> top > projects > sentences > docs > PubMed:26911284 > annotations

PubMed:26911284 JSONTXT 40 Projects

Annnotations TAB TSV DIC JSON TextAE-old TextAE

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-100 Sentence denotes Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR.
T1 0-100 Sentence denotes Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR.
TextSentencer_T2 101-300 Sentence denotes Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1-111) and the conserved carbohydrate recognition domain (CRD, residues 112-250).
T2 101-300 Sentence denotes Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1-111) and the conserved carbohydrate recognition domain (CRD, residues 112-250).
TextSentencer_T3 301-373 Sentence denotes The chimera-type galectin interacts with both glycan and peptide motifs.
T3 301-373 Sentence denotes The chimera-type galectin interacts with both glycan and peptide motifs.
TextSentencer_T4 374-493 Sentence denotes Complete (13)C/(15)N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible.
T4 374-493 Sentence denotes Complete (13)C/(15)N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible.
TextSentencer_T5 494-764 Sentence denotes Using two synthetic NT polypeptides covering residues 1-50 and 51-107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn structure from residues 18 to 32 and around PGAYP repeats.
T5 494-764 Sentence denotes Using two synthetic NT polypeptides covering residues 1-50 and 51-107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn structure from residues 18 to 32 and around PGAYP repeats.
TextSentencer_T6 765-1056 Sentence denotes Intramolecular interactions occur between the CRD F-face (the 5-stranded β-sheet behind the canonical carbohydrate-binding 6-stranded β-sheet of the S-face) and NT in full-length galectin-3, with the sequence P(23)GAW(26)…P(37)GASYPGAY(45) defining the primary binding epitope within the NT.
T6 765-1056 Sentence denotes Intramolecular interactions occur between the CRD F-face (the 5-stranded β-sheet behind the canonical carbohydrate-binding 6-stranded β-sheet of the S-face) and NT in full-length galectin-3, with the sequence P(23)GAW(26)…P(37)GASYPGAY(45) defining the primary binding epitope within the NT.
TextSentencer_T7 1057-1163 Sentence denotes Work with designed peptides indicates that the PGAX motif is crucial for self-interactions between NT/CRD.
T7 1057-1163 Sentence denotes Work with designed peptides indicates that the PGAX motif is crucial for self-interactions between NT/CRD.
TextSentencer_T8 1164-1316 Sentence denotes Phosphorylation at position Ser6 (and Ser12) (a physiological modification) and the influence of ligand binding have minimal effect on this interaction.
T8 1164-1316 Sentence denotes Phosphorylation at position Ser6 (and Ser12) (a physiological modification) and the influence of ligand binding have minimal effect on this interaction.
TextSentencer_T9 1317-1470 Sentence denotes Finally, galectin-3 molecules can interact weakly with each other via the F-faces of their CRDs, an interaction that appears to be assisted by their NTs.
T9 1317-1470 Sentence denotes Finally, galectin-3 molecules can interact weakly with each other via the F-faces of their CRDs, an interaction that appears to be assisted by their NTs.
TextSentencer_T10 1471-1597 Sentence denotes Overall, our results add insight to defining binding sites on galectin-3 beyond the canonical contact area for β-galactosides.
T10 1471-1597 Sentence denotes Overall, our results add insight to defining binding sites on galectin-3 beyond the canonical contact area for β-galactosides.