| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-104 |
Sentence |
denotes |
Xenopus galectin-VIIa binds N-glycans of members of the cortical granule lectin family (xCGL and xCGL2). |
| T1 |
0-104 |
Sentence |
denotes |
Xenopus galectin-VIIa binds N-glycans of members of the cortical granule lectin family (xCGL and xCGL2). |
| T1 |
0-104 |
Sentence |
denotes |
Xenopus galectin-VIIa binds N-glycans of members of the cortical granule lectin family (xCGL and xCGL2). |
| TextSentencer_T2 |
105-280 |
Sentence |
denotes |
We have identified members of the Xenopus cortical granule lectin (xCGL) family as candidate target glycoproteins of Xenopus galectin-VIIa (xgalectin-VIIa) in Xenopus embryos. |
| T2 |
105-280 |
Sentence |
denotes |
We have identified members of the Xenopus cortical granule lectin (xCGL) family as candidate target glycoproteins of Xenopus galectin-VIIa (xgalectin-VIIa) in Xenopus embryos. |
| T2 |
105-280 |
Sentence |
denotes |
We have identified members of the Xenopus cortical granule lectin (xCGL) family as candidate target glycoproteins of Xenopus galectin-VIIa (xgalectin-VIIa) in Xenopus embryos. |
| TextSentencer_T3 |
281-375 |
Sentence |
denotes |
In addition to the original xCGL, we also identified a novel member of the xCGL family, xCGL2. |
| T3 |
281-375 |
Sentence |
denotes |
In addition to the original xCGL, we also identified a novel member of the xCGL family, xCGL2. |
| T3 |
281-375 |
Sentence |
denotes |
In addition to the original xCGL, we also identified a novel member of the xCGL family, xCGL2. |
| TextSentencer_T4 |
376-498 |
Sentence |
denotes |
Expression of the mRNAs of xCGL and xCGL2, as well as that of xgalectin-VIIa, was observed throughout early embryogenesis. |
| T4 |
376-498 |
Sentence |
denotes |
Expression of the mRNAs of xCGL and xCGL2, as well as that of xgalectin-VIIa, was observed throughout early embryogenesis. |
| T4 |
376-498 |
Sentence |
denotes |
Expression of the mRNAs of xCGL and xCGL2, as well as that of xgalectin-VIIa, was observed throughout early embryogenesis. |
| TextSentencer_T5 |
499-768 |
Sentence |
denotes |
Two and three potential N-glycosylation sites were deduced from the amino acid sequences of xCGL and xCGL2, respectively, and xgalectin-VIIa recognizes N-glycans linked to a common site in xCGL and xCGL2 and also recognizes N-glycans linked to a site specific to xCGL2. |
| T5 |
499-768 |
Sentence |
denotes |
Two and three potential N-glycosylation sites were deduced from the amino acid sequences of xCGL and xCGL2, respectively, and xgalectin-VIIa recognizes N-glycans linked to a common site in xCGL and xCGL2 and also recognizes N-glycans linked to a site specific to xCGL2. |
| T5 |
499-768 |
Sentence |
denotes |
Two and three potential N-glycosylation sites were deduced from the amino acid sequences of xCGL and xCGL2, respectively, and xgalectin-VIIa recognizes N-glycans linked to a common site in xCGL and xCGL2 and also recognizes N-glycans linked to a site specific to xCGL2. |
| TextSentencer_T6 |
769-840 |
Sentence |
denotes |
However, interaction between xgalectin-Ia and xCGLs was not detectable. |
| T6 |
769-840 |
Sentence |
denotes |
However, interaction between xgalectin-Ia and xCGLs was not detectable. |
| T6 |
769-840 |
Sentence |
denotes |
However, interaction between xgalectin-Ia and xCGLs was not detectable. |
| TextSentencer_T7 |
841-969 |
Sentence |
denotes |
We also obtained consistent results on surface plasmon resonance analysis involving xCGLs as ligands and xgalectins as analytes. |
| T7 |
841-969 |
Sentence |
denotes |
We also obtained consistent results on surface plasmon resonance analysis involving xCGLs as ligands and xgalectins as analytes. |
| T7 |
841-969 |
