{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["17"],"submitter":["Pahal S"],"pubmed_abstract":["<h4>Background</h4>Mitochondrial dysfunction and protein aggregation are central features of brain aging and Alzheimer's disease (AD). To define how AD seed proteins modulate these processes, we applied quantitative proteomics to sarkosyl-insoluble aggregates from <i>C. elegans</i> models of normal aging and from worms expressing human Aβ or Tau transgenes.<h4>Results</h4>Normal aging produced a late-onset accrual of mitochondrial proteins within aggregates, implicating impaired energy metabolism and proteostasis collapse. Aβ expression caused a striking expansion and included glycolytic enzymes, tricarboxylic acid cycle components, ribosomal proteins, and trafficking factors, consistent with broad proteostatic and bioenergetic stress, largely overlapping with aging-associated species, yet"],"journal":["Frontiers in aging neuroscience"],"pagination":["1713391"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12835372"],"repository":["biostudies-literature"],"pubmed_title":["The aggregate proteome of <i>Caenorhabditis elegans</i> mitochondria implicates shared mechanisms of aging and Alzheimer's disease."],"pmcid":["PMC12835372"],"pubmed_authors":["Ayyadevara S","Shmookler Reis RJ","Griffin ST","Pahal S","Ganne A","Balasubramaniam M"],"additional_accession":[]},"is_claimable":false,"name":"The aggregate proteome of <i>Caenorhabditis elegans</i> mitochondria implicates shared mechanisms of aging and Alzheimer's disease.","description":"<h4>Background</h4>Mitochondrial dysfunction and protein aggregation are central features of brain aging and Alzheimer's disease (AD). To define how AD seed proteins modulate these processes, we applied quantitative proteomics to sarkosyl-insoluble aggregates from <i>C. elegans</i> models of normal aging and from worms expressing human Aβ or Tau transgenes.<h4>Results</h4>Normal aging produced a late-onset accrual of mitochondrial proteins within aggregates, implicating impaired energy metabolism and proteostasis collapse. Aβ expression caused a striking expansion and included glycolytic enzymes, tricarboxylic acid cycle components, ribosomal proteins, and trafficking factors, consistent with broad proteostatic and bioenergetic stress, largely overlapping with aging-associated species, yet","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-06-16T03:20:01.665Z","creation":"2026-06-16T03:10:00.896Z"},"accession":"S-EPMC12835372","cross_references":{"pubmed":["41607505"],"doi":["10.3389/fnagi.2025.1713391"]}}