Together for ever…: Cross-linking of proteins by a ditryptophan bond

Cross-linking of proteins by a ditryptophan bond

by Verônica Paviani

Oxidative modifications of proteins are extensively investigated because proteins are major targets of radicals and oxidants under physiological conditions [1]. The amino acid residues most susceptible to oxidation are the sulfur-containing residues cysteine and methionine and the aromatic residues histidine, phenylalanine, tyrosine and tryptophan. The oxidation of cysteine and methionine residues is reversible and protein-cysteine oxidation is emerging as a fundamental cell regulatory mechanism. In contrast, the oxidation of all other protein residues is irreversible, and may result in loss of protein

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A novel oxidative pathway for human SOD1 aggregation is revealed and may contribute to ALS pathology

by Ohara Augusto

ALS (amyotrophic lateral sclerosis) is a fatal disease characterized by the degeneration of motor neurons, resulting in progressive muscle weakness, atrophy, paralysis and death. Most cases of ALS are sporadic but about 10% of the cases have a genetic basis.ALS-causing mutations have been identified in several genes, but the mutation of Cu,Zn superoxide dismutase gene (SOD1) is the most studied and responsible for about 20% of the familial cases. SOD1-linked ALS patients exhibit pathology and symptoms similar to those of sporadic ALS patients, leading to the hypothesis that both forms of the disease have a common pathogenic mechanism. This hypothesis led to many advances in

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