ReviewMolecular neurobiology2025
Tau Liquid-Liquid Phase Separation in Alzheimer's Disease: Mechanisms, Pathogenesis, and Therapeutic Implications.
Review in Molecular neurobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The relationship between total tau protein, phosphorylated tau protein, schizophrenia and bipolar disorder: a systematic review and meta-analysis.Frontiers in psychiatry · 2026Pooled it
- Helix-Aggregation Interplay in Nucleophosmin 1: Structural, Morphological, and Cytotoxic Consequences of Fragment Length.ACS omega · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Tau protein undergoes liquid-liquid phase separation (LLPS), forming dynamic condensates that act as intermediates in the transition to neurofibrillary tangles in Alzheimer's disease (AD). This review highlights tau's dynamic and reversible LLPS behavior, an underexplored aspect of tau's role, particularly as an early pathogenic driver in AD. We summarize the molecular mechanisms and regulatory factors governing tau LLPS, with a focus on its physiological functions in microtubule stability, synaptic activity, and cellular stress responses. Additionally, we discuss how metal ions, RNA, and neurodegenerative cofactors influence tau's phase behavior in a cell-type-specific manner. Emerging strategies targeting tau LLPS-such as nanobodies, AAV-based delivery, engineered degradation platforms, and CRISPR tools-show promise for early, reversible intervention. We also explore the potential of LLPS-informed biomarkers for diagnosing and monitoring disease progression. Overall, LLPS provides a dynamic, targetable framework linking early AD pathogenesis with therapeutic innovation, opening opportunities for earlier intervention and more effective treatment strategies.
Indexed as
Identifiers
41206815What 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.