Sentence |
denotes |
We also obtained consistent results on surface plasmon resonance analysis involving xCGLs as ligands and xgalectins as analytes. |
| TextSentencer_T8 |
970-1064 |
Sentence |
denotes |
The Kd value of the interaction between xgalectin-VIIa and xCGLs was calculated to be 35.9 nM. |
| T8 |
970-1064 |
Sentence |
denotes |
The Kd value of the interaction between xgalectin-VIIa and xCGLs was calculated to be 35.9 nM. |
| T8 |
970-1064 |
Sentence |
denotes |
The Kd value of the interaction between xgalectin-VIIa and xCGLs was calculated to be 35.9 nM. |
| TextSentencer_T9 |
1065-1317 |
Sentence |
denotes |
The structures of the N-glycans of xCGLs, which were recognized by xgalectin-VIIa, were analyzed by the two-dimensional sugar map method, and three kinds of N-acetyllactosamine type, biantennary N-glycans were identified as the major neutral N-glycans. |
| T9 |
1065-1317 |
Sentence |
denotes |
The structures of the N-glycans of xCGLs, which were recognized by xgalectin-VIIa, were analyzed by the two-dimensional sugar map method, and three kinds of N-acetyllactosamine type, biantennary N-glycans were identified as the major neutral N-glycans. |
| T9 |
1065-1317 |
Sentence |
denotes |
The structures of the N-glycans of xCGLs, which were recognized by xgalectin-VIIa, were analyzed by the two-dimensional sugar map method, and three kinds of N-acetyllactosamine type, biantennary N-glycans were identified as the major neutral N-glycans. |
| TextSentencer_T10 |
1318-1435 |
Sentence |
denotes |
The binding specificity of oligosaccharides for xgalectin-VIIa was analyzed by frontal affinity chromatography (FAC). |
| T10 |
1318-1435 |
Sentence |
denotes |
The binding specificity of oligosaccharides for xgalectin-VIIa was analyzed by frontal affinity chromatography (FAC). |
| T10 |
1318-1435 |
Sentence |
denotes |
The binding specificity of oligosaccharides for xgalectin-VIIa was analyzed by frontal affinity chromatography (FAC). |
| TextSentencer_T11 |
1436-1684 |
Sentence |
denotes |
The oligosaccharide specificity pattern of xgalectin-VIIa was similar to that of the human homolog galectin-3, and it was also shown that the N-acetyllactosamine type, biantennary N-glycans exhibit high affinity for xgalectin-VIIa (Kd = 11 microM). |
| T11 |
1436-1684 |
Sentence |
denotes |
The oligosaccharide specificity pattern of xgalectin-VIIa was similar to that of the human homolog galectin-3, and it was also shown that the N-acetyllactosamine type, biantennary N-glycans exhibit high affinity for xgalectin-VIIa (Kd = 11 microM). |
| T11 |
1436-1684 |
Sentence |
denotes |
The oligosaccharide specificity pattern of xgalectin-VIIa was similar to that of the human homolog galectin-3, and it was also shown that the N-acetyllactosamine type, biantennary N-glycans exhibit high affinity for xgalectin-VIIa (Kd = 11 microM). |
| TextSentencer_T12 |
1685-1927 |
Sentence |
denotes |
These results suggest that xgalectin-VIIa interacts with xCGLs through binding to N-acetyllactosamine type N-glycans and that this interaction might make it possible to organize a lectin network involving members of different lectin families. |
| T12 |
1685-1927 |
Sentence |
denotes |
These results suggest that xgalectin-VIIa interacts with xCGLs through binding to N-acetyllactosamine type N-glycans and that this interaction might make it possible to organize a lectin network involving members of different lectin families. |
| T12 |
1685-1927 |
Sentence |
denotes |
These results suggest that xgalectin-VIIa interacts with xCGLs through binding to N-acetyllactosamine type N-glycans and that this interaction might make it possible to organize a lectin network involving members of different lectin families. |