of the biochemical bases of the interaction of human basic fibroblast growth factor (bFGF) with glycosaminoglycans (GAGs) in solution.	Glycosaminoglycans	174-178	fibroblast growth factor 2	Homo sapiens	143-147	
8508806-3	1993	This interaction has been evidenced as the capacity of different GAGs and various sulfated compounds to protect bFGF and different bFGF mutants from tryptic cleavage.	Glycosaminoglycans	65-69	fibroblast growth factor 2	Homo sapiens	112-116	
8508806-3	1993	This interaction has been evidenced as the capacity of different GAGs and various sulfated compounds to protect bFGF and different bFGF mutants from tryptic cleavage.	Glycosaminoglycans	65-69	fibroblast growth factor 2	Homo sapiens	131-135	
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Glycosaminoglycans	26-30	fibroblast growth factor 2	Homo sapiens	42-46	
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Glycosaminoglycans	26-30	fibroblast growth factor 2	Homo sapiens	340-344	
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Glycosaminoglycans	26-29	fibroblast growth factor 2	Homo sapiens	42-46	
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin > heparan sulfate > dermatan sulfate = chondroitin sulfates A and C > hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Glycosaminoglycans	26-29	fibroblast growth factor 2	Homo sapiens	340-344	
8508806-9	1993	Moreover, tryptic digestion studies performed with various heparin molecules and dextran sulfates of different size, ranging from 2.0 kDa to 500 kDa, indicate that the number of bFGF molecules which interact with a single molecule of polysaccharide is related to the molecular mass of the GAG and that six hexose residues are sufficient to protect 1-2 molecules bFGF.	Glycosaminoglycans	289-292	fibroblast growth factor 2	Homo sapiens	178-182	
8508806-10	1993	In conclusion, our findings indicate that the capacity of GAGs to protect bFGF from tryptic cleavage depends upon their size, sulfation, distribution of the anionic sites along the chain, and structural requirements of the bFGF molecule.	Glycosaminoglycans	58-62	fibroblast growth factor 2	Homo sapiens	74-78	
8508806-10	1993	In conclusion, our findings indicate that the capacity of GAGs to protect bFGF from tryptic cleavage depends upon their size, sulfation, distribution of the anionic sites along the chain, and structural requirements of the bFGF molecule.	Glycosaminoglycans	58-62	fibroblast growth factor 2	Homo sapiens	223-227