Evidence map›Paper›PMID 40563464›Full record

ReviewBiomolecules2025

The Role and Pathogenesis of Tau Protein in Alzheimer's Disease.

Xiaoyue Hong, Linshu Huang, Fang Lei, Tian Li, Yi Luo, Mengliu Zeng, Zhuo Wang

Abstract readReview
In one paragraph

Review in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Neuroprotective Potential ofBiomolecules · 2026
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Advances in the treatment of Alzheimer's disease.Frontiers in pharmacology · 2026
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Xiaoyue HongDepartment of Laboratory Medicine, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.ORCID 0009-0009-3690-411X
Linshu HuangDepartment of Laboratory Medicine, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.
Fang LeiMedical Science Research Center, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.
Tian LiDepartment of Neurology, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.
Yi LuoDepartment of Laboratory Medicine, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.
Mengliu ZengMedical Science Research Center, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.
Zhuo WangMedical Science Research Center, Zhongnan Hospital of Wuhan University, Wuhan 430071, China.ORCID 0000-0001-9997-3109

Funding

Medical Sci-Tech Innovation Platform of Zhongnan Hospital, Wuhan University PTXM2024025, PTXM2025032National Natural Science Foundation of China 82071324, 82201589Natural Science Foundation of Hubei Province 2024AFB723, 2025AFC006Science and Technology Innovation Cultivation Fund of Zhongnan Hospital, Wuhan University CXPY2024074
6 · The paper itself

Abstract

Alzheimer's disease (AD), a predominant neurodegenerative disorder, is clinically characterized by progressive cognitive deterioration and behavioral deficits. An in-depth understanding of the pathogenesis and neuropathology of AD is essential for the development of effective treatments and early diagnosis techniques. The neuropathological signature of AD involves two hallmark lesions: intraneuronal neurofibrillary tangles composed of hyperphosphorylated tau aggregates and extracellular senile plaques containing amyloid-β (Aβ) peptide depositions. Although Aβ-centric research has dominated AD investigations over the past three decades, pharmacological interventions targeting Aβ pathology have failed to demonstrate clinical efficacy. Tau, a microtubule-associated protein predominantly localized to neuronal axons, orchestrates microtubule stabilization and axonal transport through dynamic tubulin interactions under physiological conditions. In AD pathogenesis, however, tau undergoes pathogenic post-translational modifications (PTMs), encompassing hyperphosphorylation, lysine acetylation, methylation, ubiquitination, and glycosylation. These PTM-driven alterations induce microtubule network disintegration, mitochondrial dysfunction, synaptic impairment, and neuroinflammatory cascades, ultimately culminating in irreversible neurodegeneration and progressive cognitive decline. This review synthesizes contemporary advances in tau PTM research and delineates their mechanistic contributions to AD pathogenesis, thereby establishing a framework for biomarker discovery, targeted therapeutic development, and precision medicine approaches in tauopathies. This review synthesizes contemporary advances in tau PTM research and delineates their mechanistic contributions to AD pathogenesis, thereby establishing a solid theoretical and experimental basis for the early diagnosis of neurodegenerative diseases, the discovery of therapeutic targets, and the development of novel therapeutic strategies.

Indexed as

Alzheimer Diseasetau ProteinsAnimalsBiomarkersHumansPhosphorylationProtein Processing, Post-TranslationalBiomarkerstau ProteinsacetylationAlzheimer’s diseasecognitive impairmenthyperphosphorylationpost-translational modificationssynaptic dysfunctiontau

Identifiers

PMID40563464
PMCPMC12190531

What Socratic holds

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Registered trials

None linked

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 Socratic graph.