| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-85 |
Sentence |
denotes |
Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin. |
| T1 |
0-85 |
Sentence |
denotes |
Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin. |
| T2 |
86-245 |
Sentence |
denotes |
L-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. |
| T2 |
86-245 |
Sentence |
denotes |
L-selectin, the leukocyte selectin, mediates the carbohydrate-dependent attachment of circulating leukocytes to endothelium, preceding emigration into tissues. |
| T3 |
246-337 |
Sentence |
denotes |
It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. |
| T3 |
246-337 |
Sentence |
denotes |
It functions in inflammatory leukocyte trafficking and in lymphocyte homing to lymph nodes. |
| T4 |
338-526 |
Sentence |
denotes |
From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. |
| T4 |
338-526 |
Sentence |
denotes |
From previous work, the binding of L-selectin to endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34, requires oligosaccharide sialylation, sulfation, and probably fucosylation. |
| T5 |
527-692 |
Sentence |
denotes |
We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. |
| T5 |
527-692 |
Sentence |
denotes |
We have recently identified a major capping group in GlyCAM-1 as 6' sulfated sialyl Lewis x, a novel structure which potentially satisfies all of these requirements. |
| T6 |
693-924 |
Sentence |
denotes |
In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. |
| T6 |
693-924 |
Sentence |
denotes |
In the present study, we define the complete structure of beta-eliminated chains of GlyCAM-1 using metabolic radiolabeling, plant lectin binding, and glycosidase digestions in conjunction with high pH anion-exchange chromatography. |
| T7 |
925-1169 |
Sentence |
denotes |
The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1-->3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1-->3[GlcNAc beta 1-->6]GalNAc or larger core structures with additional GlcNAc residues. |
| T7 |
925-1169 |
Sentence |
denotes |
The majority of the O-glycans in GlyCAM-1 contain the T-antigen, i.e. Gal beta 1-->3GalNAc, which is incorporated into the core-2 structure, i.e. Gal beta 1-->3[GlcNAc beta 1-->6]GalNAc or larger core structures with additional GlcNAc residues. |
| T8 |
1170-1368 |
Sentence |
denotes |
The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed. |
| T8 |
1170-1368 |
Sentence |
denotes |
The structures of two O-glycans, based on core-2, were determined to be: [sequence: see text] The implications of these structures and more complex O-glycans for binding by L-selectin are discussed. |