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Science 20 August 1993:
Vol. 261. no. 5124, pp. 1047 - 1051
DOI: 10.1126/science.8351519
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Articles

Science, Vol 261, Issue 5124, 1047-1051
Copyright © 1993 by American Association for the Advancement of Science

articles

Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase

HX Deng, A Hentati, JA Tainer, Z Iqbal, A Cayabyab, WY Hung, ED Getzoff, P Hu, B Herzfeldt, RP Roos, and al. et

Department of Neurology, Northwestern University Medical School, Chicago, IL 60611.

Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 A crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.


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   Abstract »    Full Text »    PDF »
Absence of neurofilaments reduces the selective vulnerability of motor neurons and slows disease caused by a familial amyotrophic lateral sclerosis-linked superoxide dismutase 1 mutant.
T. L. Williamson, L. I. Bruijn, Q. Zhu, K. L. Anderson, S. D. Anderson, J.-P. Julien, and D. W. Cleveland (1998)
PNAS 95, 9631-9636
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Apoptosis of Retrogradely Degenerating Neurons Occurs in Association with the Accumulation of Perikaryal Mitochondria and Oxidative Damage to the Nucleus.
N. A. Al-Abdulla and L. J. Martin (1998)
Am. J. Pathol. 153, 447-456
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Rat Testicular Extracellular Superoxide Dismutase: Its Purification, Cellular Distribution, and Regulation.
D. Mruk, C.-H. Cheng, Y.-H. Cheng, M.-y. Mo, J. Grima, B. Silvestrini, W. M. Lee, and C. Y. Cheng (1998)
Biol Reprod 59, 298-308
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Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2.
R. J. Singh, H. Karoui, M. R. Gunther, J. S. Beckman, R. P. Mason, and B. Kalyanaraman (1998)
PNAS 95, 6675-6680
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Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants.
L. B. Corson, J. J. Strain, V. C. Culotta, and D. W. Cleveland (1998)
PNAS 95, 6361-6366
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Overexpression of human copper,zinc-superoxide dismutase (SOD1) prevents postischemic injury.
P. Wang, H. Chen, H. Qin, S. Sankarapandi, M. W. Becher, P. C. Wong, and J. L. Zweier (1998)
PNAS 95, 4556-4560
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