Tauopathies is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Tauopathies are a class of neurodegenerative /diseases(/diseases) defined by the pathological accumulation of abnormally hyperphosphorylated and aggregated tau] protein in the brain. Tau is a microtubule-associated protein encoded by the [MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- gene on chromosome 17q21, essential for microtubule stabilization, axonal transport, and neuronal cytoskeletal integrity. In tauopathies, tau dissociates from microtubules, becomes hyperphosphorylated, and self-assembles into insoluble paired helical filaments (PHFs) and straight filaments (SFs) that deposit as neurofibrillary tangles (NFTs), neuropil threads, and other tau inclusions (Goedert et al., 2017) (Structures et al., 2018).
Tauopathies encompass over 25 distinct clinicopathological entities, ranging from the highly prevalent Alzheimer's Disease (AD) to rare genetic frontotemporal dementias caused by [MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- mutations. The burden of tau pathology correlates more closely with clinical symptom severity and neuronal loss than [amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX-- plaques in AD, underscoring tau's central role in neurodegeneration (Nelson et al., 2012). Recent cryo-electron microscopy (cryo-EM) studies have revealed that each tauopathy features a unique tau filament fold, establishing a structure-based classification system that has transformed our understanding of these diseases (Shi et al., 2021) (Frontotemporal et al., 2015).
In the adult human brain, the [MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- gene produces six tau isoforms through alternative splicing of exons 2, 3, and 10. These isoforms differ in two features:
- N-terminal inserts: 0N (no inserts), 1N (exon 2), or 2N (exons 2 and 3)
- Microtubule-binding repeats: 3R (three repeats; exon 10 excluded) or 4R (four repeats; exon 10 included)
| Isoform |
Residues |
N-terminal |
Repeats |
Adult Brain Expression |
| 0N3R |
352 |
None |
3R |
~9% |
| 1N3R |
381 |
1 insert |
3R |
~54% (combined 3R) |
| 2N3R |
410 |
2 inserts |
3R |
~9% |
| 0N4R |
383 |
None |
4R |
~9% |
| 1N4R |
412 |
1 insert |
4R |
~54% (combined 4R) |
| 2N4R |
441 |
2 inserts |
4R |
~9% |
In the healthy adult brain, 3R and 4R tau are expressed at approximately equal levels. Perturbation of this 3R:4R ratio is pathogenic in several tauopathies.
Tau plays critical roles in:
- Microtubule stabilization: Binding and stabilizing microtubules, essential for axonal structure
- Axonal transport: Regulating kinesin and dynein motor protein trafficking along microtubules (- Signal transduction: Interacting with Fyn kinase, [GSK-3β[/entities/[gsk3-beta[/entities/[gsk3-beta[/entities/[gsk3-beta--TEMP--/entities)--FIX--, and other signaling molecules
- DNA protection: Nuclear tau protects against oxidative DNA damage (/mechanisms
- Synaptic function: Regulating synaptic plasticity and [NMDA receptor[/entities/[nmda-receptor[/entities/[nmda-receptor[/entities/[nmda-receptor--TEMP--/entities)--FIX-- receptor signaling
Tauopathies are fundamentally divided into two categories (Kovacs, 2015) (Invited et al., 2015):
Primary tauopathies: Tau is the primary (or sole) pathological hallmark, and [MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- mutations or haplotypes are the main genetic driver:
- Progressive Supranuclear Palsy (PSP)
- Corticobasal Degeneration (CBD)
- Pick's Disease
- FTLD-[MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- (Frontotemporal Dementia with [MAPT[/genes/[mapt[/genes/[mapt[/genes/[mapt--TEMP--/genes)--FIX-- mutations)
- Argyrophilic Grain Disease (AGD)
- Chronic Traumatic Encephalopathy (CTE)
- Primary Age-Related Tauopathy (PART)
- Globular glial tauopathy (GGT)
Secondary tauopathies: Tau pathology is present but accompanies another primary pathological hallmark:
- Alzheimer's Disease (AD) — tau + [amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX--
- Down Syndrome–Associated Alzheimer's — tau + [amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX--
- Lewy Body Dementia (DLB) — tau + [alpha-synuclein[/proteins/[alpha-synuclein[/proteins/[alpha-synuclein[/proteins/[alpha-synuclein--TEMP--/proteins)--FIX--; frontal-temporal atrophy |
