Dimerization, Oligomerization, and Aggregation of Human Amyotrophic Lateral Sclerosis Copper/Zinc Superoxide Dismutase 1 Protein Mutant Forms in Live Cells - SIGNAUX ET IMAGES NUMÉRIQUES, ROBOTIQUE Accéder directement au contenu
Article Dans Une Revue Journal of Biological Chemistry Année : 2014

Dimerization, Oligomerization, and Aggregation of Human Amyotrophic Lateral Sclerosis Copper/Zinc Superoxide Dismutase 1 Protein Mutant Forms in Live Cells

Résumé

Background: Copper/zinc superoxide dismutase (SOD1) genetic mutants are associated with familial amyotrophic lateral sclerosis (ALS). Mutant proteins form abnormal aggregates. Results: We used imaging of live cells to observe SOD1 proteins harboring mutations associated with ALS. Conclusion: SOD1 mutations impair its dimerization, leading to subsequent aggregation. Significance: Analysis of the SOD1 quaternary structure in living human cells correlates with previous biochemical data.
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Dates et versions

hal-02902062 , version 1 (17-07-2020)

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Jiho Kim, Honggun Lee, Joo Hyun Lee, Do-Yoon Kwon, Auguste Genovesio, et al.. Dimerization, Oligomerization, and Aggregation of Human Amyotrophic Lateral Sclerosis Copper/Zinc Superoxide Dismutase 1 Protein Mutant Forms in Live Cells. Journal of Biological Chemistry, 2014, 289 (21), pp.15094-15103. ⟨10.1074/jbc.M113.542613⟩. ⟨hal-02902062⟩
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