ReviewJournal of molecular neuroscience : MN2018
Tau Protein Squired by Molecular Chaperones During Alzheimer's Disease.
Review in Journal of molecular neuroscience : MN, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 94 citations in OpenAlex.
- Article
- Tau dysfunction in alzheimer's disease: molecular and cellular mechanisms, genetic modulation, and therapeutic perspectives.Molecular biology reports · 2026Review
- Tau-mediated Mechanisms in Alzheimer's Disease Pathogenesis.Molecular neurobiology · 2026Review
- Protein Modifications and Quality Control System: Target for Alzheimer's Disease Therapy.International journal of molecular sciences · 2026Review
- Post-translational modifications in alzheimer's disease: proteome dynamics and emerging therapeutic strategies.Metabolic brain disease · 2026Review
- Single-cell atlas of transcriptomic vulnerability across multiple neurodegenerative and neuropsychiatric diseases.medRxiv : the preprint server for health sciences · 2024Article
- Selenoprotein W modulates tau homeostasis in an Alzheimer's disease mouse model.Communications biology · 2024Article
- Chaperones-A New Class of Potential Therapeutic Targets in Alzheimer's Disease.International journal of molecular sciences · 2024Review
- Detection of APP gene recombinant in human blood plasma.Scientific reports · 2023Article
- Linking Heat Shock Protein 70 and Parkin in Parkinson's Disease.Molecular neurobiology · 2023Review
- siRNA drug delivery across the blood-brain barrier in Alzheimer's disease.Advanced drug delivery reviews · 2023Review
- Tau Protein Biosensors in the Diagnosis of Neurodegenerative Diseases.Advanced pharmaceutical bulletin · 2023Review
- Does modulation of tau hyperphosphorylation represent a reasonable therapeutic strategy for Alzheimer's disease? From preclinical studies to the clinical trials.Molecular psychiatry · 2023Review
- Microglia degrade Tau oligomers deposit via purinergic P2Y12-associated podosome and filopodia formation and induce chemotaxis.Cell & bioscience · 2023Article
- Energy Crisis Links to Autophagy and Ferroptosis in Alzheimer's Disease: Current Evidence and Future Avenues.Current neuropharmacology · 2023Article
- Glucose metabolism and AD: evidence for a potential diabetes type 3.Alzheimer's research & therapy · 2022Review
- α- Linolenic acid modulates phagocytosis and endosomal pathways of extracellular Tau in microglia.Cell adhesion & migration · 2021Article
- The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.The protein journal · 2021Review
- G-protein coupled receptor, PI3K and Rho signaling pathways regulate the cascades of Tau and amyloid-β in Alzheimer's disease.Molecular biomedicine · 2021Review
- Methylation as a key regulator of Tau aggregation and neuronal health in Alzheimer's disease.Cell communication and signaling : CCS · 2021Review
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
Abstract
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive neuronal loss, caused by misfolding and accumulation of tau and Amyloid β-42. Cellular mechanisms involving phosphatases, chaperones, ubiquitin proteasome system (UPS) and aggresomes solubilize or remove these toxic aggregates. Chaperones such as Hsp70 and Hsp90 functions in folding tau to its native form or in the downstream degrade and eliminated tau from the cell. Chaperones are involved in lysosomal degradation of tau by a process called chaperone mediated autophagy (CMA). In pathological conditions, chaperones fail to remove the toxic tau species, leading to their accumulation. In this scenario, inhibiting the chaperone activity would aid in overcoming AD. Small molecules inhibitors against chaperone activity are known to be effective in the clearance of aberrant tau from cell. In this review, the aspects of inhibition and prevention of tau aggregates formation are discussed in terms of chaperone activity and their small molecule modulators.
Indexed as
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.