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| Content Provider | Springer Nature Link |
|---|---|
| Author | Hilton, James B. White, Anthony R. Crouch, Peter J. |
| Copyright Year | 2015 |
| Abstract | Mutations to the ubiquitous antioxidant enzyme Cu/Zn superoxide dismutase (SOD1) were the first established genetic cause of the fatal, adult-onset neurodegenerative disease amyotrophic lateral sclerosis (ALS). It is widely accepted that these mutations do not cause ALS via a loss of antioxidant function, but elucidating the alternate toxic gain of function has proven to be elusive. Under physiological conditions, SOD1 binds one copper ion and one zinc ion per monomer to form a highly stable and functional homodimer, but there is now ample evidence to indicate aberrant persistence of SOD1 in an intermediate metal-deficient state may contribute to the protein’s involvement in ALS. This review briefly discusses some of the data to support a role for metal-deficient SOD1 in the development of ALS and some of the outcomes from drug development studies that have aimed to modify the symptoms of ALS by targeting the metal state of SOD1. The implications for the metal state of SOD1 in cases of sporadic ALS that do not involve mutant SOD1 are also discussed. |
| Starting Page | 481 |
| Ending Page | 487 |
| Page Count | 7 |
| File Format | |
| ISSN | 09462716 |
| Journal | Journal of Molecular Medicine |
| Volume Number | 93 |
| Issue Number | 5 |
| e-ISSN | 14321440 |
| Language | English |
| Publisher | Springer Berlin Heidelberg |
| Publisher Date | 2015-03-11 |
| Publisher Place | Berlin/Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Amyotrophic lateral sclerosis (ALS) Motor neuron disease (MND) Copper (Cu) Zinc (Zn) Cu/Zn superoxide dismutase (SOD1) Protein misfolding Diacetylbis(4-methylthiosemicarbazonato)copperII Molecular Medicine Human Genetics Internal Medicine |
| Content Type | Text |
| Resource Type | Article |
| Subject | Drug Discovery Molecular Medicine Genetics (clinical) |
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