Publisher Correction: Exploring the significance of caspase-cleaved tau in tauopathies and as a complementary pathology to phospho-tau in Alzheimer’s disease: implications for biomarker development and therapeutic targeting

Abstract

Figures

Pathological mechanisms induced by caspase-cleaved tau

Putative sites caspase-cleaved tau. Caspases 1, 3, 6, 7, and 8 cleave tau at D421. Caspase-2 cleaves tau also at D65 and D314, caspase-3 cleaves tau also at D25, caspase-6 cleaves tau also at D402 and D13. Tau consists of four domains: the projection domain (M1–Y197), a proline-rich region (P1 and P2), the microtubule-binding repeats (R1, R2, R3, R4), and a C-terminus domain (K369–L441). Amino acids 1-441

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Publisher Correction to:*** acta neuropathol commun***** 12**, 36 (2024)

10.1186/s40478-024-01744-9

Following the publication of the original article [1], it was noted that due to a typesetting error the figure legends were paired incorrectly. The figure legends for Figs. 1 and 2 were wrongly given as captions for Fig. 2, 1 respectively.

The publisher apologizes for the inconvenience caused.

Fig. 1. Pathological mechanisms induced by caspase-cleaved tau

Fig. 2. Putative sites caspase-cleaved tau. Caspases 1, 3, 6, 7, and 8 cleave tau at D421. Caspase-2 cleaves tau also at D65 and D314, caspase-3 cleaves tau also at D25, caspase-6 cleaves tau also at D402 and D13. Tau consists of four domains: the projection domain (M1–Y197), a proline-rich region (P1 and P2), the microtubule-binding repeats (R1, R2, R3, R4), and a C-terminus domain (K369–L441). Amino acids 1-441

The correct figures and captions have been included in this correction, and the original article [1] has been corrected.