ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences1999
Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 170 citations in OpenAlex.
- Limited Detectability of Network Functional Alterations in a Tauopathy Model Using Mouse Primary Cortical Cultures.Biomedicines · 2026Article
- Synucleinopathy-like clinical features and biologically defined synuclein seeding in PSP-Parkinsonism: an imperfect match.NPJ Parkinson's disease · 2026Article
- Impairment of Nrf2 signaling in the hippocampus of P301S tauopathy mice model aligns with the cognitive impairment and the associated neuroinflammation.Journal of inflammation (London, England) · 2024Article
- Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- Different Roles of p62 (SQSTM1) Isoforms in Keratin-Related Protein Aggregation.International journal of molecular sciences · 2021Article
- Possible Mechanisms of Tau Spread and Toxicity in Alzheimer's Disease.Frontiers in cell and developmental biology · 2021Review
- Alterations in the nigrostriatal system following conditional inactivation of α-synuclein in neurons of adult and aging mice.Neurobiology of aging · 2020Article
- HSP70 and HSP90 in neurodegenerative diseases.Neuroscience letters · 2020Review
- GSK3β and Tau Protein in Alzheimer's Disease and Epilepsy.Frontiers in cellular neuroscience · 2020Article
- Insights Into Peptide Inhibition of Alpha-Synuclein Aggregation.Frontiers in neuroscience · 2020Article
- Characterizing the inhibition of α-synuclein oligomerization by a pharmacological chaperone that prevents prion formation by the protein PrP.Protein science : a publication of the Protein Society · 2019Article
- In-vitro and in-silico investigation of protective mechanisms of crocin against E46K α-synuclein amyloid formation.Molecular biology reports · 2019Article
- Structural characteristics and membrane interactions of tandem α-synuclein oligomers.Scientific reports · 2018Article
- Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.F1000Research · 2017Review
- Noradrenergic Modulation of Cognition in Health and Disease.Neural plasticity · 2017Review
- The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases.Frontiers in neuroscience · 2017Review
- Untangling the Manganese-α-Synuclein Web.Frontiers in neuroscience · 2016Review
- A novel resource for studying function and dysfunction of α-synuclein: mouse lines for modulation of endogenous Snca gene expression.Scientific reports · 2015Article
- Studies of lipopolysaccharide effects on the induction of α-synuclein pathology by exogenous fibrils in transgenic mice.Molecular neurodegeneration · 2015Article
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1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease and Parkinson's disease are the most common neurodegenerative diseases. They are characterized by the degeneration of selected populations of nerve cells that develop filamentous inclusions before degeneration. The neuronal inclusions of Alzheimer's disease are made of the microtubule-associated protein tau, in a hyperphosphorylated state. Recent work has shown that the filamentous inclusions of Parkinson's disease are made of the protein alpha-synuclein and that rare, familial forms of Parkinson's disease are caused by missense mutations in the alpha-synuclein gene. Besides Parkinson's disease, the filamentous inclusions of two additional neurodegenerative diseases, namely dementia with Lewy bodies and multiple system atrophy, have also been found to be made of alpha-synuclein. Abundant filamentous tau inclusions are not limited to Alzheimer's disease. They are the defining neuropathological characteristic of frontotemporal dementias such as Pick's disease, and of progressive supranuclear palsy and corticobasal degeneration. The recent discovery of mutations in the tau gene in familial forms of frontotemporal dementia has provided a direct link between tau dysfunction and dementing disease. The new work has established that tauopathies and alpha-synucleinopathies account for most late-onset neurodegenerative diseases in man. The formation of intracellular filamentous inclusions might be the gain of toxic function that leads to the demise of affected brain cells.
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