Metal-deficient SOD1 in amyotrophic lateral sclerosis
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| 024 | 7 | 0 | |a 10.1007/s00109-015-1273-3 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00109-015-1273-3 | ||
| 245 | 0 | 0 | |a Metal-deficient SOD1 in amyotrophic lateral sclerosis |h [Elektronische Daten] |c [James Hilton, Anthony White, Peter Crouch] |
| 520 | 3 | |a 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 tomodify 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. | |
| 540 | |a The Author(s), 2015 | ||
| 690 | 7 | |a Amyotrophic lateral sclerosis (ALS) |2 nationallicence | |
| 690 | 7 | |a Motor neuron disease (MND) |2 nationallicence | |
| 690 | 7 | |a Copper (Cu) |2 nationallicence | |
| 690 | 7 | |a Zinc (Zn) |2 nationallicence | |
| 690 | 7 | |a Cu/Zn superoxide dismutase (SOD1) |2 nationallicence | |
| 690 | 7 | |a Protein misfolding |2 nationallicence | |
| 690 | 7 | |a Diacetylbis(4-methylthiosemicarbazonato)copperII |2 nationallicence | |
| 700 | 1 | |a Hilton |D James |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | |
| 700 | 1 | |a White |D Anthony |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | |
| 700 | 1 | |a Crouch |D Peter |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | |
| 773 | 0 | |t Journal of Molecular Medicine |d Springer Berlin Heidelberg |g 93/5(2015-05-01), 481-487 |x 0946-2716 |q 93:5<481 |1 2015 |2 93 |o 109 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00109-015-1273-3 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00109-015-1273-3 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hilton |D James |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a White |D Anthony |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Crouch |D Peter |u Department of Pathology, The University of Melbourne, 3010, Melbourne, Victoria, Australia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Journal of Molecular Medicine |d Springer Berlin Heidelberg |g 93/5(2015-05-01), 481-487 |x 0946-2716 |q 93:5<481 |1 2015 |2 93 |o 109 | ||