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PubMed:24451374 JSONTXT 33 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-123 Sentence denotes Vaccinia viral protein A27 is anchored to the viral membrane via a cooperative interaction with viral membrane protein A17.
T1 0-123 Sentence denotes Vaccinia viral protein A27 is anchored to the viral membrane via a cooperative interaction with viral membrane protein A17.
T2 124-245 Sentence denotes The vaccinia viral protein A27 in mature viruses specifically interacts with heparan sulfate for cell surface attachment.
T2 124-245 Sentence denotes The vaccinia viral protein A27 in mature viruses specifically interacts with heparan sulfate for cell surface attachment.
T3 246-421 Sentence denotes In addition, A27 associates with the viral membrane protein A17 to anchor to the viral membrane; however, the specific interaction between A27 and A17 remains largely unclear.
T3 246-421 Sentence denotes In addition, A27 associates with the viral membrane protein A17 to anchor to the viral membrane; however, the specific interaction between A27 and A17 remains largely unclear.
T4 422-640 Sentence denotes To uncover the active binding sites and the underlying binding mechanism, we expressed and purified the N-terminal (18-50 residues) and C-terminal (162-203 residues) fragments of A17, which are denoted A17-N and A17-C.
T4 422-640 Sentence denotes To uncover the active binding sites and the underlying binding mechanism, we expressed and purified the N-terminal (18-50 residues) and C-terminal (162-203 residues) fragments of A17, which are denoted A17-N and A17-C.
T5 641-921 Sentence denotes Through surface plasmon resonance, the binding affinity of A27/A17-N (KA = 3.40 × 10(8) m(-1)) was determined to be approximately 3 orders of magnitude stronger than that of A27/A17-C (KA = 3.40 × 10(5) m(-1)), indicating that A27 prefers to interact with A17-N rather than A17-C.
T5 641-921 Sentence denotes Through surface plasmon resonance, the binding affinity of A27/A17-N (KA = 3.40 × 10(8) m(-1)) was determined to be approximately 3 orders of magnitude stronger than that of A27/A17-C (KA = 3.40 × 10(5) m(-1)), indicating that A27 prefers to interact with A17-N rather than A17-C.
T6 922-1159 Sentence denotes Despite the disordered nature of A17-N, the A27-A17 interaction is mediated by a specific and cooperative binding mechanism that includes two active binding sites, namely (32)SFMPK(36) (denoted as F1 binding) and (20)LDKDLFTEEQ(29) (F2).
T6 922-1159 Sentence denotes Despite the disordered nature of A17-N, the A27-A17 interaction is mediated by a specific and cooperative binding mechanism that includes two active binding sites, namely (32)SFMPK(36) (denoted as F1 binding) and (20)LDKDLFTEEQ(29) (F2).
T7 1160-1276 Sentence denotes Further analysis showed that F1 has stronger binding affinity and is more resistant to acidic conditions than is F2.
T7 1160-1276 Sentence denotes Further analysis showed that F1 has stronger binding affinity and is more resistant to acidic conditions than is F2.
T8 1277-1530 Sentence denotes Furthermore, A27 mutant proteins that retained partial activity to interact with the F1 and F2 sites of the A17 protein were packaged into mature virus particles at a reduced level, demonstrating that the F1/F2 interaction plays a critical role in vivo.
T8 1277-1530 Sentence denotes Furthermore, A27 mutant proteins that retained partial activity to interact with the F1 and F2 sites of the A17 protein were packaged into mature virus particles at a reduced level, demonstrating that the F1/F2 interaction plays a critical role in vivo.
T9 1531-1685 Sentence denotes Using these results in combination with site-directed mutagenesis data, we established a computer model to explain the specific A27-A17 binding mechanism.
T9 1531-1685 Sentence denotes Using these results in combination with site-directed mutagenesis data, we established a computer model to explain the specific A27-A17 binding mechanism.