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Browsing by Subject α-synuclein

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Showing results 1 to 3 of 3
  • OER000002751.pdf.jpg
  • Journal article

  • First direct observation of ‘elongated’ conformational states in α-synuclein upon liquid-liquid phase separation

    • Authors : Ubbiali, Daniele (2023)

  • α-Synuclein (α-syn) is an intrinsically disordered protein (IDP) that undergoes liquid-liquid phase separation (LLPS), fibrillation, and forms insoluble intracellular Lewy’s bodies in neurons, which are the hallmark of Parkinson’s Disease (PD). Neurotoxicity precedes the formation of aggregates and is probably related to LLPS of α-syn in the cell. The molecular mechanisms underlying the early stages of LLPS are still elusive. To obtain s...
  • OER000004029.pdf.jpg
  • Journal article

  • O-GlcNAcylation of small heat shock proteins enhances their anti-amyloid chaperone activity

    • Authors : Balana, Aaron T; Levine, Paul M; Mukherjee, Somnath (2019)

  • A major role for the intracellular posttranslational modification O-GlcNAc appears to be the inhibition of protein aggregation. Most of the previous studies in this area have focused on O-GlcNAcylation of the amyloid-forming proteins themselves. Here, we use synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly...
  • OER000000176.pdf.jpg
  • Periodicals (Báo – Tạp chí)

  • Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation

    • Authors : Galvagnion, Céline (2020)

  • Intraneuronal accumulation of aggregated α-synuclein is a pathological hallmark of Parkinson’s disease. Therefore, mechanisms capable of promoting α-synuclein deposition bear important pathogenetic implications. Mutations of the glucocerebrosidase 1 (GBA) gene represent a prevalent Parkinson’s disease risk factor. They are associated with loss of activity of a key enzyme involved in lipid metabolism, glucocerebrosidase, supporting a mechanistic relationship between abnormal α-synuclein-l...