| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-101 |
Sentence |
denotes |
Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor. |
| T1 |
0-101 |
Sentence |
denotes |
Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor. |
| T1 |
0-101 |
Sentence |
denotes |
Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor. |
| TextSentencer_T2 |
102-241 |
Sentence |
denotes |
Midkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. |
| T2 |
102-241 |
Sentence |
denotes |
Midkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. |
| T2 |
102-241 |
Sentence |
denotes |
Midkine (MK), a heparin-binding growth factor, binds strongly to oversulfated structures in chondroitin sulfates (CSs) and heparan sulfate. |
| TextSentencer_T3 |
242-404 |
Sentence |
denotes |
To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. |
| T3 |
242-404 |
Sentence |
denotes |
To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. |
| T3 |
242-404 |
Sentence |
denotes |
To elucidate the carbohydrate structure actually involved in the strong binding, dissected brains from 13-day mouse embryos were incubated with [14C]-glucosamine. |
| TextSentencer_T4 |
405-634 |
Sentence |
denotes |
The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. |
| T4 |
405-634 |
Sentence |
denotes |
The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. |
| T4 |
405-634 |
Sentence |
denotes |
The labeled glycosaminoglycans were fractionated by MK-agarose affinity chromatography to a weakly binding fraction, which was eluted by 0.5 M NaCl, and a strongly binding fraction, which was eluted by higher NaCl concentrations. |
| TextSentencer_T5 |
635-875 |
Sentence |
denotes |
Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. |
| T5 |
635-875 |
Sentence |
denotes |
Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. |
| T5 |
635-875 |
Sentence |
denotes |
Among the unsaturated disaccharides released from the strongly binding fraction by chondroitinase ABC, DeltaDi-diSE with 4,6-disulfated N-acetylgalactosamine accounted for 32.3%, whereas its content was lower in the weakly binding fraction. |
| TextSentencer_T6 |
876-1020 |
Sentence |
denotes |
Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. |
| T6 |
876-1020 |
Sentence |
denotes |
Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. |
| T6 |
876-1020 |
Sentence |
denotes |
Artificial CS-E structure was formed using N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase purified from squid or recombinant human enzyme. |
| TextSentencer_T7 |
1021-1224 |
Sentence |
denotes |
Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. |
| T7 |
1021-1224 |
Sentence |
denotes |
Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. |
| T7 |
1021-1224 |
Sentence |
denotes |
Analysis of the products and their interaction with MK revealed that E units without 3-O-sulfation of glucuronic acid are sufficient for strong binding, provided that they are present as a dense cluster. |
| TextSentencer_T8 |
1225-1431 |
Sentence |
denotes |
Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. |
| T8 |
1225-1431 |
Sentence |
denotes |
Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. |
| T8 |
1225-1431 |
Sentence |
denotes |
Among the sulfated disaccharides released by heparitinase digestion, the trisulfated one, DeltaDiHS-triS, was the most abundant in the strongly binding fraction and was lower in the weakly binding fraction. |
| TextSentencer_T9 |
1432-1593 |
Sentence |
denotes |
Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK. |
| T9 |
1432-1593 |
Sentence |
denotes |
Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK. |
| T9 |
1432-1593 |
Sentence |
denotes |
Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK. |