| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-32 |
Sentence |
denotes |
Regulation of glycogen synthase. |
| T1 |
0-32 |
Sentence |
denotes |
Regulation of glycogen synthase. |
| TextSentencer_T2 |
33-143 |
Sentence |
denotes |
Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation. |
| T2 |
33-143 |
Sentence |
denotes |
Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation. |
| TextSentencer_T3 |
144-271 |
Sentence |
denotes |
The major yeast glycogen synthase, Gsy2p, is inactivated by phosphorylation and activated by the allosteric ligand glucose-6-P. |
| T3 |
144-271 |
Sentence |
denotes |
The major yeast glycogen synthase, Gsy2p, is inactivated by phosphorylation and activated by the allosteric ligand glucose-6-P. |
| TextSentencer_T4 |
272-436 |
Sentence |
denotes |
From studies of recombinant proteins, the control can be accommodated by a three-state model, in which unphosphorylated enzyme has intermediate activity (state II). |
| T4 |
272-436 |
Sentence |
denotes |
From studies of recombinant proteins, the control can be accommodated by a three-state model, in which unphosphorylated enzyme has intermediate activity (state II). |
| TextSentencer_T5 |
437-634 |
Sentence |
denotes |
Glucose-6-P increased V(max)/K(m) by about 2-fold (state III), whereas phosphorylation by the cyclin-dependent protein kinase Pcl10p/Pho85p decreased V(max)/K(m) by approximately 30-fold (state I). |
| T5 |
437-634 |
Sentence |
denotes |
Glucose-6-P increased V(max)/K(m) by about 2-fold (state III), whereas phosphorylation by the cyclin-dependent protein kinase Pcl10p/Pho85p decreased V(max)/K(m) by approximately 30-fold (state I). |
| TextSentencer_T6 |
635-725 |
Sentence |
denotes |
In the presence of glucose-6-P, state III is achieved regardless of phosphorylation state. |
| T6 |
635-725 |
Sentence |
denotes |
In the presence of glucose-6-P, state III is achieved regardless of phosphorylation state. |
| TextSentencer_T7 |
726-901 |
Sentence |
denotes |
The enzyme forms complexes in solution with the yeast glycogenin Glg2p, but this interaction appears not to affect control either by glucose-6-P binding or by phosphorylation. |
| T7 |
726-901 |
Sentence |
denotes |
The enzyme forms complexes in solution with the yeast glycogenin Glg2p, but this interaction appears not to affect control either by glucose-6-P binding or by phosphorylation. |
| TextSentencer_T8 |
902-995 |
Sentence |
denotes |
Scanning mutagenesis was applied to identify residues potentially involved in ligand binding. |
| T8 |
902-995 |
Sentence |
denotes |
Scanning mutagenesis was applied to identify residues potentially involved in ligand binding. |
| TextSentencer_T9 |
996-1059 |
Sentence |
denotes |
Of 22 mutant enzymes analyzed, seven were essentially inactive. |
| T9 |
996-1059 |
Sentence |
denotes |
Of 22 mutant enzymes analyzed, seven were essentially inactive. |
| TextSentencer_T10 |
1060-1189 |
Sentence |
denotes |
Five mutant proteins were altered in their activation by glucose-6-P, and two were completely unaffected by the hexose phosphate. |
| T10 |
1060-1189 |
Sentence |
denotes |
Five mutant proteins were altered in their activation by glucose-6-P, and two were completely unaffected by the hexose phosphate. |
| TextSentencer_T11 |
1190-1351 |
Sentence |
denotes |
One of these, R586A/R588A/R591A (all three of the indicated Arg residues mutated to Ala), had wild-type activity and was normally inactivated by phosphorylation. |
| T11 |
1190-1351 |
Sentence |
denotes |
One of these, R586A/R588A/R591A (all three of the indicated Arg residues mutated to Ala), had wild-type activity and was normally inactivated by phosphorylation. |
| TextSentencer_T12 |
1352-1477 |
Sentence |
denotes |
A second mutant, R579A/R580A/R582A, had somewhat reduced V(max), but its activity was not greatly reduced by phosphorylation. |
| T12 |
1352-1477 |
Sentence |
denotes |
A second mutant, R579A/R580A/R582A, had somewhat reduced V(max), but its activity was not greatly reduced by phosphorylation. |
| TextSentencer_T13 |
1478-1718 |
Sentence |
denotes |
The Arg residues in these two mutants are restricted to a highly conserved, 13-residue segment of Gsy2p that we propose to be important for glucose-6-P binding and/or the ability of the enzyme to undergo transitions between activity states. |
| T13 |
1478-1718 |
Sentence |
denotes |
The Arg residues in these two mutants are restricted to a highly conserved, 13-residue segment of Gsy2p that we propose to be important for glucose-6-P binding and/or the ability of the enzyme to undergo transitions between activity states. |