Mauro Cozzolino

TL;DR: It is demonstrated that each of 12 different familial ALS-mutant S OD1s with widely differing biophysical properties are associated with mitochondria of motoneuronal cells to a much greater extent than wild-type SOD1, and that this effect may depend on the oxidation of Cys residues.

TL;DR: The wealth of evidence implicating mitochondrial dysfunction as a major event in the pathology of ALS has prompted new studies aimed to the development of new mitochondria-targeted therapies, and it is now clear that drugs targeting more than one aspect of mitochondrial dysfunction are needed to fight this devastating disease.

TL;DR: This review focuses on existing evidence that oxidative stress is a major culprit in the pathogenesis of amyotrophic lateral sclerosis and examines whether metal-mediated oxidative stress would lead to several intracellular alterations and contribute to the induction of cell death pathways.

TL;DR: The clinical implication of these findings is that promising therapeutic approaches can be derived from multidrug treatments aimed at the simultaneous interception of damage in both motor neurons and nonmotor neuronal cells.

TL;DR: It is found that the removal of Cys-111 strongly reduces the ability of a range of different FALS-associated mutSOD1s to form aggregates and impair cell viability in cultured NSC-34 cells, consistent with the view that the redox environment influences the oligomerization/aggregation pathway of mutS OD1.