ReviewJournal of molecular neuroscience : MN2016
Interactions Between α-Synuclein and Tau Protein: Implications to Neurodegenerative Disorders.
Review in Journal of molecular neuroscience : MN, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Gene expression meta-analysis of Parkinson's disease and its relationship with Alzheimer's disease.Molecular brain · 2019Pooled it
- Tau protein: Physiological functions and multifaceted roles in neurodegenerative and psychiatric disorders.Genomic psychiatry : advancing science from genes to society · 2025Article
- Synuclein Proteoforms: Role in Health and Disease.Molecular neurobiology · 2025Review
- Pathological and physiological functional cross-talks of α-synuclein and tau in the central nervous system.Neural regeneration research · 2024Review
- Article
- Selective In Vitro and Ex Vivo Staining of Brain Neurofibrillary Tangles and Amyloid Plaques by Novel Ethylene Ethynylene-Based Optical Sensors.Biosensors · 2023Article
- Altered Cortical Palmitoylation Induces Widespread Molecular Disturbances in Parkinson's Disease.International journal of molecular sciences · 2022Article
- Functional Cooperation of α-Synuclein and Tau Is Essential for Proper Corticogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- The associations of cerebrospinal fluid biomarkers with cognition, and rapid eye movement sleep behavior disorder in early Parkinson's disease.Frontiers in neuroscience · 2022Article
- α-Synuclein modulates tau spreading in mouse brains.The Journal of experimental medicine · 2021Article
- Contactin-1 Is Reduced in Cerebrospinal Fluid of Parkinson's Disease Patients and Is Present within Lewy Bodies.Biomolecules · 2020Article
- Phosphorylation and oligomerization of α-synuclein associated with GSK-3β activation in the rTg4510 mouse model of tauopathy.Acta neuropathologica communications · 2020Article
- Modeling Parkinson's Disease Using Induced Pluripotent Stem Cells.Stem cells international · 2020Review
- Differential Aggregation and Phosphorylation of Alpha Synuclein in Membrane Compartments Associated With Parkinson Disease.Frontiers in neuroscience · 2019Article
- A Longitudinal Study of Total and Phosphorylated α-Synuclein with Other Biomarkers in Cerebrospinal Fluid of Alzheimer's Disease and Mild Cognitive Impairment.Journal of Alzheimer's disease : JAD · 2018Article
- Dementia Research Australia: the Australian Dementia Research Development Fellowship Program.Journal of molecular neuroscience : MN · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau and α-Synuclein (α-Syn) are abundant brain proteins with distinct biological functions. Findings suggest that interactions between α-Syn and tau at the cellular level cause disruption of cytoskeletal organization, axonal transport defects, and aberrant synaptic organization. The ability of tau and α-Syn to affect each other directly or indirectly might contribute to the overlap in the clinical and pathological features of tauopathies and synucleinopathies. The interactions between α-Syn and tau, and the underlying molecular pathogenic mechanisms, including induction and spread of protein aggregates, still deserve further investigation.
Indexed as
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What OpenQuestion holds
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.