Enzymatic removal of specific glycan modifications from tau vesicle surfaces using targeted glycosidases could disrupt the molecular interactions that promote tau aggregation, effectively 'dissolving' the pathological protein networks by altering their surface chemistry.
Auto-built from this analysis's top knowledge-graph edges.
graph TD
HK1["HK1"] -->|participates in| glucose_metabolism["glucose_metabolism"]
ST6GAL1["ST6GAL1"] -->|regulates| sialylation["sialylation"]
MAPT["MAPT"] -->|participates in| vesicle_transport["vesicle_transport"]
ST6GAL1_1["ST6GAL1"] -->|catalyzes| sialylation_2["sialylation"]
LGALS3["LGALS3"] -->|regulates| autophagy["autophagy"]
MGAT5["MGAT5"] -->|catalyzes| N_glycosylation["N_glycosylation"]
glycan_patterns["glycan_patterns"] -->|characterizes| tau_vesicles["tau_vesicles"]
n2_deoxy_D_glucose_analogs["2-deoxy-D-glucose analogs"] -->|disrupts| glycosylation_patterns["glycosylation patterns"]
LGALS3_3["LGALS3"] -->|targets| tau_vesicles_4["tau_vesicles"]
MGAT5_5["MGAT5"] -->|marks| tau_vesicles_6["tau_vesicles"]
NEU1["NEU1"] -.->|inhibits| tau_aggregation["tau_aggregation"]
synthetic_glycan_mimetics["synthetic_glycan_mimetics"] -.->|inhibits| tau_spreading["tau_spreading"]
style HK1 fill:#ce93d8,stroke:#333,color:#000
style glucose_metabolism fill:#81c784,stroke:#333,color:#000
style ST6GAL1 fill:#ce93d8,stroke:#333,color:#000
style sialylation fill:#ffd54f,stroke:#333,color:#000
style MAPT fill:#ce93d8,stroke:#333,color:#000
style vesicle_transport fill:#4fc3f7,stroke:#333,color:#000
style ST6GAL1_1 fill:#ce93d8,stroke:#333,color:#000
style sialylation_2 fill:#4fc3f7,stroke:#333,color:#000
style LGALS3 fill:#ce93d8,stroke:#333,color:#000
style autophagy fill:#4fc3f7,stroke:#333,color:#000
style MGAT5 fill:#ce93d8,stroke:#333,color:#000
style N_glycosylation fill:#4fc3f7,stroke:#333,color:#000
style glycan_patterns fill:#4fc3f7,stroke:#333,color:#000
style tau_vesicles fill:#4fc3f7,stroke:#333,color:#000
style n2_deoxy_D_glucose_analogs fill:#4fc3f7,stroke:#333,color:#000
style glycosylation_patterns fill:#4fc3f7,stroke:#333,color:#000
style LGALS3_3 fill:#4fc3f7,stroke:#333,color:#000
style tau_vesicles_4 fill:#4fc3f7,stroke:#333,color:#000
style MGAT5_5 fill:#ce93d8,stroke:#333,color:#000
style tau_vesicles_6 fill:#4fc3f7,stroke:#333,color:#000
style NEU1 fill:#ce93d8,stroke:#333,color:#000
style tau_aggregation fill:#4fc3f7,stroke:#333,color:#000
style synthetic_glycan_mimetics fill:#4fc3f7,stroke:#333,color:#000
style tau_spreading fill:#4fc3f7,stroke:#333,color:#000No linked papers recorded for this hypothesis yet.
No curated PDB or AlphaFold mapping for NEU1 yet. Search RCSB →
No clinical trials data linked to this hypothesis yet.
No curated ClinVar variants loaded for this hypothesis.
Run scripts/backfill_clinvar_variants.py to fetch P/LP/VUS variants.
No DepMap CRISPR Chronos data found for NEU1.
Run python3 scripts/backfill_hypothesis_depmap.py to populate.
| Prediction | Predicted | Observed | Status | Conf |
|---|---|---|---|---|
| IF NEU1 is overexpressed (≥3-fold endogenous levels) in human neuroblastoma cells inducibly expressing tau, THEN extracellular tau concentration in conditioned media at 72 hours will decrease by at le | Extracellular tau ELISA signal reduced to ≤60% of vector control levels, with corresponding increase in intracellulartau showing impaired secretion | — no observation — | pending | 0.30 |
| IF recombinant tau protein is pre-treated with neuraminidase (to remove terminal sialic acid residues) PRIOR to aggregation induction, THEN Thioflavin-S fluorescence signal at 48 hours will be reduced | Thioflavin-S fluorescence signal ≤70% of vehicle-treated tau aggregation controls | — no observation — | pending | 0.35 |