TY  - JOUR
AU  - Fahmy, Nagia
AU  - Müller, Kathrin
AU  - Andersen, Peter Munch
AU  - Marklund, Stefan L
AU  - Otto, Markus
AU  - Ludolph, Albert
AU  - Hamdi, Nabila
TI  - A novel homozygous p.Ser69Pro SOD1 mutation causes severe young-onset ALS with decreased enzyme activity.
JO  - Journal of neurology
VL  - 270
IS  - 3
SN  - 0340-5354
CY  - Berlin
PB  - Springer
M1  - DZNE-2023-00004
SP  - 1770-1773
PY  - 2023
N1  - ISSN 1432-1459 not unique: **2 hits**.
AB  - 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
KW  - Humans
KW  - Superoxide Dismutase-1: genetics
KW  - Amyotrophic Lateral Sclerosis: genetics
KW  - Amyotrophic Lateral Sclerosis: diagnosis
KW  - Mutation
KW  - Homozygote
KW  - Motor Neurons
KW  - Superoxide Dismutase: genetics
KW  - Superoxide Dismutase-1 (NLM Chemicals)
KW  - Enzyme activity (Other)
KW  - Homozygous (Other)
KW  - Novel mutation (Other)
KW  - SOD1 (Other)
KW  - Young-onset (Other)
KW  - Superoxide Dismutase (NLM Chemicals)
KW  - SOD1 protein, human (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C2  - pmc:PMC9971132
C6  - pmid:36472686
DO  - DOI:10.1007/s00415-022-11489-x
UR  - https://pub.dzne.de/record/169125
ER  -