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PubMed:12681911 JSONTXT 42 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-117 Sentence denotes On the reaction pathways and determination of transition-state structures for retaining alpha-galactosyltransferases.
T1 0-117 Sentence denotes On the reaction pathways and determination of transition-state structures for retaining alpha-galactosyltransferases.
TextSentencer_T2 118-363 Sentence denotes The catalytic mechanism of retaining glycosyltransferases is not yet completely understood, but one possible mechanism, by analogy with retaining glycosidases, is a double-displacement mechanism via a covalent glycosyl-enzyme intermediate (CGE).
T2 118-363 Sentence denotes The catalytic mechanism of retaining glycosyltransferases is not yet completely understood, but one possible mechanism, by analogy with retaining glycosidases, is a double-displacement mechanism via a covalent glycosyl-enzyme intermediate (CGE).
TextSentencer_T3 364-477 Sentence denotes We have investigated various reaction pathways for this mechanism using non-empirical quantum mechanical methods.
T3 364-477 Sentence denotes We have investigated various reaction pathways for this mechanism using non-empirical quantum mechanical methods.
TextSentencer_T4 478-687 Sentence denotes Because a double-displacement mechanism presumes a reaction happening in two steps, we have used predefined reaction coordinates to calculate the potential energy surface describing each step of the mechanism.
T4 478-687 Sentence denotes Because a double-displacement mechanism presumes a reaction happening in two steps, we have used predefined reaction coordinates to calculate the potential energy surface describing each step of the mechanism.
TextSentencer_T5 688-861 Sentence denotes By investigating several potential candidates to act as a catalytic base, this study attempts to shed some light on the unclear mechanism of the second step of the reaction.
T5 688-861 Sentence denotes By investigating several potential candidates to act as a catalytic base, this study attempts to shed some light on the unclear mechanism of the second step of the reaction.
TextSentencer_T6 862-1018 Sentence denotes All intermediates and transition states on the reaction pathways were characterized using basis sets up to the DFT/B3LYP/6-311++G**//DFT/B3LYP/6-31G* level.
T6 862-1018 Sentence denotes All intermediates and transition states on the reaction pathways were characterized using basis sets up to the DFT/B3LYP/6-311++G**//DFT/B3LYP/6-31G* level.
TextSentencer_T7 1019-1146 Sentence denotes Reaction pathways and structural changes were compared with the results previously obtained for inverting glycosyltransferases.
T7 1019-1146 Sentence denotes Reaction pathways and structural changes were compared with the results previously obtained for inverting glycosyltransferases.
TextSentencer_T8 1147-1325 Sentence denotes The outcome of this study indicates, that among the reaction models investigated, the energetically favorable one is also the most plausible given the existing experimental data.
T8 1147-1325 Sentence denotes The outcome of this study indicates, that among the reaction models investigated, the energetically favorable one is also the most plausible given the existing experimental data.
TextSentencer_T9 1326-1483 Sentence denotes This model requires the presence of only one catalytic acid in the active site with the UDP functioning as a general base in the second step of the reaction.
T9 1326-1483 Sentence denotes This model requires the presence of only one catalytic acid in the active site with the UDP functioning as a general base in the second step of the reaction.
TextSentencer_T10 1484-1649 Sentence denotes This mechanism is in agreement with both kinetic data in the literature and the description of X-ray structures of retaining glycosyltransferases solved up to today.
T10 1484-1649 Sentence denotes This mechanism is in agreement with both kinetic data in the literature and the description of X-ray structures of retaining glycosyltransferases solved up to today.