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PubMed:11744633 JSONTXT 66 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-101 Sentence denotes Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.
T1 0-101 Sentence denotes Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.
T1 0-101 Sentence denotes Minimal requirements for the binding of selectin ligands to a C-type carbohydrate-recognition domain.
TextSentencer_T2 102-222 Sentence denotes The C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures.
T2 102-222 Sentence denotes The C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures.
T2 102-222 Sentence denotes The C-type carbohydrate-recognition domains of E-selectin and rat serum mannose-binding protein have similar structures.
TextSentencer_T3 223-557 Sentence denotes Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues.
T3 223-557 Sentence denotes Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues.
T3 223-557 Sentence denotes Selectin/mannose-binding protein chimeras created by transfer of key sequences from E-selectin into mannose-binding protein have previously been shown to bind the selectin ligand sialyl-Lewis(X) through a Ca(2+)-dependent subsite, common to many C-type lectins, and an accessory site containing positively charged amino acid residues.
TextSentencer_T4 558-896 Sentence denotes Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different.
T4 558-896 Sentence denotes Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different.
T4 558-896 Sentence denotes Further characterization of these chimeras as well as analysis of novel constructs containing additional regions of E-selectin demonstrate that selectin-like interaction with sialyl-Lewis(X) can be faithfully reproduced even though structural evidence indicates that the mechanisms of binding to E-selectin and the chimeras are different.
TextSentencer_T5 897-1119 Sentence denotes Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding.
T5 897-1119 Sentence denotes Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding.
T5 897-1119 Sentence denotes Selectin-like binding to the nonfucosylated sulfatide and sulfoglucuronyl glycolipids can also be reproduced with selectin/mannose-binding protein chimeras that contain the two subsites involved in sialyl-Lewis(X) binding.
TextSentencer_T6 1120-1383 Sentence denotes These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite.
T6 1120-1383 Sentence denotes These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite.
T6 1120-1383 Sentence denotes These results indicate that binding of structurally distinct anionic glycans to C-type carbohydrate-recognition domains can be mediated by the Ca(2+)-dependent subsite in combination with a positively charged region that forms an ionic strength-sensitive subsite.