| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-147 |
Sentence |
denotes |
Non-conserved, S-nitrosylated cysteines in glypican-1 react with N-unsubstituted glucosamines in heparan sulfate and catalyze deaminative cleavage. |
| T1 |
0-147 |
Sentence |
denotes |
Non-conserved, S-nitrosylated cysteines in glypican-1 react with N-unsubstituted glucosamines in heparan sulfate and catalyze deaminative cleavage. |
| T1 |
0-147 |
Sentence |
denotes |
Non-conserved, S-nitrosylated cysteines in glypican-1 react with N-unsubstituted glucosamines in heparan sulfate and catalyze deaminative cleavage. |
| TextSentencer_T2 |
148-372 |
Sentence |
denotes |
The membrane lipid-anchored glypicans (Gpcs) [heparan sulfate (HS) proteoglycans (PGs)] are present in both vertebrates and invertebrates and serve as important modulators of growth factors and morphogens during development. |
| T2 |
148-372 |
Sentence |
denotes |
The membrane lipid-anchored glypicans (Gpcs) [heparan sulfate (HS) proteoglycans (PGs)] are present in both vertebrates and invertebrates and serve as important modulators of growth factors and morphogens during development. |
| T2 |
148-372 |
Sentence |
denotes |
The membrane lipid-anchored glypicans (Gpcs) [heparan sulfate (HS) proteoglycans (PGs)] are present in both vertebrates and invertebrates and serve as important modulators of growth factors and morphogens during development. |
| TextSentencer_T3 |
373-565 |
Sentence |
denotes |
Their core proteins are similar and consist of a large N-terminal domain comprising 14 evolutionary conserved cysteines and a C-terminal stalk carrying the HS side chains and the lipid anchor. |
| T3 |
373-565 |
Sentence |
denotes |
Their core proteins are similar and consist of a large N-terminal domain comprising 14 evolutionary conserved cysteines and a C-terminal stalk carrying the HS side chains and the lipid anchor. |
| T3 |
373-565 |
Sentence |
denotes |
Their core proteins are similar and consist of a large N-terminal domain comprising 14 evolutionary conserved cysteines and a C-terminal stalk carrying the HS side chains and the lipid anchor. |
| TextSentencer_T4 |
566-652 |
Sentence |
denotes |
Cysteines in Gpc-1 can be S-nitrosylated but their positions have not been identified. |
| T4 |
566-652 |
Sentence |
denotes |
Cysteines in Gpc-1 can be S-nitrosylated but their positions have not been identified. |
| T4 |
566-652 |
Sentence |
denotes |
Cysteines in Gpc-1 can be S-nitrosylated but their positions have not been identified. |
| TextSentencer_T5 |
653-824 |
Sentence |
denotes |
The recently determined crystal structure of the N-terminal domain of Gpc-1 has revealed that all the evolutionary conserved cysteines form intramolecular disulfide bonds. |
| T5 |
653-824 |
Sentence |
denotes |
The recently determined crystal structure of the N-terminal domain of Gpc-1 has revealed that all the evolutionary conserved cysteines form intramolecular disulfide bonds. |
| T5 |
653-824 |
Sentence |
denotes |
The recently determined crystal structure of the N-terminal domain of Gpc-1 has revealed that all the evolutionary conserved cysteines form intramolecular disulfide bonds. |
| TextSentencer_T6 |
825-945 |
Sentence |
denotes |
However, Gpc-1 contains two more, non-conserved cysteines in the C-terminal stalk, located near the HS attachment sites. |
| T6 |
825-945 |
Sentence |
denotes |
However, Gpc-1 contains two more, non-conserved cysteines in the C-terminal stalk, located near the HS attachment sites. |
| T6 |
825-945 |
Sentence |
denotes |
However, Gpc-1 contains two more, non-conserved cysteines in the C-terminal stalk, located near the HS attachment sites. |
