Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Open accessAbstract
Tau protein plays a critical role in the assembly, stabilization, and modulation of microtubules, which are important for the normal function of neurons and the brain. In diseased conditions, several pathological modifications of tau protein manifest. These changes lead to tau protein aggregation and the formation of paired helical filaments (PHF) and neurofibrillary tangles (NFT), which are common hallmarks of Alzheimer’s disease and other tauopathies. The accumulation of PHFs and NFTs results in impairment of physiological functions, apoptosis, and neuronal loss, which is reflected as cognitive impairment, and in the late stages of the disease, leads to death. The causes of this pathological transformation of tau protein haven’t been fully understood yet. In both physiological and pathological conditions, tau interacts with several proteins which maintain their proper function or can participate in their pathological modifications. Interaction partners of tau protein and associated molecular pathways can either initiate and drive the tau pathology or can act neuroprotective, by reducing pathological tau proteins or inflammation. In this review, we focus on the tau as a multifunctional protein and its known interacting partners active in regulations of different processes and the roles of these proteins in Alzheimer’s disease and tauopathies.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The accumulation of tau protein in neurofibrillary tangles, known as tau protein modulation, provides a novel venue for disease modification.
“The accumulation of tau protein in neurofibrillary tangles, which is known as tau protein modulation, provides a novel venue for disease modification.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [198]
The goal of tau treatments is to prevent tau from aggregating and spreading.
“The goal of tau treatments is to prevent tau from aggregating and spreading.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [198]
Numerous approaches, such as tau aggregation inhibitors, are being studied to address the tau protein problem and prevent tau tangle formation.
“Numerous approaches, such as tau aggregation inhibitors, are being studied in an effort to address the tau protein problem and prevent tau tangle formation.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [198]
There is evidence that tau vaccinations may slow the disease's course by reducing tau protein accumulation.
“First, there is evidence that tau vaccinations may slow the disease’s course by reducing tau protein accumulation [198,199,200,201].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [198]
Techniques for tau immunotherapy, such as those being tried with AADvac1, function by teaching the immune system to eliminate aberrant tau proteins from the brain.
“Techniques for tau immunotherapy, such as those being tried with AADvac1, function by teaching the immune system to eliminate aberrant tau proteins from the brain.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [198]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
The citation lists haven’t been fetched yet
References 650 · Cited by 220
Research works printed but not linked: 1
- [120]Goldman R.D. Steinert P.M. Cellular and Molecular Biology of Intermediate Filaments Springer Science & Business Media New York, NY, USA 2013
- Authors
- Sinsky, J., Pichlerova, K., & Hanes, J.
- Affiliations
- Institute of Neuroimmunology, Slovak Academy of Sciences, Dubravska Cesta 9, 845 10 Bratislava, Slovakia
- Slovak Academy of Sciences (SK)
- Corresponding author
- Hanes, Jozef
- ORCID
- Hanes, Jozef
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2021-08-26
- Volume
- 22
- Issue
- 17
- Pages
- 9207
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC8431036
- OpenAlex
- W3195441701
- Cited by
- 220
- References
- 650
- Citations by year
- 2026: 35 · 2025: 83 · 2024: 55 · 2023: 27 · 2022: 15 · 2021: 4
- FWCI
- 3.37
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Agentúra na Podporu Výskumu a Vývoja (APVV-16-0531 and APVV-18-0302)
- Vedecká Grantová Agentúra MŠVVaŠ SR a SAV (VEGA 2/0123/21 and VEGA 2/0150/19)
- SAS Grants for Phd Students (APP0040)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, tauopathy, Alzheimer's disease, protein-protein interaction, microtubule stabilization, tau aggregation, paired helical filaments, neurofibrillary tangles, neuroprotection, neuroinflammation, apoptosis, cognitive impairment
- MeSH terms
- Alzheimer Disease, Animals, Carrier Proteins, Disease Susceptibility, Humans, Neurons, Protein Binding, Protein Processing, Post-Translational, Signal Transduction, Biomarkers, tau Proteins, Tauopathies, Proteolysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
