{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Ramani B"],"funding":["NINDS NIH HHS"],"pubmed_abstract":["Polyglutamine (polyQ) diseases, including Huntington's disease and several spinocerebellar ataxias, are caused by abnormally expanded CAG nucleotide repeats, which encode aggregation-prone polyQ tracts. Substantial prior evidence supports a pathogenic role for polyQ protein misfolding and aggregation, with molecular chaperones showing promise in suppressing disease phenotypes in cellular and animal models. In this study, we developed a FRET-based reporter system that models polyQ aggregation in human cells and used it to perform a high-throughput CRISPR interference screen targeting all known molecular chaperones. This screen identified as a strong suppressor of polyQ aggregation the Hsp40 co-chaperone DNAJC7, which has previously been shown to modify aggregation of other disease proteins "],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.08.10.669490"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12363876"],"repository":["biostudies-literature"],"pubmed_title":["The Hsp40 co-chaperone DNAJC7 modifies polyglutamine but not polyglycine aggregation."],"pmcid":["PMC12363876"],"funding_grant_id":["K08 NS133300","R25 NS070680"],"pubmed_authors":["Ramani B","Ehsani K","Kampmann M"],"additional_accession":[]},"is_claimable":false,"name":"The Hsp40 co-chaperone DNAJC7 modifies polyglutamine but not polyglycine aggregation.","description":"Polyglutamine (polyQ) diseases, including Huntington's disease and several spinocerebellar ataxias, are caused by abnormally expanded CAG nucleotide repeats, which encode aggregation-prone polyQ tracts. Substantial prior evidence supports a pathogenic role for polyQ protein misfolding and aggregation, with molecular chaperones showing promise in suppressing disease phenotypes in cellular and animal models. In this study, we developed a FRET-based reporter system that models polyQ aggregation in human cells and used it to perform a high-throughput CRISPR interference screen targeting all known molecular chaperones. This screen identified as a strong suppressor of polyQ aggregation the Hsp40 co-chaperone DNAJC7, which has previously been shown to modify aggregation of other disease proteins ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-07-11T03:16:39.232Z","creation":"2026-07-11T03:08:31.708Z"},"accession":"S-EPMC12363876","cross_references":{"pubmed":["40832276"],"doi":["10.1101/2025.08.10.669490"]}}