ArticleInternational journal of Alzheimer's disease2011
Functional implications of glycogen synthase kinase-3-mediated tau phosphorylation.
Article in International journal of Alzheimer's disease, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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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.
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.
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Who cites it
53 citing papers in PubMed, 117 citations in OpenAlex.
- Current Landscape of Glycogen Synthase Kinase-3β PET Tracers: Progress, Limitations, and Perspectives-A Narrative Review.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- Progranulin deficiency in the brain activates an insulin signaling pathway that may promote neurodegeneration.iScience · 2026Article
- Septin crosstalk with microtubules and actin is regulated by a GSK3-dependent phosphoswitch.bioRxiv : the preprint server for biology · 2026Article
- ApoE4 Upregulates GSK-3β to Aggravate Alzheimer-Like Pathologies and Cognitive Impairment in Type 2 Diabetic Mice.CNS neuroscience & therapeutics · 2025Article
- Palmitic Acid Induces Posttranslational Modifications of Tau Protein in Alzheimer's Disease-Related Epitopes and Increases Intraneuronal Tau Levels.Molecular neurobiology · 2024Article
- Uncovering the Therapeutic Potential of Lithium Chloride in Type 2 Diabetic Cardiomyopathy: Targeting Tau Hyperphosphorylation and TGF-β Signaling via GSK-3β Inhibition.Pharmaceutics · 2024Article
- Article
- Spinocerebellar ataxia type 11 (SCA11): TTBK2 variants, functions and associated disease mechanisms.Cerebellum (London, England) · 2024Review
- P25/CDK5-mediated Tau Hyperphosphorylation in Both Ipsilateral and Contralateral Cerebra Contributes to Cognitive Deficits in Post-stroke Mice.Current medical science · 2023Article
- Elucidation of the GSK3α Structure Informs the Design of Novel, Paralog-Selective Inhibitors.ACS chemical neuroscience · 2023Article
- Direct and Indirect Effects of Filamin A on Tau Pathology in Neuronal Cells.Molecular neurobiology · 2023Article
- String/Cdc25 phosphatase is a suppressor of Tau-associated neurodegeneration.Disease models & mechanisms · 2023Article
- Validating MARK2 Gene Polymorphism as a Predictor of Response to Lithium Treatment in Bipolar PatientsIranian biomedical journal · 2022Article
- Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.Protein science : a publication of the Protein Society · 2021Review
- Chalcone and its analogs: Therapeutic and diagnostic applications in Alzheimer's disease.Bioorganic chemistry · 2021Review
- Differential effects of putative N-glycosylation sites in human Tau on Alzheimer's disease-related neurodegeneration.Cellular and molecular life sciences : CMLS · 2021Article
- Review
- Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution.Science advances · 2020Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tau is primarily a neuronal microtubule-associated protein that has functions related to the stabilisation of microtubules. Phosphorylation of tau is an important dynamic and regulatory element involved in the binding of tau to tubulin. Thus, highly phosphorylated tau is more likely to be present in the cytosolic compartment of neurons, whereas reduced phosphate burden allows tau to bind to and stabilise the microtubule cytoskeleton. Highly phosphorylated forms of tau are deposited in the brain in a range of neurodegenerative disorders including Alzheimer's disease, progressive supranuclear palsy, and frontotemporal lobar degeneration associated with Pick bodies. A key candidate kinase for both physiological and pathological tau phosphorylation is glycogen synthase kinase-3 (GSK-3). Multiple phosphorylation sites have been identified on tau exposed to GSK-3 in vitro and in cells. In this review, we highlight recent data suggesting a role for GSK-3 activity on physiological tau function and on tau dysfunction in neurodegenerative disease.
Identifiers
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.