PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21870866-3	2011	LERE-QSAR analysis quantitatively revealed that the complex formation is driven by hydrogen-bonding and electrostatic interaction of hNEU2 with sialic acid analogues.	N-Acetylneuraminic Acid	144-155	neuraminidase 2	Homo sapiens	133-138	
29124209-1	2015	Human cytosolic sialidase (Neuraminidase 2, NEU2) catalyzes the removal of terminal sialic acid residues from glycoconjugates.	N-Acetylneuraminic Acid	84-95	neuraminidase 2	Homo sapiens	6-25	
29124209-1	2015	Human cytosolic sialidase (Neuraminidase 2, NEU2) catalyzes the removal of terminal sialic acid residues from glycoconjugates.	N-Acetylneuraminic Acid	84-95	neuraminidase 2	Homo sapiens	27-42	
29124209-1	2015	Human cytosolic sialidase (Neuraminidase 2, NEU2) catalyzes the removal of terminal sialic acid residues from glycoconjugates.	N-Acetylneuraminic Acid	84-95	neuraminidase 2	Homo sapiens	44-48	
25222608-1	2014	The removal of sialic acid (Sia) residues from glycoconjugates in vertebrates is mediated by a family of neuraminidases (sialidases) consisting of Neu1, Neu2, Neu3 and Neu4 enzymes.	N-Acetylneuraminic Acid	15-26	neuraminidase 2	Homo sapiens	153-157	
25222608-1	2014	The removal of sialic acid (Sia) residues from glycoconjugates in vertebrates is mediated by a family of neuraminidases (sialidases) consisting of Neu1, Neu2, Neu3 and Neu4 enzymes.	N-Acetylneuraminic Acid	28-31	neuraminidase 2	Homo sapiens	153-157	
25222608-4	2014	We found significant differences in substrate specificity of the enzymes towards the substrates containing alpha2,6-linked Sia, which were readily cleaved by Neu3 and Neu1 but not by Neu4 and Neu2.	N-Acetylneuraminic Acid	123-126	neuraminidase 2	Homo sapiens	192-196	
20486931-3	2010	We previously reported the synthesis of chimeric alpha/delta-peptides from glutamic acids (Glu) and the sialic acid derivative Neu2en.	N-Acetylneuraminic Acid	104-115	neuraminidase 2	Homo sapiens	127-131	
17374613-8	2007	In fact, three cytosolic glycoproteins, in the range 45-66 kDa, showed a 50-70% decrease of their sialic acid content upon Neu2 expression, supporting their possible role as modulators of the Bcr-Abl complex.	N-Acetylneuraminic Acid	98-109	neuraminidase 2	Homo sapiens	123-127	
2765299-3	1989	After treatment with neuraminidase 2.92 nmol/mg dry weight and 3.73 nmol/mg dry weight of sialic acid were freed from U 251 cells and C6 cell, but only 8.11% (U 251 cell) and 11.24% (C 6 cell) of these sialic acids originated from glycolipid, and thus the major part of sialic acid might be released from glycoprotein of the cells.	N-Acetylneuraminic Acid	90-101	neuraminidase 2	Homo sapiens	21-36	
20978010-8	2011	All showed much lower activities than with the corresponding sialic acid substrate, with the influenza virus N1 being the most active and human NEU2 being the least active.	N-Acetylneuraminic Acid	61-72	neuraminidase 2	Homo sapiens	144-148	
11746676-0	2001	Computational 3-D modeling and site-directed mutation of an antibody that binds Neu2en5Ac, a transition state analogue of a sialic acid.	N-Acetylneuraminic Acid	124-135	neuraminidase 2	Homo sapiens	80-84	
2745406-5	1989	The results revealed: 1) an identical response in binding activity and sialic acid content in cells subjected to minimal exposure to neuraminidase; 2) a parallel and synchronous recovery of both parameters following modulation; 3) an invariant binding of high affinity ligands, and 4) the ability of galactose oxidase to restore, at least partially, the cell"s ability to bind asialoglycoprotein.	N-Acetylneuraminic Acid	71-82	neuraminidase 2	Homo sapiens	133-149	
2765299-3	1989	After treatment with neuraminidase 2.92 nmol/mg dry weight and 3.73 nmol/mg dry weight of sialic acid were freed from U 251 cells and C6 cell, but only 8.11% (U 251 cell) and 11.24% (C 6 cell) of these sialic acids originated from glycolipid, and thus the major part of sialic acid might be released from glycoprotein of the cells.	N-Acetylneuraminic Acid	202-213	neuraminidase 2	Homo sapiens	21-36	
558203-3	1977	While maximal sialic acid release was obtained with 5 units neuraminidase/2 x10(9) erythrocytes, maximal concanavalin A agglutination was only obtained after exposure to 20 units neuramindase.	N-Acetylneuraminic Acid	14-25	neuraminidase 2	Homo sapiens	60-75	
32665690-8	2020	Such possibility relies upon a putative role in sialic acid biology, where GBA3 participates in a cellular network involving NEU2 and CMAH.	N-Acetylneuraminic Acid	48-59	neuraminidase 2	Homo sapiens	125-129	
29341588-8	2018	We report that 9- O-acetylation had a significant, and differential, impact on sialic acid hydrolysis by hNEU with general substrate tolerance following the trend of Neu5Ac > Neu5Gc >> Neu5,9Ac2 for NEU2, NEU3, and NEU4.	N-Acetylneuraminic Acid	79-90	neuraminidase 2	Homo sapiens	208-212