PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9201993-1	1997	The degradation of glucosylceramide in lysosomes is accomplished by glucosylceramidase with the assistance of, at least, another protein, saposin C (Sap C), which is generated from a large precursor together with three other similar proteins, saposins A, B, and D.	Glucosylceramides	19-35	SH2 domain containing 1A	Homo sapiens	149-152	
9201993-8	1997	Sap C increased the rate of hydrolysis of both the artificial water soluble substrate, 4-methylumbelliferyl-beta-D-glucopyranoside, and the lipid substrate, glucosylceramide, while Sap A only stimulated degradation of the sphingolipid.	Glucosylceramides	157-173	SH2 domain containing 1A	Homo sapiens	0-3	
9201993-12	1997	In conclusion, our results show that both Sap A and Sap C are required for maximal hydrolysis of glucosylceramide inserted in PS-containing LUV, that their effects are synergistic, and that their mode of action is different.	Glucosylceramides	97-113	SH2 domain containing 1A	Homo sapiens	42-45	
9201993-12	1997	In conclusion, our results show that both Sap A and Sap C are required for maximal hydrolysis of glucosylceramide inserted in PS-containing LUV, that their effects are synergistic, and that their mode of action is different.	Glucosylceramides	97-113	SH2 domain containing 1A	Homo sapiens	52-55	
9201993-14	1997	It can be envisaged that Sap A in conjunction with Sap C might have a physiological role in glucosylceramide degradation.	Glucosylceramides	92-108	SH2 domain containing 1A	Homo sapiens	25-28	
9201993-14	1997	It can be envisaged that Sap A in conjunction with Sap C might have a physiological role in glucosylceramide degradation.	Glucosylceramides	92-108	SH2 domain containing 1A	Homo sapiens	51-54