Pub. Date : 1996 Feb 27
PMID : 8611584
18 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. | vicinal methionine | CaM5 | Triticum aestivum |
| 2 | Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. | vicinal methionine | CaM5 | Triticum aestivum |
| 3 | Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. | Hydrogen Peroxide | CaM5 | Triticum aestivum |
| 4 | Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. | Hydrogen Peroxide | CaM5 | Triticum aestivum |
| 5 | In order to investigate the possibility that calmodulin (CaM) may be a principal target of reactive oxygen species (ROS) produced under conditions of oxidative stress, we have examined wheat germ CaM for the presence of highly reactive sites that correlate with the loss of function. | Reactive Oxygen Species | CaM5 | Triticum aestivum |
| 6 | In order to investigate the possibility that calmodulin (CaM) may be a principal target of reactive oxygen species (ROS) produced under conditions of oxidative stress, we have examined wheat germ CaM for the presence of highly reactive sites that correlate with the loss of function. | Reactive Oxygen Species | CaM5 | Triticum aestivum |
| 7 | In order to investigate the possibility that calmodulin (CaM) may be a principal target of reactive oxygen species (ROS) produced under conditions of oxidative stress, we have examined wheat germ CaM for the presence of highly reactive sites that correlate with the loss of function. | Reactive Oxygen Species | CaM5 | Triticum aestivum |
| 8 | In order to investigate the possibility that calmodulin (CaM) may be a principal target of reactive oxygen species (ROS) produced under conditions of oxidative stress, we have examined wheat germ CaM for the presence of highly reactive sites that correlate with the loss of function. | Reactive Oxygen Species | CaM5 | Triticum aestivum |
| 9 | We find that one of the vicinal methionines (i.e., Met146 or Met147) near the C-terminus of CaM is selectively oxidized. | vicinal | CaM5 | Triticum aestivum |
| 10 | We find that one of the vicinal methionines (i.e., Met146 or Met147) near the C-terminus of CaM is selectively oxidized. | Methionine | CaM5 | Triticum aestivum |
| 11 | There is a 30-fold decrease in the calcium affinity of oxidatively modified CaM. | Calcium | CaM5 | Triticum aestivum |
| 12 | While there is a little change in the binding constant between the carboxyl-terminal domain of calcium-saturated CaM and a peptide homologous to the autoinhibitory sequence of the PM-Ca-ATPase, we find that there is a 9-fold reduction in the affinity of the amino-terminal domain of CaM with respect to the ability to bind target peptides. | Calcium | CaM5 | Triticum aestivum |
| 13 | While there is a little change in the binding constant between the carboxyl-terminal domain of calcium-saturated CaM and a peptide homologous to the autoinhibitory sequence of the PM-Ca-ATPase, we find that there is a 9-fold reduction in the affinity of the amino-terminal domain of CaM with respect to the ability to bind target peptides. | Calcium | CaM5 | Triticum aestivum |
| 14 | The extent of oxidative modification to one of the vicinal methionines near the carboxyl-terminal domain correlates with the loss of CaM-dependent activation of the PM-Ca-ATPase. | Methionine | CaM5 | Triticum aestivum |
| 15 | We suggest that the functional sensitivity of CaM to the oxidation of one of the C-terminal vicinal methionines permits CAM to serve a regulatory role in modulating cellular metabolism under conditions of oxidative stress. | vicinal methionines | CaM5 | Triticum aestivum |
| 16 | We suggest that the functional sensitivity of CaM to the oxidation of one of the C-terminal vicinal methionines permits CAM to serve a regulatory role in modulating cellular metabolism under conditions of oxidative stress. | vicinal methionines | CaM5 | Triticum aestivum |
| 17 | The predominant oxidation of a methionine near the carboxyl terminal of CaM is rationalized in terms of the enhanced solvent accessibility of these vicinal methionines. | Methionine | CaM5 | Triticum aestivum |
| 18 | The predominant oxidation of a methionine near the carboxyl terminal of CaM is rationalized in terms of the enhanced solvent accessibility of these vicinal methionines. | vicinal methionines | CaM5 | Triticum aestivum |