Modified TDP-43 (phosphorylation, ubiquitination) in AD neurons undergoes altered LLPS behavior, forming pathologically stable stress granules that outcompete transient, functional granules. This TDP-43 condensate dominance displaces essential RNA processing factors (TIA1, G3BP1, hnRNP A1) into aggregation-prone states, mirroring the RBM45 hijacking mechanism observed in ALS. The prediction is that AD-associated TDP-43 modifications increase stress granule dwell time and promote co-aggregation o
Radar Chart — 10 Dimensions
Score Comparison Bars
Mechanistic
0.65
Evidence
0.60
Novelty
0.70
Feasibility
0.00
Impact
0.00
Druggability
0.00
Safety
0.00
Competition
0.00
Data
0.00
Reproducible
0.00
KG Connect
0.50
Score Breakdown
Dimension
TDP-43 Liquid-Liquid Phase Sep
Mechanistic
0.650
Evidence
0.600
Novelty
0.700
Feasibility
0.000
Impact
0.000
Druggability
0.000
Safety
0.000
Competition
0.000
Data
0.000
Reproducible
0.000
KG Connect
0.500
Evidence
TDP-43 Liquid-Liquid Phase Separation Dominance in Stress Gr