A Daresbury led international initiative on the role of the protein superoxide dismutase in motor neuron disease was recently highlighted following a meeting at King's College, London.

This is mentioned in the paragraph 'Theory becomes unstuck!'. This is taken from the latest MND Association magazine 'Thumbprint'.
See the 'Thumbprint' magazine article (pdf) "Superlative Summer for Research" featuring this meeting.

More than 90 point mutations in human CuZn superoxide dismutase (SOD1) lead to the development of familial amyotrophic lateral sclerosis (FALS), also known also as motor neuron disease. A growing body of evidence suggests that a subset of mutations located close to the dimeric interface can lead to a major destabilization of the mutant enzymes. X-ray scattering and diffraction experiments at Daresbury Laboratory on the A4V and I113T FALS mutants of SOD1 show that the dimeric molecule is substantially destabilized in comparison with wild-type SOD1. These results support the view that the pathogenic properties of this subset of FALS mutants are at least in part due to this destabilization.

 

The Motor Neurone Disease Association web site. www.mndassociation.org

 

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