PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1612112-0	1992	Neuraminidase reduces the number of super-high-affinity [3H]oxotremorine-M binding sites in lung.	Tritium	57-59	neuraminidase 1	Homo sapiens	0-13	
8254757-5	1994	Treatment with neuraminidase, O-glycosidase, and N-glycanase F was found to be necessary to remove all radiolabel from [3H]glucosamine-labelled envelope glycoprotein, a result seen for both recombinant and HIV-1-derived envelope glycoprotein.	Tritium	120-122	neuraminidase 1	Homo sapiens	15-28	
1612112-2	1992	[3H]Oxo-M labelled super-high-affinity binding sites (KD of 1.36 nM), as indicated by the very high affinity displayed by carbachol when tested in competition with 0.5 mM [3H]oxo-M. Neuraminidase reduced the number of [3H]oxo-M binding sites with no change occurring in the KD.	Tritium	1-3	neuraminidase 1	Homo sapiens	182-195	
2962888-3	1988	The exoglycosidase, neuraminidase, altered the electrophoretic mobility of the 94 kDa labeled band to 54 kDa with a slight modification in the binding affinity of [3H]spiperone.	Tritium	164-166	neuraminidase 1	Homo sapiens	20-33	
1692606-3	1990	Neuraminidase decreased the affinity of the M2-selective agonist carbamylcholine in competitive binding experiments performed with [3H]QNB and [3H]NMS.	Tritium	132-134	neuraminidase 1	Homo sapiens	0-13	
1692606-3	1990	Neuraminidase decreased the affinity of the M2-selective agonist carbamylcholine in competitive binding experiments performed with [3H]QNB and [3H]NMS.	Tritium	144-146	neuraminidase 1	Homo sapiens	0-13	
1692606-5	1990	Neuraminidase did not modify the binding parameters of 3H-antagonists but reduced the number of agonist binding sites revealed by [3H]oxo-M.	Tritium	131-133	neuraminidase 1	Homo sapiens	0-13	
3059890-10	1988	However, the extent of total cell surface sialation, as assessed by neuraminidase-releasable [3H]glucosamine from metabolically labeled monolayers, did not differ between pre- and postconfluent cultures, suggesting that some specific sialated cell surface constituent is responsible for decreased PMN adherence to postconfluent monolayers.	Tritium	94-97	neuraminidase 1	Homo sapiens	68-81	
2935663-3	1985	The influences of diltiazem on 3H-NTD bindings differed between NUase treated and untreated preparations.	Tritium	31-33	neuraminidase 1	Homo sapiens	64-69	
3942785-8	1986	Treatment of serotonectin with neuraminidase resulted in a quantitative release of sialic acid without loss of antigenicity or binding capacity for [3H]serotonin.	Tritium	149-151	neuraminidase 1	Homo sapiens	31-44	
2448618-3	1987	Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation.	Tritium	75-77	neuraminidase 1	Homo sapiens	0-13	
2448618-3	1987	Neuraminidase treatment or mild acid hydrolysis confirmed the presence of [3H]sialyl residues in sialoglycolipids synthesized after [3H]fetuin incubation.	Tritium	133-135	neuraminidase 1	Homo sapiens	0-13	
3624873-3	1987	Neuraminidase-treated (NT)-PMN bound and internalized [3H]FMLP (used as receptor marker) as well as normal PMN.	Tritium	55-57	neuraminidase 1	Homo sapiens	0-13	
2935663-6	1985	Scatchard plot analysis indicated that a high dose of diltiazem (10(-6) M) increased only the affinity of 3H-NTD to the binding site in both the NUase-treated and untreated preparations.	Tritium	106-108	neuraminidase 1	Homo sapiens	145-150	
1217707-0	1975	Neuraminidase assay utilizing sialyl-oligosaccharide substrates with tritium-labeled aglycone.	Tritium	69-76	neuraminidase 1	Homo sapiens	0-13