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Please use this identifier to cite or link to this item: http://dspace.bsu.edu.ru/handle/123456789/62966
Title: Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid
Authors: Aubrey, L. D.
Ninkina, N.
Sabine, M.
Ulameca
Abramycheva, N. Y.
Eftychia Vasili
Keywords: medicine
pharmacology
α-synuclein
Parkinson’s disease
single nucleotide polymorphism
amyotrophic lateral sclerosis
amyloid
Issue Date: 2024
Citation: Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid / L.D. Aubrey, N. Ninkina, Sabine M. Ulameca [et al.] // Proceedings of the National Academy of Sciences of the United States of America. - 2024. - Vol.121, №2.-Art. e2309700120
Abstract: α-, β-, and γ-Synuclein are intrinsically disordered proteins implicated in physiological processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic protein associated with Parkinson’s disease and certain other neurodegenerative disorders. Intensive research has focused on the mechanisms that cause αSyn to form amyloid structures, identifying its NAC region as being necessary and sufficient for amyloid assembly
URI: http://dspace.bsu.edu.ru/handle/123456789/62966
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