Alzheimer’s-causing mutations shift Aβ length by destabilizing γ-secretase-Aβn interactions

(Cell 170, 443–456.e1–e14; July 27, 2017) Our paper reported that Alzheimer’s disease-linked mutations in Presenilin and the amyloid precursor protein (APP) destabilize interactions between gamma-secretase APP leading to production of longer beta peptides. We have identified two errors Figure 3C manuscript. During preparation final figures, we mislabeled temperature values for PSEN1 mutants. They should appear as 37, 41.3, 45.7, 51, 55.1, 58.1, 60, 65 °C. Instead, figure displays 62.5, Additionally, image R278I mutant was truncated omitting part lane. This has been replaced with full size blot. These changes corrected below. do not affect results presented or interpretation data. The authors apologize readers any confusion these may caused. Alzheimer’s-Causing Mutations Shift Aβ Length by Destabilizing γ-Secretase-Aβn InteractionsSzaruga et al.CellJuly 2017In BriefSequential γ-secretase cuts on generates progressively less stable enzyme-substrate (E-S) complexes. disease–causing E-S complexes thereby enhance amyloidogenic production. Full-Text PDF Open Archive