{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brooks C"],"funding":["NEI NIH HHS","NIA NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["e0308058"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11449290"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(10)"],"pubmed_abstract":["Neurodegenerative diseases are characterized by the presence of misfolded and aggregated proteins which are thought to contribute to the development of the disease. In one form of inherited blinding disease, retinitis pigmentosa, a P23H mutation in the light-sensing receptor, rhodopsin causes rhodopsin misfolding resulting in complete vision loss. We investigated whether a xenogeneic protein-unfolding ATPase (unfoldase) from thermophilic Archaea, termed PANet, could counteract the proteotoxicity of P23H rhodopsin. We found that PANet increased the number of surviving photoreceptors in P23H rhodopsin mice and recognized rhodopsin as a substate in vitro. This data supports the feasibility and efficacy of using a xenogeneic unfoldase as a therapeutic approach in mouse models of human neurodeg"],"journal":["PloS one"],"pubmed_title":["Therapeutic potential of archaeal unfoldase PANet and the gateless T20S proteasome in P23H rhodopsin retinitis pigmentosa mice."],"pmcid":["PMC11449290"],"funding_grant_id":["R01 GM107129","R01 AG064188","GM107129","EY030050","R01 EY030056"],"pubmed_authors":["Schupp J","Kolson D","Billington N","Smith D","Chuah J","Brooks C","Sechrest E","Deng WT","Sokolov M"],"additional_accession":[]},"is_claimable":false,"name":"Therapeutic potential of archaeal unfoldase PANet and the gateless T20S proteasome in P23H rhodopsin retinitis pigmentosa mice.","description":"Neurodegenerative diseases are characterized by the presence of misfolded and aggregated proteins which are thought to contribute to the development of the disease. In one form of inherited blinding disease, retinitis pigmentosa, a P23H mutation in the light-sensing receptor, rhodopsin causes rhodopsin misfolding resulting in complete vision loss. We investigated whether a xenogeneic protein-unfolding ATPase (unfoldase) from thermophilic Archaea, termed PANet, could counteract the proteotoxicity of P23H rhodopsin. We found that PANet increased the number of surviving photoreceptors in P23H rhodopsin mice and recognized rhodopsin as a substate in vitro. This data supports the feasibility and efficacy of using a xenogeneic unfoldase as a therapeutic approach in mouse models of human neurodeg","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-06-13T05:33:14.639Z","creation":"2025-04-06T13:20:58.465Z"},"accession":"S-EPMC11449290","cross_references":{"pubmed":["39361629"],"doi":["10.1371/journal.pone.0308058"]}}