| 4R tauopathies | PSP, CBD, AGD, GGT | Tufted [astrocytes[/cell-types/[astrocytes[/cell-types/[astrocytes[/cell-types/[astrocytes--TEMP--/cell-types)--FIX-- (PSP), astrocytic plaques (CBD), argyrophilic grains (AGD) |
| 3R+4R tauopathies | AD, CTE, PART, FTLD-[MAPT[/entities/[tau-protein[/entities/[tau-protein[/entities/[tau-protein--TEMP--/entities)--FIX-- (some) | NFTs containing both 3R and 4R tau isoforms |
The most revolutionary advance in tauopathy classification has come from cryo-EM determination of tau filament structures extracted from patient brains. Each tauopathy features a unique tau filament fold, providing a molecular fingerprint for disease classification (Shi et al., 2021; Falcon et al., 2018) (Novel et al., 2019):
| Tauopathy |
Fold Type |
Tau Repeats in Core |
Key Structural Features |
| AD |
Alzheimer fold |
R3-R4 + post-repeat |
C-shaped; paired helical and straight filaments |
| CTE |
CTE fold |
R3-R4 + post-repeat |
Similar to AD but with unique hydrophobic cavity |
| PART |
AD-like fold |
R3-R4 + post-repeat |
Identical to AD fold |
| Pick's Disease |
Pick fold |
R1-R3 (3R only) |
Elongated; distinct from all 4R folds |
| CBD |
CBD fold |
R2-R4 |
Four-layered; extensive β-helix |
| PSP |
PSP fold |
R1-R4 |
Three-layered; distinct from CBD despite clinical similarity |
| AGD |
AGD fold |
R2-R4 |
Four-layered; similar to CBD fold |
| GGT |
GGT fold |
R2-R4 |
Three-layered; similar to PSP fold |
Key insights from cryo-EM studies:
- PSP and CBD are structurally distinct: Despite clinical overlap, their tau filament folds are fundamentally different — PSP filaments resemble GGT, while CBD filaments resemble AGD (Shi et al., 2021)
- AD and CTE share similarities: Both feature 3R+4R tau with C-shaped folds, but CTE has a unique hydrophobic cavity that distinguishes it
- One fold per disease: Each tauopathy consistently features the same fold across all examined patients, suggesting the fold is disease-defining
Over 60 pathogenic mutations in the MAPT gene have been identified, predominantly causing Frontotemporal Dementia with parkinsonism linked to chromosome 17 (FTDP-17) (Ghetti et al., 2015):
Missense mutations: Affect tau's microtubule-binding capacity or aggregation propensity:
- P301L, P301S: Most common; impair microtubule binding and promote 4R tau aggregation; widely used in mouse models
- V337M, R406W: Promote PHF-like aggregation
- N279K, S305N: Increase exon 10 inclusion, elevating 4R:3R ratio
- G272V, ΔK280: Reduce microtubule binding and enhance aggregation
Splicing mutations: Alter the 3R:4R ratio by affecting exon 10 splicing:
- Intronic mutations in the stem-loop structure downstream of exon 10 increase 4R tau expression
- This imbalance alone is sufficient to cause neurodegeneration
The MAPT locus contains a ~900 kb inversion polymorphism defining two major haplotypes:
- H1 haplotype: Associated with increased risk of PSP, CBD, and Parkinson's Disease
- H2 haplotype: Protective; primarily found in European populations
-
**[APOE[/genes/[apoe[/genes/[apoe[/genes/[apoe--TEMP--/genes)--FIX--:
-
Kinases promoting pathological phosphorylation: [GSK-3β[/entities/[gsk3-beta[/entities/[gsk3-beta[/entities/[gsk3-beta--TEMP--/entities)--FIX--, [CDK5[/entities/[cdk5[/entities/[cdk5[/entities/[cdk5--TEMP--/entities)--FIX--, DYRK1A, MARK kinases, CK1
-
Phosphatases with reduced activity: [PP2A[/entities/[pp2a[/entities/[pp2a[/entities/[pp2a--TEMP--/entities)--FIX-- (responsible for ~70% of tau dephosphorylation; activity reduced ~50% in AD brain)
Hyperphosphorylation causes tau to:
- Lose affinity for microtubules → microtubule destabilization → axonal transport failure
- Gain self-association capacity → oligomer and fibril formation
- Become resistant to proteolytic degradation
Tau propagation occurs through a prion-like mechanism of templated misfolding and cell-to-cell transmission:
- Braak staging: Tau pathology in AD follows a stereotypical pattern from entorhinal [cortex[/brain-regions/[cortex[/brain-regions/[cortex[/brain-regions/[cortex--TEMP--/brain-regions)--FIX-- → [hippocampus[/brain-regions/[hippocampus[/brain-regions/[hippocampus[/brain-regions/[hippocampus--TEMP--/brain-regions)--FIX-- → neocortex (Braak staging)
