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- W2775806608 abstract "Abstract Familial mutations in C99 can increase the total level of the soluble Aβ peptides produced by proteolysis, as well as the Aβ42/Aβ40 ratio, both of which are linked to the progression of Alzheimer’s disease. We show that the extracellular sequence of C99 forms β-sheet structure upon interaction with membrane bilayers. Mutations that disrupt this structure result in a significant increase in Aβ production and, in specific cases, result in an increase in the amount of Aβ42 relative to Aβ40. Fourier transform infrared and solid-state NMR spectroscopic studies reveal a central β-hairpin within the extracellular sequence comprising Y10-E11-V12 and L17-V18-F19 connected by a loop involving H13-H14-Q15. These results suggest how familial mutations in the extracellular sequence influence C99 processing and provide a structural basis for the development of small molecule modulators that would reduce Aβ production." @default.
- W2775806608 created "2017-12-22" @default.
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- W2775806608 date "2017-12-07" @default.
- W2775806608 modified "2023-09-26" @default.
- W2775806608 title "β-Sheet Structure within the Extracellular Domain of C99 Regulates Amyloidogenic Processing" @default.
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- W2775806608 doi "https://doi.org/10.1038/s41598-017-17144-0" @default.
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