An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis †
Ray SS, Nowak RJ, Strokovich K, Brown RH, Walz T, Lansbury PT. An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis †. Biochemistry 2004, 43: 4899-4905. PMID: 15109247, DOI: 10.1021/bi030246r.Peer-Reviewed Original ResearchConceptsSuperoxide dismutase 1Familial amyotrophic lateral sclerosisDisulfide bondsDisease-associated proteinsIntersubunit disulfide bondsWild-type SOD1Symmetry-related residuesWild-type superoxide dismutase 1Dimer interfaceMutant formsAmyloid poresMutant superoxide dismutase 1Pathogenic speciesAmytrophic lateral sclerosisAbolished aggregationConcentration-dependent lossSOD1 inclusionsVitro aggregationPoint mutationsDimer dissociationEnzymatic activityWT dimerLateral sclerosisDismutase 1Animal modeling studies