Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase, (Q27658869)

2

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Alexander B Taylor

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P John Hart

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Rodney L Levine

Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †

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language of work or name

English

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publication date

16 February 2010

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published in

Biochemistry

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volume

49

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issue

6

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page(s)

1191-8

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cites work

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The sulfurtransferases

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A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value.

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Labile Sulfur in Human Superoxide Dismutase

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Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site

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Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mut

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