ReviewMolecular neurobiology2013
α-Synuclein posttranslational modification and alternative splicing as a trigger for neurodegeneration.
Review in Molecular neurobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
75 citing papers in PubMed, 139 citations in OpenAlex.
- Magnetoreceptive CRY/MagR complexes: linking circadian redox signalling to protein aggregation in Alzheimer's and Parkinson's disease.ADMET & DMPK · 2026Review
- Alternative splicing and the aging brain in AfrAbia: New frontiers in dementia research.IBRO neuroscience reports · 2025Article
- Single cell transcriptomics reveals enrichment of aggregation-prone alpha-synuclein isoforms across synucleinopathies.bioRxiv : the preprint server for biology · 2025Article
- Aβ42 promotes the aggregation of α-synuclein splice isoforms via heterogeneous nucleation.FEBS letters · 2025Article
- Progress in Disease-Modifying Therapies for Parkinson's Disease.Aging and disease · 2025Review
- Fluid biomarkers in atypical Parkinsonism: current state and future perspectives.Journal of neural transmission (Vienna, Austria : 1996) · 2025Review
- Amyloid formation of alternatively spliced variants of α-synuclein.Protein science : a publication of the Protein Society · 2025Article
- Protective effects of paederoside in rotenone-induced cellular models of Parkinson's disease.Frontiers in cell and developmental biology · 2025Article
- Lead Phytomolecules for Treating Parkinson's Disease.Central nervous system agents in medicinal chemistry · 2025Review
- The potential of phosphorylated α-synuclein as a biomarker for the diagnosis and monitoring of multiple system atrophy.CNS neuroscience & therapeutics · 2024Review
- Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024Review
- The C-terminus of α-Synuclein Regulates its Dynamic Cellular Internalization by Neurexin 1β.Molecular biology of the cell · 2023Article
- Inactive S. aureus Cas9 downregulates alpha-synuclein and reduces mtDNA damage and oxidative stress levels in human stem cell model of Parkinson's disease.Scientific reports · 2023Article
- Alternative splicing in neurodegenerative disease and the promise of RNA therapies.Nature reviews. Neuroscience · 2023Review
- Sex-Specific Effects of Early-Life Iron Deficiency and Prenatal Choline Treatment on Adult Rat Hippocampal Transcriptome.Nutrients · 2023Article
- Nuclease-dead S.bioRxiv : the preprint server for biology · 2023Article
- Diagnosing multiple system atrophy: current clinical guidance and emerging molecular biomarkers.Frontiers in neurology · 2023Review
- Diagnostic and therapeutic agents that target alpha-synuclein in Parkinson's disease.Journal of neurology · 2022Review
- Alpha-synuclein as a biomarker in Parkinson's disease: focus on neural derived extracelluar vesicles.Neural regeneration research · 2022Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lewy body diseases include Parkinson disease and dementia with Lewy bodies and are characterized by the widespread distribution of Lewy bodies in virtually every brain area. The main component of Lewy bodies is alpha-synuclein (AS). Accumulating evidence suggests that AS oligomerization and aggregation are strongly associated with the pathogenesis of Lewy body diseases. AS is a small soluble protein with aggregation-prone properties under certain conditions. These properties are enhanced by posttranslational modifications such as phosphorylation, ubiquitination, nitration, and truncation. Accordingly, Lewy bodies contain abundant phosphorylated, nitrated, and monoubiquitinated AS. However, alternative splicing of the AS gene is also known to modify AS aggregation propensities. Splicing gives rise to four related forms of the protein, the main transcript and those that lack exon 4, exon 6, or both. Since AS structure and properties have been extensively studied, it is possible to predict the consequences of the splicing out of the two aforesaid exons. The present review discusses the latest insights on the mechanisms of AS posttranslational modifications and intends to depict their role in the pathogenesis of Lewy body diseases. The implications of deregulated alternative splicing are examined as well, and a hypothesis for the development of the pure form of dementia with Lewy bodies is proposed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.