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ABSTRACT: Background
Alzheimer's disease (AD) is characterized by the presence of neurofibrillary tangles made of hyperphosphorylated tau and senile plaques composed of beta-amyloid. These pathognomonic deposits have been implicated in the pathogenesis, although the molecular mechanisms and consequences remain undetermined. UFM1 is an important, but understudied ubiquitin-like protein that is covalently attached to substrates. This UFMylation has recently been identified as major modifier of tau aggregation upon seeding in experimental models. However, potential alterations of the UFM1 pathway in human AD brain have not been investigated yet.Methods
Here we used frontal and temporal cortex samples from individuals with or without AD to measure the protein levels of the UFMylation pat
SUBMITTER: Yan T
PROVIDER: S-EPMC11188091 | biostudies-literature | 2024 May
REPOSITORIES: biostudies-literature