Pub. Date : 2013 Feb 15
PMID : 23264618
12 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 2 | Wild-type SOD1 forms a highly conserved intra-molecular disulfide bond, whereas pathological SOD1 proteins are cross-linked via intermolecular disulfide bonds and form insoluble oligomers. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 3 | Wild-type SOD1 forms a highly conserved intra-molecular disulfide bond, whereas pathological SOD1 proteins are cross-linked via intermolecular disulfide bonds and form insoluble oligomers. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 4 | A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 5 | A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 6 | A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 7 | Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 8 | Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 9 | The disulfide scrambling produces SOD1 monomers with distinct electrophoretic mobility and also reproduces the formation of disulfide-linked oligomers. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 10 | The disulfide scrambling produces SOD1 monomers with distinct electrophoretic mobility and also reproduces the formation of disulfide-linked oligomers. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 11 | We have also found that the familial form of amyotrophic lateral sclerosis-causing mutations facilitate the disulfide scrambling in SOD1. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 12 | Based upon our results, therefore, scrambling of the conserved disulfide bond will be a key event to cause the pathological changes in disease-associated mutant SOD1 proteins. | Disulfides | superoxide dismutase 1 | Homo sapiens |