| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-63 |
Sentence |
denotes |
Expression of a novel human sialidase encoded by the NEU2 gene. |
| T1 |
0-63 |
Sentence |
denotes |
Expression of a novel human sialidase encoded by the NEU2 gene. |
| T1 |
0-63 |
Sentence |
denotes |
Expression of a novel human sialidase encoded by the NEU2 gene. |
| TextSentencer_T2 |
64-235 |
Sentence |
denotes |
Sialidases (E.C.3.2.1.18) belong to a group of glycohydrolytic enzymes, widely distributed in nature, which remove sialic acid residues from glycoproteins and glycolipids. |
| T2 |
64-235 |
Sentence |
denotes |
Sialidases (E.C.3.2.1.18) belong to a group of glycohydrolytic enzymes, widely distributed in nature, which remove sialic acid residues from glycoproteins and glycolipids. |
| T2 |
64-235 |
Sentence |
denotes |
Sialidases (E.C.3.2.1.18) belong to a group of glycohydrolytic enzymes, widely distributed in nature, which remove sialic acid residues from glycoproteins and glycolipids. |
| TextSentencer_T3 |
236-438 |
Sentence |
denotes |
All of the sialidase so far characterized at the molecular level share an Asp block, repeated three to five times in the primary structure, and an F/YRIP sequence motif which is part of the active site. |
| T3 |
236-438 |
Sentence |
denotes |
All of the sialidase so far characterized at the molecular level share an Asp block, repeated three to five times in the primary structure, and an F/YRIP sequence motif which is part of the active site. |
| T3 |
236-438 |
Sentence |
denotes |
All of the sialidase so far characterized at the molecular level share an Asp block, repeated three to five times in the primary structure, and an F/YRIP sequence motif which is part of the active site. |
| TextSentencer_T4 |
439-559 |
Sentence |
denotes |
Using a sequence homology-based approach, we previously identified a human gene, named NEU2, mapping to chromosome 2q37. |
| T4 |
439-559 |
Sentence |
denotes |
Using a sequence homology-based approach, we previously identified a human gene, named NEU2, mapping to chromosome 2q37. |
| T4 |
439-559 |
Sentence |
denotes |
Using a sequence homology-based approach, we previously identified a human gene, named NEU2, mapping to chromosome 2q37. |
| TextSentencer_T5 |
560-722 |
Sentence |
denotes |
NEU2 encoded protein is a polypeptide of 380 amino acids with two Asp block consensuses and the YRIP sequence in the amino terminal part of the primary structure. |
| T5 |
560-722 |
Sentence |
denotes |
NEU2 encoded protein is a polypeptide of 380 amino acids with two Asp block consensuses and the YRIP sequence in the amino terminal part of the primary structure. |
| T5 |
560-722 |
Sentence |
denotes |
NEU2 encoded protein is a polypeptide of 380 amino acids with two Asp block consensuses and the YRIP sequence in the amino terminal part of the primary structure. |
| TextSentencer_T6 |
723-784 |
Sentence |
denotes |
Here we demonstrate that NEU2 encodes a functional sialidase. |
| T6 |
723-784 |
Sentence |
denotes |
Here we demonstrate that NEU2 encodes a functional sialidase. |
| T6 |
723-784 |
Sentence |
denotes |
Here we demonstrate that NEU2 encodes a functional sialidase. |
| TextSentencer_T7 |
785-946 |
Sentence |
denotes |
NEU2 was expressed in COS7 cells, giving rise to a dramatic increase in the sialidase activity measured in cell extracts with the artificial substrate 4-MU-NANA. |
| T7 |
785-946 |
Sentence |
denotes |
NEU2 was expressed in COS7 cells, giving rise to a dramatic increase in the sialidase activity measured in cell extracts with the artificial substrate 4-MU-NANA. |
| T7 |
785-946 |
Sentence |
denotes |
NEU2 was expressed in COS7 cells, giving rise to a dramatic increase in the sialidase activity measured in cell extracts with the artificial substrate 4-MU-NANA. |
| TextSentencer_T8 |
947-1156 |
Sentence |
denotes |
Using a rabbit polyclonal antiserum, on Western blots a protein band with a molecular weight of about 42 kDa was detectable, and its cytosolic localization was demonstrated with cell fractionation experiments. |
| T8 |
947-1156 |
Sentence |
denotes |
Using a rabbit polyclonal antiserum, on Western blots a protein band with a molecular weight of about 42 kDa was detectable, and its cytosolic localization was demonstrated with cell fractionation experiments. |
| T8 |
947-1156 |
Sentence |
denotes |
Using a rabbit polyclonal antiserum, on Western blots a protein band with a molecular weight of about 42 kDa was detectable, and its cytosolic localization was demonstrated with cell fractionation experiments. |
| TextSentencer_T9 |
1157-1223 |
Sentence |
denotes |
These results were confirmed using immunohistochemical techniques. |
| T9 |
1157-1223 |
Sentence |
denotes |
These results were confirmed using immunohistochemical techniques. |
| T9 |
1157-1223 |
Sentence |
denotes |
These results were confirmed using immunohistochemical techniques. |
| TextSentencer_T10 |
1224-1304 |
Sentence |
denotes |
NEU2 expression in E.coli cells allowed purification of the recombinant protein. |
| T10 |
1224-1304 |
Sentence |
denotes |
NEU2 expression in E.coli cells allowed purification of the recombinant protein. |
| T10 |
1224-1304 |
Sentence |
denotes |
NEU2 expression in E.coli cells allowed purification of the recombinant protein. |
| TextSentencer_T11 |
1305-1457 |
Sentence |
denotes |
As already observed in the enzyme expressed in COS7 cells, NEU2 pH optimum corresponds to 5.6 and the polypeptide showed a K(m)for 4-MU-NANA of 0.07 mM. |
| T11 |
1305-1457 |
Sentence |
denotes |
As already observed in the enzyme expressed in COS7 cells, NEU2 pH optimum corresponds to 5.6 and the polypeptide showed a K(m)for 4-MU-NANA of 0.07 mM. |
| T11 |
1305-1457 |
Sentence |
denotes |
As already observed in the enzyme expressed in COS7 cells, NEU2 pH optimum corresponds to 5.6 and the polypeptide showed a K(m)for 4-MU-NANA of 0.07 mM. |
| TextSentencer_T12 |
1458-1692 |
Sentence |
denotes |
In addition, based on the detectable similarities between the NEU2 amino acid sequence and bacterial sialidases, a prediction of the three-dimensional structure of the enzyme was carried out using a protein homology modeling approach. |
| T12 |
1458-1692 |
Sentence |
denotes |
In addition, based on the detectable similarities between the NEU2 amino acid sequence and bacterial sialidases, a prediction of the three-dimensional structure of the enzyme was carried out using a protein homology modeling approach. |
| T12 |
1458-1692 |
Sentence |
denotes |
In addition, based on the detectable similarities between the NEU2 amino acid sequence and bacterial sialidases, a prediction of the three-dimensional structure of the enzyme was carried out using a protein homology modeling approach. |