Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-105 |
Sentence |
denotes |
Mammalian cell ganglioside-binding specificities of E. coli enterotoxins LT-IIb and variant LT-IIb(T13I). |
T1 |
0-105 |
Sentence |
denotes |
Mammalian cell ganglioside-binding specificities of E. coli enterotoxins LT-IIb and variant LT-IIb(T13I). |
T2 |
106-250 |
Sentence |
denotes |
LT-IIb, a type II heat-labile enterotoxin of Escherichia coli, is a potent immunologic adjuvant with high affinity binding for ganglioside GD1a. |
T2 |
106-250 |
Sentence |
denotes |
LT-IIb, a type II heat-labile enterotoxin of Escherichia coli, is a potent immunologic adjuvant with high affinity binding for ganglioside GD1a. |
T3 |
251-369 |
Sentence |
denotes |
Earlier study suggested that LT-IIb bound preferentially to the terminal sugar sequence NeuAcalpha2-3Galbeta1-3GalNAc. |
T3 |
251-369 |
Sentence |
denotes |
Earlier study suggested that LT-IIb bound preferentially to the terminal sugar sequence NeuAcalpha2-3Galbeta1-3GalNAc. |
T4 |
370-450 |
Sentence |
denotes |
However, studies in our laboratory suggested a less restrictive binding epitope. |
T4 |
370-450 |
Sentence |
denotes |
However, studies in our laboratory suggested a less restrictive binding epitope. |
T5 |
451-613 |
Sentence |
denotes |
LT-IIb(T13I), an LT-IIb variant, engineered by a single isoleucine-threonine substitution, retains biological activity, but with less robust inflammatory effects. |
T5 |
451-613 |
Sentence |
denotes |
LT-IIb(T13I), an LT-IIb variant, engineered by a single isoleucine-threonine substitution, retains biological activity, but with less robust inflammatory effects. |
T6 |
614-823 |
Sentence |
denotes |
We theorized that LT-IIb has a less restrictive binding epitope than previously proposed and that immunologic differences between LT-IIb and LT-IIb (T13I) correlate with subtle ganglioside binding differences. |
T6 |
614-823 |
Sentence |
denotes |
We theorized that LT-IIb has a less restrictive binding epitope than previously proposed and that immunologic differences between LT-IIb and LT-IIb (T13I) correlate with subtle ganglioside binding differences. |
T7 |
824-1067 |
Sentence |
denotes |
Ganglioside binding epitopes, determined by affinity overlay immunoblotting and enzymatic degradation of ganglioside components of RAW264.7 macrophages, indicated that LT-IIb bound to a broader array of gangliosides than previously recognized. |
T7 |
824-1067 |
Sentence |
denotes |
Ganglioside binding epitopes, determined by affinity overlay immunoblotting and enzymatic degradation of ganglioside components of RAW264.7 macrophages, indicated that LT-IIb bound to a broader array of gangliosides than previously recognized. |
T8 |
1068-1162 |
Sentence |
denotes |
Each possessed NeuAcalpha2-3Galbeta1-3GalNAc, although not necessarily as a terminal sequence. |
T8 |
1068-1162 |
Sentence |
denotes |
Each possessed NeuAcalpha2-3Galbeta1-3GalNAc, although not necessarily as a terminal sequence. |
T9 |
1163-1287 |
Sentence |
denotes |
Rather, each had a requisite terminal or penultimate single sialic acid and binding was independent of ceramide composition. |
T9 |
1163-1287 |
Sentence |
denotes |
Rather, each had a requisite terminal or penultimate single sialic acid and binding was independent of ceramide composition. |
T10 |
1288-1462 |
Sentence |
denotes |
RAW264.7 enterotoxin-binding and non-binding ganglioside epitopes were definitively identified as GD1a and GM1a, respectively, by enzymatic degradation and mass spectroscopy. |
T10 |
1288-1462 |
Sentence |
denotes |
RAW264.7 enterotoxin-binding and non-binding ganglioside epitopes were definitively identified as GD1a and GM1a, respectively, by enzymatic degradation and mass spectroscopy. |
T11 |
1463-1679 |
Sentence |
denotes |
Affinity overlay immunoblots, constructed to the diverse array of known ganglioside structures of murine peritoneal macrophages, established that LT-IIb bound NeuAc- and NeuGc-gangliosides with nearly equal affinity. |
T11 |
1463-1679 |
Sentence |
denotes |
Affinity overlay immunoblots, constructed to the diverse array of known ganglioside structures of murine peritoneal macrophages, established that LT-IIb bound NeuAc- and NeuGc-gangliosides with nearly equal affinity. |
T12 |
1680-1782 |
Sentence |
denotes |
However, LT-IIb(T13I) exhibited enhanced affinity for NeuGc-gangliosides and more restrictive binding. |
T12 |
1680-1782 |
Sentence |
denotes |
However, LT-IIb(T13I) exhibited enhanced affinity for NeuGc-gangliosides and more restrictive binding. |
T13 |
1783-1969 |
Sentence |
denotes |
These studies further elucidate the binding epitope for LT-IIb and suggest that the diminished inflammatory activity of LT-IIb(T13I) is mediated by a subtle shift in ganglioside binding. |
T13 |
1783-1969 |
Sentence |
denotes |
These studies further elucidate the binding epitope for LT-IIb and suggest that the diminished inflammatory activity of LT-IIb(T13I) is mediated by a subtle shift in ganglioside binding. |
T14 |
1970-2072 |
Sentence |
denotes |
These studies underscore the high degree of specificity required for ganglioside-protein interactions. |
T14 |
1970-2072 |
Sentence |
denotes |
These studies underscore the high degree of specificity required for ganglioside-protein interactions. |