| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-102 |
Sentence |
denotes |
Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. |
| T1 |
0-102 |
Sentence |
denotes |
Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. |
| T1 |
0-102 |
Sentence |
denotes |
Functional and structural bases of a cysteine-less mutant as a long-lasting substitute for galectin-1. |
| TextSentencer_T2 |
103-290 |
Sentence |
denotes |
Galectin-1 (Gal-1), a member of the beta-galactoside-binding animal lectin family, has a wide range of biological activities, which makes it an attractive target for medical applications. |
| T2 |
103-290 |
Sentence |
denotes |
Galectin-1 (Gal-1), a member of the beta-galactoside-binding animal lectin family, has a wide range of biological activities, which makes it an attractive target for medical applications. |
| T2 |
103-290 |
Sentence |
denotes |
Galectin-1 (Gal-1), a member of the beta-galactoside-binding animal lectin family, has a wide range of biological activities, which makes it an attractive target for medical applications. |
| TextSentencer_T3 |
291-418 |
Sentence |
denotes |
Unlike other galectins, Gal-1 is susceptible to oxidation at cysteine residues, which is troublesome for in vitro/vivo studies. |
| T3 |
291-418 |
Sentence |
denotes |
Unlike other galectins, Gal-1 is susceptible to oxidation at cysteine residues, which is troublesome for in vitro/vivo studies. |
| T3 |
291-418 |
Sentence |
denotes |
Unlike other galectins, Gal-1 is susceptible to oxidation at cysteine residues, which is troublesome for in vitro/vivo studies. |
| TextSentencer_T4 |
419-558 |
Sentence |
denotes |
To overcome this problem, we prepared a cysteine-less mutant of Gal-1 (CSGal-1) by substituting all cysteine residues with serine residues. |
| T4 |
419-558 |
Sentence |
denotes |
To overcome this problem, we prepared a cysteine-less mutant of Gal-1 (CSGal-1) by substituting all cysteine residues with serine residues. |
| T4 |
419-558 |
Sentence |
denotes |
To overcome this problem, we prepared a cysteine-less mutant of Gal-1 (CSGal-1) by substituting all cysteine residues with serine residues. |
| TextSentencer_T5 |
559-871 |
Sentence |
denotes |
In the case of wild-type Gal-1, the formation of covalent dimers/oligomers was evident after 10 days of storage in the absence of a reducing agent with a concomitant decrease in hemagglutination activity, while CSGal-1 did not form multimers and retained full hemagglutination activity after 400 days of storage. |
| T5 |
559-871 |
Sentence |
denotes |
In the case of wild-type Gal-1, the formation of covalent dimers/oligomers was evident after 10 days of storage in the absence of a reducing agent with a concomitant decrease in hemagglutination activity, while CSGal-1 did not form multimers and retained full hemagglutination activity after 400 days of storage. |
| T5 |
559-871 |
Sentence |
denotes |
In the case of wild-type Gal-1, the formation of covalent dimers/oligomers was evident after 10 days of storage in the absence of a reducing agent with a concomitant decrease in hemagglutination activity, while CSGal-1 did not form multimers and retained full hemagglutination activity after 400 days of storage. |
| TextSentencer_T6 |
872-1026 |
Sentence |
denotes |
Frontal affinity chromatography showed that the sugar-binding specificity and affinity of Gal-1 for model glycans were barely affected by the mutagenesis. |
| T6 |
872-1026 |
Sentence |
denotes |
Frontal affinity chromatography showed that the sugar-binding specificity and affinity of Gal-1 for model glycans were barely affected by the mutagenesis. |
| T6 |
872-1026 |
Sentence |
denotes |
Frontal affinity chromatography showed that the sugar-binding specificity and affinity of Gal-1 for model glycans were barely affected by the mutagenesis. |
| TextSentencer_T7 |
1027-1154 |
Sentence |
denotes |
Gal-1 is known to induce cell signaling leading to an increase in the intracytoplasmic calcium concentration and to cell death. |
| T7 |
1027-1154 |
Sentence |
denotes |
Gal-1 is known to induce cell signaling leading to an increase in the intracytoplasmic calcium concentration and to cell death. |
| T7 |
1027-1154 |
Sentence |
denotes |
Gal-1 is known to induce cell signaling leading to an increase in the intracytoplasmic calcium concentration and to cell death. |
| TextSentencer_T8 |
1155-1310 |
Sentence |
denotes |
CSGal-1 is also capable of inducing calcium flux and growth inhibition in Jurkat cells, which are comparable to or more potent than those induced by Gal-1. |
| T8 |
1155-1310 |
Sentence |
denotes |
CSGal-1 is also capable of inducing calcium flux and growth inhibition in Jurkat cells, which are comparable to or more potent than those induced by Gal-1. |
| T8 |
1155-1310 |
Sentence |
denotes |
CSGal-1 is also capable of inducing calcium flux and growth inhibition in Jurkat cells, which are comparable to or more potent than those induced by Gal-1. |
| TextSentencer_T9 |
1311-1382 |
Sentence |
denotes |
The X-ray structure of the CSGal-1/lactose complex has been determined. |
| T9 |
1311-1382 |
Sentence |
denotes |
The X-ray structure of the CSGal-1/lactose complex has been determined. |
| T9 |
1311-1382 |
Sentence |
denotes |
The X-ray structure of the CSGal-1/lactose complex has been determined. |
| TextSentencer_T10 |
1383-1594 |
Sentence |
denotes |
The structure of CSGal-1 is almost identical to that of wild-type human Gal-1, showing that the amino acid substitutions do not affect the overall structure or carbohydrate-binding site structure of the protein. |
| T10 |
1383-1594 |
Sentence |
denotes |
The structure of CSGal-1 is almost identical to that of wild-type human Gal-1, showing that the amino acid substitutions do not affect the overall structure or carbohydrate-binding site structure of the protein. |
| T10 |
1383-1594 |
Sentence |
denotes |
The structure of CSGal-1 is almost identical to that of wild-type human Gal-1, showing that the amino acid substitutions do not affect the overall structure or carbohydrate-binding site structure of the protein. |
| TextSentencer_T11 |
1595-1674 |
Sentence |
denotes |
These results indicate that CSGal-1 can serve as a stable substitute for Gal-1. |
| T11 |
1595-1674 |
Sentence |
denotes |
These results indicate that CSGal-1 can serve as a stable substitute for Gal-1. |
| T11 |
1595-1674 |
Sentence |
denotes |
These results indicate that CSGal-1 can serve as a stable substitute for Gal-1. |