ArticleFEBS letters2020
Carboxy-terminal truncations of mouse α-synuclein alter aggregation and prion-like seeding.
Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Differential role of C-terminal truncations on alpha-synuclein pathology and Lewy body formation.NPJ Parkinson's disease · 2025Article
- The small molecule ZPD-2 inhibits the aggregation and seeded polymerisation of C-terminally truncated α-Synuclein.The FEBS journal · 2024Article
- Effect of host and strain factors on α-synuclein prion pathogenesis.Trends in neurosciences · 2024Review
- C-terminal truncation modulates α-Synuclein's cytotoxicity and aggregation by promoting the interactions with membrane and chaperone.Communications biology · 2022Article
- Neurons with Cat's Eyes: A Synthetic Strain of α-Synuclein Fibrils Seeding Neuronal Intranuclear Inclusions.Biomolecules · 2022Article
- The C-terminal tail of α-synuclein protects against aggregate replication but is critical for oligomerization.Communications biology · 2022Article
- Review
- The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates.Frontiers in cellular neuroscience · 2022Review
- Roles of α‑synuclein in gastrointestinal microbiome dysbiosis‑related Parkinson's disease progression (Review).Molecular medicine reports · 2021Review
- Cathepsin K is a potent disaggregase of α-synuclein fibrils.Biochemical and biophysical research communications · 2020Article
- Carboxy-terminal truncation and phosphorylation of α-synuclein elongates survival in a prion-like seeding mouse model of synucleinopathy.Neuroscience letters · 2020Article
- The emerging role of α-synuclein truncation in aggregation and disease.The Journal of biological chemistry · 2020Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
α-synuclein (αsyn) forms pathologic inclusions in several neurodegenerative diseases termed synucleinopathies. The inclusions are comprised of αsyn fibrils harboring prion-like properties. Prion-like activity of αsyn has been studied by intracerebral injection of fibrils into mice, where the presence of a species barrier requires the use of mouse αsyn. Post-translational modifications to αsyn such as carboxy (C)-terminal truncation occur in synucleinopathies, and their implications for prion-like aggregation and seeding are under investigation. Herein, C-truncated forms of αsyn found in human disease are recapitulated in mouse αsyn to study their seeding activity in vitro, in HEK293T cells, in neuronal-glial culture, and in nontransgenic mice. The results show that C-truncation of mouse αsyn accelerates aggregation of αsyn but alters prion-like seeding of inclusion formation.
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