PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14505645-0	2003	Novel sulfated gangliosides, high-affinity ligands for neural siglecs, inhibit NADase activity of leukocyte cell surface antigen CD38.	Gangliosides	15-27	CD38 molecule	Homo sapiens	129-133	
16261579-2	2006	Our results suggest that CD38 is likely to recognize the two phosphate groups in NAD and the two carboxyl groups in tandem sialic acid residues of gangliosides.	Gangliosides	147-159	CD38 molecule	Homo sapiens	25-29	
14505645-2	2003	These sulfated gangliosides were potent inhibitors of NADase activity of leukocyte cell surface antigen CD38.	Gangliosides	15-27	CD38 molecule	Homo sapiens	104-108	
14579585-0	2003	Complex gangliosides as cell surface inhibitors for the ecto-NAD+ glycohydrolase of CD38.	Gangliosides	8-20	CD38 molecule	Homo sapiens	84-88	
11170409-0	2001	Complex gangliosides as cell surface inhibitors for the ecto-NAD+ glycohydrolase of CD38.	Gangliosides	8-20	CD38 molecule	Homo sapiens	84-88	
11170409-5	2001	In the present study, we examined the effect of exogenous gangliosides on the NADase activity of CD38 on the surface of retinoic acid-treated human leukemic HL60 cells and CD38-transfected THP-1 cells.	Gangliosides	58-70	CD38 molecule	Homo sapiens	97-101	
11170409-11	2001	These results suggest a novel role of complex gangliosides for the first time as cell surface inhibitors of CD38 through specific and cis interaction between the oligosaccharide moiety and the extracellular domain.	Gangliosides	46-58	CD38 molecule	Homo sapiens	108-112	
8662799-0	1996	Inhibition of NAD+ glycohydrolase and ADP-ribosyl cyclase activities of leukocyte cell surface antigen CD38 by gangliosides.	Gangliosides	111-123	CD38 molecule	Homo sapiens	103-107	
8662799-4	1996	Here, we investigated the effect of gangliosides on the enzymatic activity of leukocyte cell surface antigen CD38, which is identified as an ecto-NADase (Kontani, K., Nishina, H., Ohoka, Y., Takahashi, K., and Katada, T. (1993) J. Biol.	Gangliosides	36-48	CD38 molecule	Homo sapiens	109-113	
8662799-7	1996	Gangliosides GM1a and GQ1balpha inhibited the NADase activity in the immunoprecipitate of anti-CD38 antibody from the membrane extract of retinoic acid-treated human leukemic HL-60 cells.	Gangliosides	0-12	CD38 molecule	Homo sapiens	95-99	
10731682-0	2000	Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside.	Gangliosides	135-146	CD38 molecule	Homo sapiens	115-119	
10731682-2	2000	The extracellular catalytic domain of CD38 was expressed as a fusion protein with maltose-binding protein, and was crystallized in the complex with a ganglioside, G(T1b), one of the possible physiological inhibitors of this ectoenzyme.	Gangliosides	150-161	CD38 molecule	Homo sapiens	38-42	
8662799-8	1996	Gangliosides also inhibited the NADase activity of the extracellular domain of CD38 antigen that was deprived of the transmembrane domain and was expressed in Escherichia coli as a fusion protein with maltose-binding protein (MBP-CD38).	Gangliosides	0-12	CD38 molecule	Homo sapiens	79-83	
8662799-8	1996	Gangliosides also inhibited the NADase activity of the extracellular domain of CD38 antigen that was deprived of the transmembrane domain and was expressed in Escherichia coli as a fusion protein with maltose-binding protein (MBP-CD38).	Gangliosides	0-12	CD38 molecule	Homo sapiens	230-234	
8662799-9	1996	The order of the inhibitory effect of purified ganglioside species on the NADase activity on MBP-CD38 was as follows: GQ1balpha > GT1b, GQ1b > GD1a, GD1b, GM1a, GM1b, GD3, GM3.	Gangliosides	47-58	CD38 molecule	Homo sapiens	97-101	
8662799-13	1996	At present, gangliosides are the only endogenous species that can block the enzymatic activity of CD38 antigen.	Gangliosides	12-24	CD38 molecule	Homo sapiens	98-102