alpha-synuclein and miglustat

alpha-synuclein has been researched along with miglustat* in 1 studies

Other Studies

1 other study(ies) available for alpha-synuclein and miglustat

Article	Year
GBA1 deficiency negatively affects physiological α-synuclein tetramers and related multimers. Proceedings of the National Academy of Sciences of the United States of America, 2018, 01-23, Volume: 115, Issue:4 Accumulating evidence suggests that α-synuclein (α-syn) occurs physiologically as a helically folded tetramer that resists aggregation. However, the mechanisms underlying the regulation of formation of α-syn tetramers are still mostly unknown. Cellular membrane lipids are thought to play an important role in the regulation of α-syn tetramer formation. Since glucocerebrosidase 1 (GBA1) deficiency contributes to the aggregation of α-syn and leads to changes in neuronal glycosphingolipids (GSLs) including gangliosides, we hypothesized that GBA1 deficiency may affect the formation of α-syn tetramers. Here, we show that accumulation of GSLs due to GBA1 deficiency decreases α-syn tetramers and related multimers and increases α-syn monomers in CRISPR-GBA1 knockout (KO) SH-SY5Y cells. Moreover, α-syn tetramers and related multimers are decreased in N370S Topics: 1-Deoxynojirimycin; alpha-Synuclein; Cell Line, Tumor; Dopaminergic Neurons; Glucosylceramidase; Glycosphingolipids; Humans; Parkinson Disease; Protein Multimerization	2018

Article

Year

GBA1 deficiency negatively affects physiological α-synuclein tetramers and related multimers.

Proceedings of the National Academy of Sciences of the United States of America, 2018, 01-23, Volume: 115, Issue:4

Accumulating evidence suggests that α-synuclein (α-syn) occurs physiologically as a helically folded tetramer that resists aggregation. However, the mechanisms underlying the regulation of formation of α-syn tetramers are still mostly unknown. Cellular membrane lipids are thought to play an important role in the regulation of α-syn tetramer formation. Since glucocerebrosidase 1 (GBA1) deficiency contributes to the aggregation of α-syn and leads to changes in neuronal glycosphingolipids (GSLs) including gangliosides, we hypothesized that GBA1 deficiency may affect the formation of α-syn tetramers. Here, we show that accumulation of GSLs due to GBA1 deficiency decreases α-syn tetramers and related multimers and increases α-syn monomers in CRISPR-GBA1 knockout (KO) SH-SY5Y cells. Moreover, α-syn tetramers and related multimers are decreased in N370S

Topics: 1-Deoxynojirimycin; alpha-Synuclein; Cell Line, Tumor; Dopaminergic Neurons; Glucosylceramidase; Glycosphingolipids; Humans; Parkinson Disease; Protein Multimerization

2018