| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-98 |
Sentence |
denotes |
Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells. |
| T1 |
0-98 |
Sentence |
denotes |
Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells. |
| TextSentencer_T2 |
99-227 |
Sentence |
denotes |
Galectins are implicated in a large variety of biological functions, many of which depend on their carbohydrate-binding ability. |
| T2 |
99-227 |
Sentence |
denotes |
Galectins are implicated in a large variety of biological functions, many of which depend on their carbohydrate-binding ability. |
| TextSentencer_T3 |
228-428 |
Sentence |
denotes |
Fifteen members of the family have been identified in vertebrates based on binding to galactose (Gal) that is mediated by one or two, evolutionarily conserved, carbohydrate-recognition domains (CRDs). |
| T3 |
228-428 |
Sentence |
denotes |
Fifteen members of the family have been identified in vertebrates based on binding to galactose (Gal) that is mediated by one or two, evolutionarily conserved, carbohydrate-recognition domains (CRDs). |
| TextSentencer_T4 |
429-564 |
Sentence |
denotes |
Variations in glycan structures expressed on glycoconjugates at the cell surface may, therefore, affect galectin binding and functions. |
| T4 |
429-564 |
Sentence |
denotes |
Variations in glycan structures expressed on glycoconjugates at the cell surface may, therefore, affect galectin binding and functions. |
| TextSentencer_T5 |
565-891 |
Sentence |
denotes |
To identify roles for different glycans in the binding of the three types of mammalian galectins to cells, we performed fluorescence cytometry at 4 degrees C with recombinant rat galectin-1, human galectin-3, and three forms of human galectin-8, to Chinese hamster ovary (CHO) cells and 12 different CHO glycosylation mutants. |
| T5 |
565-891 |
Sentence |
denotes |
To identify roles for different glycans in the binding of the three types of mammalian galectins to cells, we performed fluorescence cytometry at 4 degrees C with recombinant rat galectin-1, human galectin-3, and three forms of human galectin-8, to Chinese hamster ovary (CHO) cells and 12 different CHO glycosylation mutants. |
| TextSentencer_T6 |
892-987 |
Sentence |
denotes |
All galectin species bound to parent CHO cells and binding was inhibited >90% by 0.2 M lactose. |
| T6 |
892-987 |
Sentence |
denotes |
All galectin species bound to parent CHO cells and binding was inhibited >90% by 0.2 M lactose. |
| TextSentencer_T7 |
988-1084 |
Sentence |
denotes |
Galectin-8 isoforms with either a long or a short inter-CRD linker bound similarly to CHO cells. |
| T7 |
988-1084 |
Sentence |
denotes |
Galectin-8 isoforms with either a long or a short inter-CRD linker bound similarly to CHO cells. |
| TextSentencer_T8 |
1085-1257 |
Sentence |
denotes |
However, a truncated form of galectin-8 containing only the N-terminal CRD bound only weakly to CHO cells and the C-terminal galectin-8 CRD exhibited extremely low binding. |
| T8 |
1085-1257 |
Sentence |
denotes |
However, a truncated form of galectin-8 containing only the N-terminal CRD bound only weakly to CHO cells and the C-terminal galectin-8 CRD exhibited extremely low binding. |
| TextSentencer_T9 |
1258-1504 |
Sentence |
denotes |
Binding of the galectins to the different CHO glycosylation mutants revealed that complex N-glycans are the major ligands for each galectin except the N-terminal CRD of galectins-8, and also identified some fine differences in glycan recognition. |
| T9 |
1258-1504 |
Sentence |
denotes |
Binding of the galectins to the different CHO glycosylation mutants revealed that complex N-glycans are the major ligands for each galectin except the N-terminal CRD of galectins-8, and also identified some fine differences in glycan recognition. |
| TextSentencer_T10 |
1505-1690 |
Sentence |
denotes |
Interestingly, increased binding of galectin-1 at 4 degrees C correlated with increased propidium iodide (PI) uptake, whereas galectin-3 or -8 binding did not induce permeability to PI. |
| T10 |
1505-1690 |
Sentence |
denotes |
Interestingly, increased binding of galectin-1 at 4 degrees C correlated with increased propidium iodide (PI) uptake, whereas galectin-3 or -8 binding did not induce permeability to PI. |
| TextSentencer_T11 |
1691-1974 |
Sentence |
denotes |
The CHO glycosylation mutants with various repertoires of cell surface glycans are a useful tool for investigating galectin-cell interactions as they present complex and simple glycans in a natural mixture of multivalent protein and lipid glycoconjugates anchored in a cell membrane. |
| T11 |
1691-1974 |
Sentence |
denotes |
The CHO glycosylation mutants with various repertoires of cell surface glycans are a useful tool for investigating galectin-cell interactions as they present complex and simple glycans in a natural mixture of multivalent protein and lipid glycoconjugates anchored in a cell membrane. |