%0 Journal Article
%A Fahmy, Nagia
%A Müller, Kathrin
%A Andersen, Peter Munch
%A Marklund, Stefan L
%A Otto, Markus
%A Ludolph, Albert
%A Hamdi, Nabila
%T A novel homozygous p.Ser69Pro SOD1 mutation causes severe young-onset ALS with decreased enzyme activity.
%J Journal of neurology
%V 270
%N 3
%@ 0340-5354
%C Berlin
%I Springer
%M DZNE-2023-00004
%P 1770-1773
%D 2023
%Z ISSN 1432-1459 not unique: **2 hits**.
%X The dose-effect of various SOD1 mutations on SOD1 enzymatic activity offers valuable insights into ALS pathogenesis with possible therapeutic implications. Homozygous SOD1 mutations, yet scarce, are of special interest. We report a novel homozygous SOD1 mutation with decreased enzymatic activity and severe early onset ALS phenotype.Whole exome sequencing and targeted screening of commonly implicated genes were conducted. Repeat-primed PCR and fragment length analysis were used for C9orf72. Bi-directional Sanger sequencing was used for SOD1 and other genes. SOD1 activity was measured by direct spectrophotometry. Serum neurofilament light chain level was measured by the ELLA immunoassay system.The homozygous patient for a novel SOD1 variant p.Ser69Pro showed poor SOD1 enzymatic activity (16
%K Humans
%K Superoxide Dismutase-1: genetics
%K Amyotrophic Lateral Sclerosis: genetics
%K Amyotrophic Lateral Sclerosis: diagnosis
%K Mutation
%K Homozygote
%K Motor Neurons
%K Superoxide Dismutase: genetics
%K Superoxide Dismutase-1 (NLM Chemicals)
%K Enzyme activity (Other)
%K Homozygous (Other)
%K Novel mutation (Other)
%K SOD1 (Other)
%K Young-onset (Other)
%K Superoxide Dismutase (NLM Chemicals)
%K SOD1 protein, human (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%2 pmc:PMC9971132
%$ pmid:36472686
%R 10.1007/s00415-022-11489-x
%U https://pub.dzne.de/record/169125