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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-94 Sentence denotes Structural glycobiology of heparin dynamics on the exosite 2 of coagulation cascade proteases:
T1 0-94 Sentence denotes Structural glycobiology of heparin dynamics on the exosite 2 of coagulation cascade proteases:
T1 0-94 Sentence denotes Structural glycobiology of heparin dynamics on the exosite 2 of coagulation cascade proteases:
TextSentencer_T2 95-155 Sentence denotes Implications for glycosaminoglycans antithrombotic activity.
T2 95-155 Sentence denotes Implications for glycosaminoglycans antithrombotic activity.
T2 95-155 Sentence denotes Implications for glycosaminoglycans antithrombotic activity.
TextSentencer_T3 156-303 Sentence denotes fIIa and fXa are two of the main targets of antithrombin, a serine proteases inhibitor that plays a major role in the regulation of blood clotting.
T3 156-303 Sentence denotes fIIa and fXa are two of the main targets of antithrombin, a serine proteases inhibitor that plays a major role in the regulation of blood clotting.
T3 156-303 Sentence denotes fIIa and fXa are two of the main targets of antithrombin, a serine proteases inhibitor that plays a major role in the regulation of blood clotting.
TextSentencer_T4 304-503 Sentence denotes The formation of ternary complexes between such molecules and glycosaminoglycans, as heparin, is the main path for inhibiting those enzymes, which may occur through two distinct mechanisms of action.
T4 304-503 Sentence denotes The formation of ternary complexes between such molecules and glycosaminoglycans, as heparin, is the main path for inhibiting those enzymes, which may occur through two distinct mechanisms of action.
T4 304-503 Sentence denotes The formation of ternary complexes between such molecules and glycosaminoglycans, as heparin, is the main path for inhibiting those enzymes, which may occur through two distinct mechanisms of action.
TextSentencer_T5 504-765 Sentence denotes While these serine proteases present distinct susceptibilities to these paths, in which fIIa demands an interaction with heparin, neither the molecular basis of this differential inhibition nor the role of fIIa glycosylation on this process is fully understood.
T5 504-765 Sentence denotes While these serine proteases present distinct susceptibilities to these paths, in which fIIa demands an interaction with heparin, neither the molecular basis of this differential inhibition nor the role of fIIa glycosylation on this process is fully understood.
T5 504-765 Sentence denotes While these serine proteases present distinct susceptibilities to these paths, in which fIIa demands an interaction with heparin, neither the molecular basis of this differential inhibition nor the role of fIIa glycosylation on this process is fully understood.
TextSentencer_T6 766-955 Sentence denotes Thus, the present work evaluated through molecular dynamics simulations the effects of glycosylation on fIIa and the consequences of heparin binding to both proteases function and dynamics.
T6 766-955 Sentence denotes Thus, the present work evaluated through molecular dynamics simulations the effects of glycosylation on fIIa and the consequences of heparin binding to both proteases function and dynamics.
T6 766-955 Sentence denotes Thus, the present work evaluated through molecular dynamics simulations the effects of glycosylation on fIIa and the consequences of heparin binding to both proteases function and dynamics.
TextSentencer_T7 956-1159 Sentence denotes Based on the obtained data, fIIa N-linked glycan promoted an increase in the active site pocket size by stabilizing regions that encircle it, while heparin binding was observed to reverse such an effect.
T7 956-1159 Sentence denotes Based on the obtained data, fIIa N-linked glycan promoted an increase in the active site pocket size by stabilizing regions that encircle it, while heparin binding was observed to reverse such an effect.
T7 956-1159 Sentence denotes Based on the obtained data, fIIa N-linked glycan promoted an increase in the active site pocket size by stabilizing regions that encircle it, while heparin binding was observed to reverse such an effect.
TextSentencer_T8 1160-1320 Sentence denotes Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes.
T8 1160-1320 Sentence denotes Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes.
T8 1160-1320 Sentence denotes Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes.
TextSentencer_T9 1321-1454 Sentence denotes Finally, the enzymes catalytic triad organization was disrupted due to a strong glycosaminoglycan binding to the proteases exosite 2.
T9 1321-1454 Sentence denotes Finally, the enzymes catalytic triad organization was disrupted due to a strong glycosaminoglycan binding to the proteases exosite 2.
T9 1321-1454 Sentence denotes Finally, the enzymes catalytic triad organization was disrupted due to a strong glycosaminoglycan binding to the proteases exosite 2.
TextSentencer_T10 1455-1693 Sentence denotes Such data support an atomic-level explanation for the higher inhibition constant of the antithrombin-heparin complex over fIIa than fXa, as well as for the different susceptibilities of those enzymes for antithrombin mechanisms of action.
T10 1455-1693 Sentence denotes Such data support an atomic-level explanation for the higher inhibition constant of the antithrombin-heparin complex over fIIa than fXa, as well as for the different susceptibilities of those enzymes for antithrombin mechanisms of action.
T10 1455-1693 Sentence denotes Such data support an atomic-level explanation for the higher inhibition constant of the antithrombin-heparin complex over fIIa than fXa, as well as for the different susceptibilities of those enzymes for antithrombin mechanisms of action.