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- W2893833768 abstract "Alzheimer’s disease (AD) comprises two major pathological hallmarks: extraneuronal deposition of β-amyloid (Aβ) peptides (“senile plaques”) and intraneuronal aggregation of the microtubule-associated protein tau (“neurofibrillary tangles”). Aβ is derived from sequential cleavage of the β-amyloid precursor protein by β- and γ-secretases, while aggregated tau is hyperphosphorylated in AD. Mounting evidence suggests that dysregulated trafficking of these AD-related proteins contributes to AD pathogenesis. Rab proteins are small GTPases that function as master regulators of vesicular transport and membrane trafficking. Multiple Rab GTPases have been implicated in AD-related protein trafficking, and their expression has been observed to be altered in postmortem AD brain. Here we review current implicated roles of Rab GTPase dysregulation in AD pathogenesis. Further elucidation of the pathophysiological role of Rab GTPases will likely reveal novel targets for AD therapeutics." @default.
- W2893833768 created "2018-10-05" @default.
- W2893833768 creator A5021602427 @default.
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- W2893833768 creator A5060805677 @default.
- W2893833768 creator A5065851220 @default.
- W2893833768 creator A5074999356 @default.
- W2893833768 date "2018-09-27" @default.
- W2893833768 modified "2023-10-16" @default.
- W2893833768 title "Role of Rab GTPases in Alzheimer’s Disease" @default.
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