| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-172 |
Sentence |
denotes |
Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation. |
| T1 |
0-172 |
Sentence |
denotes |
Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation. |
| T1 |
0-172 |
Sentence |
denotes |
Interaction profile of galectin-5 with free saccharides and mammalian glycoproteins: probing its fine specificity and the effect of naturally clustered ligand presentation. |
| TextSentencer_T2 |
173-285 |
Sentence |
denotes |
Cell-surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. |
| T2 |
173-285 |
Sentence |
denotes |
Cell-surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. |
| T2 |
173-285 |
Sentence |
denotes |
Cell-surface glycans are functional docking sites for tissue lectins such as the members of the galectin family. |
| TextSentencer_T3 |
286-409 |
Sentence |
denotes |
This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. |
| T3 |
286-409 |
Sentence |
denotes |
This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. |
| T3 |
286-409 |
Sentence |
denotes |
This interaction triggers a wide variety of responses; hence, there is a keen interest in defining its structural features. |
| TextSentencer_T4 |
410-584 |
Sentence |
denotes |
Toward this aim, we have used enzyme-linked lectinosorbent (ELLSA) and inhibition assays with the prototype rat galectin-5 and panels of free saccharides and glycoconjugates. |
| T4 |
410-584 |
Sentence |
denotes |
Toward this aim, we have used enzyme-linked lectinosorbent (ELLSA) and inhibition assays with the prototype rat galectin-5 and panels of free saccharides and glycoconjugates. |
| T4 |
410-584 |
Sentence |
denotes |
Toward this aim, we have used enzyme-linked lectinosorbent (ELLSA) and inhibition assays with the prototype rat galectin-5 and panels of free saccharides and glycoconjugates. |
| TextSentencer_T5 |
585-786 |
Sentence |
denotes |
Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Galbeta1-3/4GlcNAc (I/II) and multiantennary N-glycans with II termini. |
| T5 |
585-786 |
Sentence |
denotes |
Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Galbeta1-3/4GlcNAc (I/II) and multiantennary N-glycans with II termini. |
| T5 |
585-786 |
Sentence |
denotes |
Among 45 natural glycans tested for lectin binding, galectin-5 reacted best with glycoproteins (gps) presenting a high density of Galbeta1-3/4GlcNAc (I/II) and multiantennary N-glycans with II termini. |
| TextSentencer_T6 |
787-997 |
Sentence |
denotes |
Their reactivities, on a nanogram basis, were up to 4.3 x 10(2), 3.2 x 10(2), 2.5 x 10(2), and 1.7 x 10(4) times higher than monomeric Galbeta1-3/4GlcNAc (I/II), triantennary-II (Tri-II), and Gal, respectively. |
| T6 |
787-997 |
Sentence |
denotes |
Their reactivities, on a nanogram basis, were up to 4.3 x 10(2), 3.2 x 10(2), 2.5 x 10(2), and 1.7 x 10(4) times higher than monomeric Galbeta1-3/4GlcNAc (I/II), triantennary-II (Tri-II), and Gal, respectively. |
| T6 |
787-997 |
Sentence |
denotes |
Their reactivities, on a nanogram basis, were up to 4.3 x 10(2), 3.2 x 10(2), 2.5 x 10(2), and 1.7 x 10(4) times higher than monomeric Galbeta1-3/4GlcNAc (I/II), triantennary-II (Tri-II), and Gal, respectively. |
| TextSentencer_T7 |
998-1114 |
Sentence |
denotes |
Galectin-5 also bound well to several blood group type B (Galalpha1-3Gal)- and A (GalNAcalpha1-3Gal)-containing gps. |
| T7 |
998-1114 |
Sentence |
denotes |
Galectin-5 also bound well to several blood group type B (Galalpha1-3Gal)- and A (GalNAcalpha1-3Gal)-containing gps. |
| T7 |
998-1114 |
Sentence |
denotes |
Galectin-5 also bound well to several blood group type B (Galalpha1-3Gal)- and A (GalNAcalpha1-3Gal)-containing gps. |
| TextSentencer_T8 |
1115-1214 |
Sentence |
denotes |
It reacted weakly or not at all with tumor-associated Tn (GalNAcalpha1-Ser/Thr) and sialylated gps. |
| T8 |
1115-1214 |
Sentence |
denotes |
It reacted weakly or not at all with tumor-associated Tn (GalNAcalpha1-Ser/Thr) and sialylated gps. |
| T8 |
1115-1214 |
Sentence |
denotes |
It reacted weakly or not at all with tumor-associated Tn (GalNAcalpha1-Ser/Thr) and sialylated gps. |
| TextSentencer_T9 |
1215-1449 |
Sentence |
denotes |
Among the mono-, di-, and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Galalpha1-3Gal beta1-4GlcNAc), B-active IIbeta1-3L (Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc), and Tri-II were the best. |
| T9 |
1215-1449 |
Sentence |
denotes |
Among the mono-, di-, and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Galalpha1-3Gal beta1-4GlcNAc), B-active IIbeta1-3L (Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc), and Tri-II were the best. |
| T9 |
1215-1449 |
Sentence |
denotes |
Among the mono-, di-, and oligosaccharides and mammalian glycoconjugates tested, blood group B-active II (Galalpha1-3Gal beta1-4GlcNAc), B-active IIbeta1-3L (Galalpha1-3Galbeta1-4GlcNAc beta1-3Galbeta1-4Glc), and Tri-II were the best. |
| TextSentencer_T10 |
1450-2150 |
Sentence |
denotes |
It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 > or = Galbeta1-3 > Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. |
| T10 |
1450-2150 |
Sentence |
denotes |
It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 > or = Galbeta1-3 > Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. |
| T10 |
1450-2150 |
Sentence |
denotes |
It is concluded that (1) Galbeta1-3/4GlcNAc and other Galbeta1-related oligosaccharides with alpha1-3 extensions are essential for binding, their polyvalent form in cellular glycoconjugates being a key recognition force for galectin-5; (2) the combining site of galectin-5 appears to be of a shallow-groove type sufficiently large to accommodate a substituted beta-galactoside, especially with alpha-anomeric extension at the non-reducing end (e.g., human blood group B-active II and B-active IIbeta1-3L); (3) the preference within beta-anomeric positioning is Galbeta1-4 > or = Galbeta1-3 > Galbeta1-6; and (4) hydrophobic interactions in the vicinity of the core galactose unit can enhance binding. |
| TextSentencer_T11 |
2151-2324 |
Sentence |
denotes |
These results are important for the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications. |
| T11 |
2151-2324 |
Sentence |
denotes |
These results are important for the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications. |
| T11 |
2151-2324 |
Sentence |
denotes |
These results are important for the systematic comparison of ligand selection in this family of adhesion/growth-regulatory effectors with potential for medical applications. |