| TextSentencer_T7 |
946-1159 |
Sentence |
denotes |
We show here that the non-conserved cysteines are free thiols as a Gpc-1 core protein containing the C-terminal stalk could be biotinylated by 1-biotinamido-4-(4'-[maleimidomethyl-cyclohexane]-carboxyamido)butane. |
| T7 |
946-1159 |
Sentence |
denotes |
We show here that the non-conserved cysteines are free thiols as a Gpc-1 core protein containing the C-terminal stalk could be biotinylated by 1-biotinamido-4-(4'-[maleimidomethyl-cyclohexane]-carboxyamido)butane. |
| T7 |
946-1159 |
Sentence |
denotes |
We show here that the non-conserved cysteines are free thiols as a Gpc-1 core protein containing the C-terminal stalk could be biotinylated by 1-biotinamido-4-(4'-[maleimidomethyl-cyclohexane]-carboxyamido)butane. |
| TextSentencer_T8 |
1160-1389 |
Sentence |
denotes |
After S-nitrosylation by using a nitric oxide (NO) donor and copper ions, the Gpc-1 core protein was retained on an affinity matrix substituted with HS oligosaccharides containing N-unsubstituted glucosamines (GlcNH(2)/NH(3)(+)). |
| T8 |
1160-1389 |
Sentence |
denotes |
After S-nitrosylation by using a nitric oxide (NO) donor and copper ions, the Gpc-1 core protein was retained on an affinity matrix substituted with HS oligosaccharides containing N-unsubstituted glucosamines (GlcNH(2)/NH(3)(+)). |
| T8 |
1160-1389 |
Sentence |
denotes |
After S-nitrosylation by using a nitric oxide (NO) donor and copper ions, the Gpc-1 core protein was retained on an affinity matrix substituted with HS oligosaccharides containing N-unsubstituted glucosamines (GlcNH(2)/NH(3)(+)). |
| TextSentencer_T9 |
1390-1466 |
Sentence |
denotes |
The protein was displaced with 0.2 M glucosamine but also by 2 mM ascorbate. |
| T9 |
1390-1466 |
Sentence |
denotes |
The protein was displaced with 0.2 M glucosamine but also by 2 mM ascorbate. |
| T9 |
1390-1466 |
Sentence |
denotes |
The protein was displaced with 0.2 M glucosamine but also by 2 mM ascorbate. |
| TextSentencer_T10 |
1467-1593 |
Sentence |
denotes |
In the latter case, the HS of the affinity matrix was simultaneously cleaved into fragments containing anhydromannose (anMan). |
| T10 |
1467-1593 |
Sentence |
denotes |
In the latter case, the HS of the affinity matrix was simultaneously cleaved into fragments containing anhydromannose (anMan). |
| T10 |
1467-1593 |
Sentence |
denotes |
In the latter case, the HS of the affinity matrix was simultaneously cleaved into fragments containing anhydromannose (anMan). |
| TextSentencer_T11 |
1594-1727 |
Sentence |
denotes |
We propose that the S-nitrosocysteine residues interact with closely located GlcNH(2)/NH(3)(+) in the HS side chains of the Gpc-1 PG. |
| T11 |
1594-1727 |
Sentence |
denotes |
We propose that the S-nitrosocysteine residues interact with closely located GlcNH(2)/NH(3)(+) in the HS side chains of the Gpc-1 PG. |
| T11 |
1594-1727 |
Sentence |
denotes |
We propose that the S-nitrosocysteine residues interact with closely located GlcNH(2)/NH(3)(+) in the HS side chains of the Gpc-1 PG. |
| TextSentencer_T12 |
1728-1892 |
Sentence |
denotes |
Addition of ascorbate induces a series of reactions that eventually releases HS fragments with reducing terminal anMan, presumably without the formation of free NO. |
| T12 |
1728-1892 |
Sentence |
denotes |
Addition of ascorbate induces a series of reactions that eventually releases HS fragments with reducing terminal anMan, presumably without the formation of free NO. |
| T12 |
1728-1892 |
Sentence |
denotes |
Addition of ascorbate induces a series of reactions that eventually releases HS fragments with reducing terminal anMan, presumably without the formation of free NO. |