- Trans-synaptic spreading: Tau seeds released from [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX-- are taken up by connected [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX--, where they template misfolding of endogenous tau
- Extracellular release: Via exosomes, extracellular vesicles, tunneling nanotubes, and direct secretion
- Strain-specific propagation: Different tau conformations (strains) maintain their structural properties during propagation, explaining disease-specific spreading patterns
Tau pathology causes neurodegeneration through multiple mechanisms:
- Microtubule destabilization: Loss of tau function disrupts axonal transport of mitochondria, synaptic vesicles, and organelles
- Synaptic dysfunction: Tau oligomers impair synaptic plasticity, [LTP[/entities/[long-term-potentiation[/entities/[long-term-potentiation[/entities/[long-term-potentiation--TEMP--/entities)--FIX--, and receptor trafficking
- Mitochondrial damage: Tau interacts with mitochondrial complex I and V, impairing oxidative stress and energy metabolism
- Nuclear dysfunction: Tau disrupts nuclear pore complexes and nucleocytoplasmic transport
- neuroinflammation: Tau activates [microglia[/cell-types/[microglia[/cell-types/[microglia[/cell-types/[microglia--TEMP--/cell-types)--FIX-- and [astrocytes)[/cell-types/[astrocytes[/cell-types/[astrocytes[/cell-types/[astrocytes--TEMP--/cell-types)--FIX--, sustaining inflammatory signaling and contributing to neurodegeneration.
PSP is the most common primary 4R tauopathy, characterized by:
- Classic Richardson syndrome: Vertical supranuclear gaze palsy, postural instability with early falls, axial rigidity, frontal cognitive decline
- Variant phenotypes: PSP-parkinsonism (PSP-P), PSP-corticobasal syndrome (PSP-CBS), PSP-frontal (PSP-F), PSP-progressive gait freezing (PSP-PGF)
- Neuropathology: Tufted [astrocytes[/cell-types/[astrocytes[/cell-types/[astrocytes[/cell-types/[astrocytes--TEMP--/cell-types)--FIX--, globose NFTs, neuropil threads; predominantly affecting basal ganglia, brainstem, and cerebellum
- Prevalence: 5-7 per 100,000; median survival 7-8 years
CBD is a 4R tauopathy presenting as (Novel et al., 2020):
- Corticobasal syndrome: Asymmetric rigidity, limb dystonia, alien limb phenomenon, cortical sensory loss, apraxia
- Other presentations: Frontal behavioral-spatial syndrome, progressive nonfluent aphasia, PSP-like syndrome
- Neuropathology: Astrocytic plaques (distinguishing feature from PSP), ballooned [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX--, thread-like tau pathology; asymmetric cortical and basal ganglia involvement
- Prevalence: 2-3 per 100,000; median survival 6-8 years
Pick's Disease is the primary 3R tauopathy, characterized by:
- Clinical features: Behavioral variant FTD (bvFTD), personality changes, language deficits, frontal-temporal atrophy
- Neuropathology: Round, silver-positive Pick bodies in [neurons[/entities/[neurons[/entities/[neurons[/entities/[neurons--TEMP--/entities)--FIX-- of cortical layers II and VI, dentate gyrus; circumscribed frontal and temporal lobe atrophy ("knife-edge" atrophy)
- Distinction: Can only be definitively diagnosed neuropathologically
CTE is a 3R+4R tauopathy caused by repetitive traumatic brain injury:
- Clinical features: Behavioral changes (aggression, impulsivity), mood disturbances (depression, suicidality), cognitive impairment, motor symptoms in advanced stages
- Neuropathology: Perivascular tau deposits at sulcal depths (pathognomonic), progressing from focal to widespread neocortical involvement across four stages
- Unique features: Environmental etiology (trauma), distinct cryo-EM fold with hydrophobic cavity
In AD, tau pathology follows Braak staging:
- Braak I-II: Entorhinal [cortex[/brain-regions/[cortex[/brain-regions/[cortex[/brain-regions/[cortex--TEMP--/brain-regions)--FIX-- (transentorhinal tau
- Braak III-IV: Limbic regions (hippocampal tau
- Braak V-VI: Neocortex (isocortical tau
Tau burden correlates better with cognitive decline and neuronal loss than amyloid plaque burden, supporting the "tau hypothesis" as a complement to the amyloid cascade hypothesis.
