Extended Data Fig. 5: Seeded aggregation of full-length 3R, but not 4R, tau by the sarkosyl-insoluble fraction from the brain of patient 4 with Pick’s disease.
From: Structures of filaments from Pick’s disease reveal a novel tau protein fold
a, Coomassie-stained SDS–PAGE of the 0N3R and 0N4R recombinant tau preparations used for seeded aggregation. Two additional recombinant tau preparations were performed with similar results. b, Thioflavin T fluorescence measurements of 0N3R (red) and 0N4R (blue) recombinant tau after incubation with (triangles) or without (circles) the sarkosyl-insoluble fraction from the frontotemporal cortex of patient 4. The results are from three independent experiments using separate recombinant protein preparations. The sarkosyl-insoluble fraction from Pick’s disease brain efficiently seeded the aggregation of 3R, but not 4R, tau. RFU, relative fluorescent units.
