Pub. Date : 2001 Oct 9
PMID : 11580274
38 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 2 | Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents. | Sulfhydryl Compounds | lens aldose reductase pseudogene | Bos taurus |
| 3 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 4 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 5 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 6 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 7 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 8 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 9 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 10 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 11 | Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 12 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | Glyceraldehyde | lens aldose reductase pseudogene | Bos taurus |
| 13 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | Glyceraldehyde | lens aldose reductase pseudogene | Bos taurus |
| 14 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | Glyceraldehyde | lens aldose reductase pseudogene | Bos taurus |
| 15 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | sorbinil | lens aldose reductase pseudogene | Bos taurus |
| 16 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | sorbinil | lens aldose reductase pseudogene | Bos taurus |
| 17 | Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors. | sorbinil | lens aldose reductase pseudogene | Bos taurus |
| 18 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Dithiothreitol | lens aldose reductase pseudogene | Bos taurus |
| 19 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Dithiothreitol | lens aldose reductase pseudogene | Bos taurus |
| 20 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Glutathione | lens aldose reductase pseudogene | Bos taurus |
| 21 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Glutathione | lens aldose reductase pseudogene | Bos taurus |
| 22 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 23 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Mercaptoethanol | lens aldose reductase pseudogene | Bos taurus |
| 24 | Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents. | Mercaptoethanol | lens aldose reductase pseudogene | Bos taurus |
| 25 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 26 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 27 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | glutathionyl | lens aldose reductase pseudogene | Bos taurus |
| 28 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | glutathionyl | lens aldose reductase pseudogene | Bos taurus |
| 29 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | glutathionyl | lens aldose reductase pseudogene | Bos taurus |
| 30 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | glutathionyl | lens aldose reductase pseudogene | Bos taurus |
| 31 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 32 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 33 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 34 | The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 35 | A rationale for the special susceptibility of Cys-ALR2 and CysGly-ALR2, as compared to GS-ALR2, to the thermally induced intramolecular rearrangement is given on the basis of a molecular dynamic and energy minimization approach. | Cysteine | lens aldose reductase pseudogene | Bos taurus |
| 36 | A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed. | Sulfhydryl Compounds | lens aldose reductase pseudogene | Bos taurus |
| 37 | A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed. | Disulfides | lens aldose reductase pseudogene | Bos taurus |
| 38 | A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed. | Sulfhydryl Compounds | lens aldose reductase pseudogene | Bos taurus |