Tau PET tracers enable in vivo visualization of tau deposits:
- Flortaucipir (AV-1451/Tauvid): First FDA-approved tau PET tracer; binds preferentially to AD-type 3R+4R tau
- Second-generation tracers: PI-2620, MK-6240, GTP1, JNJ-311 — improved specificity, reduced off-target binding
- Limitations: Most tracers have higher affinity for AD tau folds than primary tauopathy folds (PSP, CBD), creating diagnostic challenges
- CSF p-tau181, [p-tau217[/entities/[p-tau217[/entities/[p-tau217[/entities/[p-tau217--TEMP--/entities)--FIX--, p-tau231: Reflect tau phosphorylation; highly specific for AD pathology; [p-tau217[/entities/[p-tau217[/entities/[p-tau217[/entities/[p-tau217--TEMP--/entities)--FIX-- shows strongest diagnostic accuracy (Palmqvist et al., 2020)
- Plasma p-tau: Blood-based tau biomarkers enabling screening; [p-tau217[/entities/[p-tau217[/entities/[p-tau217[/entities/[p-tau217--TEMP--/entities)--FIX-- in plasma shows >95% accuracy for AD vs. non-AD
- CSF total tau: Reflects neuronal injury; elevated in AD and rapidly progressive dementias (e.g., CJD)
- MTBR-tau243: Novel biomarker measuring tau microtubule-binding region; specific for primary tauopathies (PSP, CBD) (Horie et al., 2023)
- Seeded tau aggregation assays: Analogous to α-synuclein SAAs; under development for antemortem diagnosis of primary tauopathies
| Tauopathy |
Characteristic Imaging Findings |
| AD |
Medial temporal atrophy, posterior cingulate/precuneus hypometabolism |
| PSP |
Midbrain atrophy ("hummingbird sign"), third ventricle dilation |
| CBD |
Asymmetric cortical atrophy (frontoparietal), basal ganglia changes |
| Pick's Disease |
Frontal and temporal "knife-edge" atrophy |
| CTE |
Cavum septum pellucidum, medial temporal atrophy (diagnosed post-mortem) |
Several tau-targeting antibodies are in clinical development (tau-targeted therapeutics)):
- Semorinemab: Anti-tau antibody targeting N-terminus; Phase 2 in AD did not meet primary endpoint but showed trends in functional outcomes
- E2814: Anti-tau antibody targeting MTBR; in [DIAN]-TU trial for dominantly inherited AD ([DIAN] study)
- Bepranemab: Targets tau central region; Phase 2 for AD
- Zagotenemab: Targets aggregated tau; showed limited efficacy; development paused
- Methylene blue / LMTM (TRx0237): Inhibits tau aggregation; Phase 3 trials showed limited efficacy as monotherapy
- IONIS-MAPTRx (BIIB080): ASO targeting MAPT mRNA to reduce total tau production; Phase 1b showed dose-dependent CSF tau reduction; advancing in PSP and AD trials
- NIO752: Intrathecal ASO targeting MAPT; in clinical development
- [GSK-3β[/entities/[gsk3-beta[/entities/[gsk3-beta[/entities/[gsk3-beta--TEMP--/entities)--FIX-- inhibitors: Lithium, tideglusib — targeting tau phosphorylation; limited clinical success
- [CDK5[/entities/[cdk5[/entities/[cdk5[/entities/[cdk5--TEMP--/entities)--FIX-- modulators: Targeting p25/CDK5 hyperactivation
- DYRK1A inhibitors: Relevant for Down syndrome-associated tauopathy
- autophagy activation: [mTOR[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration[/mechanisms/[mtor-neurodegeneration--TEMP--/mechanisms)--FIX-- inhibitors, [TFEB[/entities/[tfeb[/entities/[tfeb[/entities/[tfeb--TEMP--/entities)--FIX-- activators to enhance tau degradation
- Ubiquitin-proteasome system: Targeted protein degradation (PROTACs) for tau
