2004
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
2002
α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils
Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT. α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils. Journal Of Molecular Biology 2002, 322: 1089-1102. PMID: 12367530, DOI: 10.1016/s0022-2836(02)00735-0.Peer-Reviewed Original Research