Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-63 |
Sentence |
denotes |
Mass spectrometric analysis of nitric oxide-modified caspase-3. |
T1 |
0-63 |
Sentence |
denotes |
Mass spectrometric analysis of nitric oxide-modified caspase-3. |
TextSentencer_T2 |
64-135 |
Sentence |
denotes |
Caspases are a family of cysteine proteases activated during apoptosis. |
T2 |
64-135 |
Sentence |
denotes |
Caspases are a family of cysteine proteases activated during apoptosis. |
TextSentencer_T3 |
136-249 |
Sentence |
denotes |
Modification of caspases by nitric oxide and its relevance during apoptosis is currently a controversial subject. |
T3 |
136-249 |
Sentence |
denotes |
Modification of caspases by nitric oxide and its relevance during apoptosis is currently a controversial subject. |
TextSentencer_T4 |
250-332 |
Sentence |
denotes |
In this study we analyzed the S-nitrosated form of caspase-3 at a molecular level. |
T4 |
250-332 |
Sentence |
denotes |
In this study we analyzed the S-nitrosated form of caspase-3 at a molecular level. |
TextSentencer_T5 |
333-489 |
Sentence |
denotes |
By using electrospray ionization-mass spectrometry, we detected poly-S-nitrosation of caspase-3 with an average of about 2 molecules of NO bound per enzyme. |
T5 |
333-489 |
Sentence |
denotes |
By using electrospray ionization-mass spectrometry, we detected poly-S-nitrosation of caspase-3 with an average of about 2 molecules of NO bound per enzyme. |
TextSentencer_T6 |
490-611 |
Sentence |
denotes |
Although NO treatment completely inhibited enzyme activity, S-nitrosation was not restricted to the active site cysteine. |
T6 |
490-611 |
Sentence |
denotes |
Although NO treatment completely inhibited enzyme activity, S-nitrosation was not restricted to the active site cysteine. |
TextSentencer_T7 |
612-775 |
Sentence |
denotes |
Rather, we detected multiple relative mass increases of 30 +/- 1 Da in both the p12 and p17 subunits of caspase-3, corresponding to single to triple S-nitrosation. |
T7 |
612-775 |
Sentence |
denotes |
Rather, we detected multiple relative mass increases of 30 +/- 1 Da in both the p12 and p17 subunits of caspase-3, corresponding to single to triple S-nitrosation. |
TextSentencer_T8 |
776-886 |
Sentence |
denotes |
The stability of these S-nitrosations differed in physiologically relevant concentrations of 5 mM glutathione. |
T8 |
776-886 |
Sentence |
denotes |
The stability of these S-nitrosations differed in physiologically relevant concentrations of 5 mM glutathione. |
TextSentencer_T9 |
887-1092 |
Sentence |
denotes |
Whereas all S-nitroso bonds in the p12 subunit were cleaved with release of NO and partial formation of protein-mixed disulfides with glutathione, a single S-nitrosation in the p17 subunit remained stable. |
T9 |
887-1092 |
Sentence |
denotes |
Whereas all S-nitroso bonds in the p12 subunit were cleaved with release of NO and partial formation of protein-mixed disulfides with glutathione, a single S-nitrosation in the p17 subunit remained stable. |
TextSentencer_T10 |
1093-1355 |
Sentence |
denotes |
Since this S-nitrosation was not observed in a mutant form of caspase-3 lacking the active site cysteine, we conclude that NO nitrosates the active site cysteine of caspase-3 and that this modification is notably inert to fast trans-nitrosation with glutathione. |
T10 |
1093-1355 |
Sentence |
denotes |
Since this S-nitrosation was not observed in a mutant form of caspase-3 lacking the active site cysteine, we conclude that NO nitrosates the active site cysteine of caspase-3 and that this modification is notably inert to fast trans-nitrosation with glutathione. |
TextSentencer_T11 |
1356-1525 |
Sentence |
denotes |
Furthermore, we provide evidence that treatment of caspase-3 with NO can lead to mixed disulfide formation with glutathione, demonstrating the oxidative character of NO. |
T11 |
1356-1525 |
Sentence |
denotes |
Furthermore, we provide evidence that treatment of caspase-3 with NO can lead to mixed disulfide formation with glutathione, demonstrating the oxidative character of NO. |