- Immunotherapy: Microglial phagocytosis of extracellular tau aggregates
- Tau PET-guided therapy: Using tau PET to select patients and monitor treatment response
- Gene therapy: AAV-mediated delivery of tau-targeting shRNAs or miRNAs
- Splicing modulators: Correcting 3R:4R tau ratio in splice-site mutation carriers
- Prion-like spreading inhibitors: Blocking tau release, uptake, or templating to stop propagation
| Model |
Tau Expression |
Key Features |
Commonly Used For |
| PS19 (P301S) |
Human 1N4R P301S |
NFT-like pathology, neuronal loss, motor deficits |
Tauopathy research, therapeutic testing |
| rTg4510 |
Human 0N4R P301L (inducible) |
Massive forebrain tau pathology, memory deficits |
Tau propagation, reversibility studies |
| hTau |
All 6 human isoforms (mouse MAPT KO) |
Both 3R and 4R pathology; slower progression |
AD-type tau research |
| THY-Tau22 |
Human 4R tau with G272V/P301S |
Progressive hippocampal tauopathy |
Behavioral studies |
- Injection of brain-derived tau filaments: Patient-derived tau seeds faithfully reproduce disease-specific pathology patterns in mice, confirming strain hypothesis
- Synthetic tau PFFs: Recombinant tau preformed fibrils enable controlled seeding experiments
- AAV-tau models: Viral vector delivery for region-specific tau expression
| Disease |
Category |
Prevalence |
Mean Onset |
Survival |
| AD |
Secondary (3R+4R) |
~11% over 65 |
65-75 years |
8-12 years |
| PSP |
Primary (4R) |
5-7/100,000 |
60-70 years |
7-8 years |
| CBD |
Primary (4R) |
2-3/100,000 |
60-70 years |
6-8 years |
| Pick's Disease |
Primary (3R) |
Rare |
40-60 years |
6-10 years |
| CTE |
Primary (3R+4R) |
Unknown (contact sports) |
Variable |
Variable |
| AGD |
Primary (4R) |
5-30% of autopsy cases |
>60 years (often incidental) |
Often asymptomatic |
| PART |
Primary (3R+4R) |
Very common in elderly |
>65 years |
Usually clinically silent |
- Cryo-EM-guided drug design: Using high-resolution filament structures to design fold-specific therapeutics and diagnostics
- Blood-based tau biomarkers: Plasma [p-tau217[/entities/[p-tau217[/entities/[p-tau217[/entities/[p-tau217--TEMP--/entities)--FIX--, p-tau181, and novel MTBR-tau species for early detection and screening
- Tau strain biology: Understanding how distinct tau conformations determine cell tropism, spreading patterns, and clinical phenotypes
- Tau PET for primary tauopathies: Developing tracers with improved affinity for 4R tau folds (PSP, CBD)
- Combination therapy: Targeting both tau and [amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta[/entities/[amyloid-beta--TEMP--/entities)--FIX-- in AD, or tau and neuroinflammation in primary tauopathies (Revisiting et al., 2025)
- Tau vaccines: Active immunization strategies to prevent tau seeding and propagation
- Single-cell transcriptomics: Identifying cell-type-specific vulnerability to tau pathology (selective neuronal vulnerability)
- Tau-Targeted Therapeutics
The study of Tauopathies has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Recent structural studies indicate that [tauopathies[/mechanisms/[tauopathies[/mechanisms/[tauopathies[/mechanisms/[tauopathies--TEMP--/mechanisms)--FIX-- are best interpreted through mutation-dependent fold diversity, context-dependent filament remodeling, and convergent AD-like conformers in specific MAPT genotypes.
