| DC Field | Value | Language |
|---|
| dc.contributor.author | Aubrey, L. D. | - |
| dc.contributor.author | Ninkina, N. | - |
| dc.contributor.author | Sabine, M. | - |
| dc.contributor.author | Ulameca | - |
| dc.contributor.author | Abramycheva, N. Y. | - |
| dc.contributor.author | Eftychia Vasili | - |
| dc.date.accessioned | 2024-06-14T07:24:56Z | - |
| dc.date.available | 2024-06-14T07:24:56Z | - |
| dc.date.issued | 2024 | - |
| dc.identifier.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 | ru |
| dc.identifier.uri | http://dspace.bsu.edu.ru/handle/123456789/62966 | - |
| dc.description.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 | ru |
| dc.language.iso | en | ru |
| dc.subject | medicine | ru |
| dc.subject | pharmacology | ru |
| dc.subject | α-synuclein | ru |
| dc.subject | Parkinson’s disease | ru |
| dc.subject | single nucleotide polymorphism | ru |
| dc.subject | amyotrophic lateral sclerosis | ru |
| dc.subject | amyloid | ru |
| dc.title | Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid | ru |
| dc.type | Article | ru |
| Appears in Collections: | Статьи из периодических изданий и сборников (на иностранных языках) = Articles from periodicals and collections (in foreign languages)
|
