{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Yan T"],"funding":["NIA NIH HHS"],"pubmed_abstract":["<h4>Background</h4>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.<h4>Methods</h4>Here we used frontal and temporal cortex samples from individuals with or without AD to measure the protein levels of the UFMylation pat"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.05.24.595755"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11188091"],"repository":["biostudies-literature"],"pubmed_title":["The UFMylation pathway is impaired in Alzheimer's disease."],"pmcid":["PMC11188091"],"funding_grant_id":["R56 AG062556"],"pubmed_authors":["Dickson DW","Fiesel FC","Murray ME","Heckman MG","Liu CC","Bu G","Craver EC","Yan T","Lou Z","Springer W","Wang X","Rawlinson BD","Ertekin-Taner N"],"additional_accession":[]},"is_claimable":false,"name":"The UFMylation pathway is impaired in Alzheimer's disease.","description":"<h4>Background</h4>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.<h4>Methods</h4>Here we used frontal and temporal cortex samples from individuals with or without AD to measure the protein levels of the UFMylation pat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-15T03:17:16.994Z","creation":"2026-06-15T03:08:49.984Z"},"accession":"S-EPMC11188091","cross_references":{"pubmed":["38903110"],"doi":["10.1101/2024.05.24.595755"]}}