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Goedert, M., et al. (2017). Tau filaments in neurodegenerative diseases. FEBS Letters, 591(13), 1978-1992. https://pubmed.ncbi.nlm.nih.gov/28643839/
-
Falcon, B., et al. (2018). Novel tau filament folds in neurodegenerative diseases. Acta Neuropathologica, 136(5), 709-717. https://pubmed.ncbi.nlm.nih.gov/29415014/
-
Nelson, P.T., et al. (2012). Correlation of Alzheimer's Disease neuropathologic changes with cognitive status. Journal of Neuropathology & Experimental Neurology, 71(5), 362-381. https://pubmed.ncbi.nlm.nih.gov/22325145/
-
Shi, Y., et al. (2021). Structure-based classification of tauopathies. Nature, 598(7880), 359-363. https://pubmed.ncbi.nlm.nih.gov/34588692/
-
Kovacs, G.G. (2015). Neuropathology of tauopathies. Handbook of Clinical Neurology, 130, 549-581. https://pubmed.ncbi.nlm.nih.gov/25604547/
-
Wang, Y., & Mandelkow, E. (2016). Tau in physiology and pathology. Nature Reviews Neuroscience, 17(1), 5-21. https://pubmed.ncbi.nlm.nih.gov/26651968/
-
Ballatore, C., Lee, V.M., & Trojanowski, J.Q. (2007). Tau-mediated neurodegeneration in Alzheimer's Disease and related disorders. Nature Reviews Neuroscience, 8(9), 663-672. https://pubmed.ncbi.nlm.nih.gov/11381127/
-
Fitzpatrick, A.W.P., et al. (2017). Cryo-EM structures of tau filaments from Alzheimer's Disease. Nature, 547(7662), 185-190. https://pubmed.ncbi.nlm.nih.gov/28678775/
-
Grundke-Iqbal, I., et al. (1986). Abnormal phosphorylation of the microtubule-associated protein tau in Alzheimer cytoskeletal pathology. Proceedings of the National Academy of Sciences, 83(13), 4913-4917. https://pubmed.ncbi.nlm.nih.gov/2424028/
-
Buée, L., et al. (2000). tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Research Reviews, 33(1), 95-130. https://pubmed.ncbi.nlm.nih.gov/10967355/
-
Hyman, B.T., et al. (2014). National Institute on Aging-Alzheimer's Association criteria for neuropathologic assessment of Alzheimer's Disease. Alzheimer's & Dementia, 10(4), 724-726. https://pubmed.ncbi.nlm.nih.gov/24774886/
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Lee et al., Repositioning of polyubiquitin alters the pathologic tau filament structure (2025)
-
Trojanowski et al., Traumatic brain injury or head impacts from contact sports are associated with tau astrogliopathy (2025)
-
Trojanowski et al., Deciphering distinct genetic risk factors for FTLD-TDP pathological subtypes via whole-genome sequencing (2025)
-
Goedert et al., Distinct tau filament folds in human MAPT mutants P301L and P301T (2025)
-
Goedert et al., Tau filaments with the Alzheimer fold in human MAPT mutants V337M and R406W (2025)
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Lee et al., ACSS2 upregulation enhances neuronal resilience to aging and tau-associated neurodegeneration (2026)
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Goedert et al., Seeding biosensor cell line that reproduces the Alzheimer tau fold (2025)
🟡 Moderate Confidence
| Dimension |
Score |
| Supporting Studies |
18 references |
| Replication |
0% |
| Effect Sizes |
50% |
| Contradicting Evidence |
0% |
| Mechanistic Completeness |
50% |
Overall Confidence: 45%