Pub. Date : 2015 Dec 18
PMID : 26511321
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 2 | The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 3 | Mature SOD1 owes its exceptional stability to a number of post-translational modifications as follows: formation of the intramolecular disulfide bond, binding of copper and zinc, and dimerization. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 4 | Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 5 | Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 6 | Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. | Disulfides | superoxide dismutase 1 | Homo sapiens |
| 7 | Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. | Disulfides | superoxide dismutase 1 | Homo sapiens |