PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3935131-4	1985	Normal fibroblasts and fibroblasts of variant B and O of GM2 gangliosidosis secrete GM2-activator protein as a 24-kDa polypeptide, which is able to stimulate degradation of ganglioside GM2 by beta-hexosaminidase A in the in vitro assay.	Gangliosides	173-184	O-GlcNAcase	Homo sapiens	192-211	
19898953-1	2009	GM(2)-gangliosidosis is a rare and heterogeneous inherited metabolic disorder caused by autosomal recessive mutations in genes encoding the lysosomal enzyme beta-hexosaminidase, resulting in the accumulation of ganglioside GM(2) in various tissues, particularly the central nervous system.	Gangliosides	211-222	O-GlcNAcase	Homo sapiens	157-176	
6225718-0	1983	Activating proteins for ganglioside GM2 degradation by beta-hexosaminidase isoenzymes in tissue extracts from different species.	Gangliosides	24-35	O-GlcNAcase	Homo sapiens	55-74	
7451432-4	1981	The ganglioside was found to be resistant to neuraminidase (Clostridium perfringens), beta-hexosaminidase (jack bean), and beta-galactosidase.	Gangliosides	4-15	O-GlcNAcase	Homo sapiens	86-105	
31097363-1	2019	The catabolism of ganglioside GM2 is dependent on the lysosomal enzyme beta-hexosaminidase A and a supporting lipid transfer protein, the GM2 activator protein.	Gangliosides	18-29	O-GlcNAcase	Homo sapiens	71-90	
20821051-1	2010	GM2 gangliosidosis type Sandhoff is caused by a defect of beta-hexosaminidase, an enzyme involved in the catabolism of gangliosides.	Gangliosides	119-131	O-GlcNAcase	Homo sapiens	58-77	
17994285-1	2007	Sandhoff disease, Gaucher disease type I and sialidosis type I are lysosomal storage disorders caused, respectively, by deficiency of activity of beta-hexosaminidase (storage of GM(2) and GA(2) ganglioside), glucosylceramidase (storage of glucosylceramide) and alpha-neuraminidase (storage of glucopeptides and/or oligosaccharides).	Gangliosides	194-205	O-GlcNAcase	Homo sapiens	146-165	
18588514-2	2008	We previously demonstrated that Hex associated with human fibroblast PM as the mature form, which is functionally active towards G(M2) ganglioside.	Gangliosides	135-146	O-GlcNAcase	Homo sapiens	32-35	
9572057-1	1998	The GM2 gangliosidoses are a group of heritable neurodegenerative disorders caused by excessive accumulation of the ganglioside GM2 owing to deficiency in beta-hexosaminidase activity.	Gangliosides	116-127	O-GlcNAcase	Homo sapiens	155-174	
12662933-3	2003	Interest in human beta-hexosaminidase stems from its association with Tay-Sachs and Sandhoff disease; these are prototypical lysosomal storage disorders resulting from the abnormal accumulation of G(M2)-ganglioside (G(M2)).	Gangliosides	203-214	O-GlcNAcase	Homo sapiens	18-37	
12760286-1	2003	In the GM2 gangliosidosis B1 variant, the mutated isoenzyme A of beta-hexosaminidase (Hex) is incapable of hydrolyzing ganglioside GM2 and negatively charged substrates.	Gangliosides	119-130	O-GlcNAcase	Homo sapiens	65-84	
12760286-1	2003	In the GM2 gangliosidosis B1 variant, the mutated isoenzyme A of beta-hexosaminidase (Hex) is incapable of hydrolyzing ganglioside GM2 and negatively charged substrates.	Gangliosides	119-130	O-GlcNAcase	Homo sapiens	86-89	
11278374-2	2001	Since most previous in vitro investigations used micellar ganglioside GM2 as substrate, we studied the degradation of membrane-bound ganglioside GM2 by water-soluble beta-hexosaminidase A in the presence of the GM2 activator protein in a detergent-free, liposomal assay system.	Gangliosides	133-144	O-GlcNAcase	Homo sapiens	166-185	
7766021-5	1995	Homoloyg search and limited proteolytic digestion showed that the enzyme has a C-terminal 58-kDa catalytic domain very similar to that of human lysosomal beta-hexosaminidase that is responsible for hydrolyzing gangliosides.	Gangliosides	210-222	O-GlcNAcase	Homo sapiens	154-173