{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Montresor S"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["e16214"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11657929"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["169(1)"],"pubmed_abstract":["Chaperones safeguard protein homeostasis by promoting folding and preventing aggregation. HSP110 is a cytosolic chaperone that functions as a nucleotide exchange factor for the HSP70 cycle. Together with HSP70 and a J-domain protein (JDP), HSP110 maintains protein folding and resolubilizes aggregates. Interestingly, HSP110 is vital for the HSP70/110/JDP-mediated disaggregation of amyloidogenic proteins implicated in neurodegenerative diseases (i.e., α-synuclein, HTT, and tau). However, despite its abundance, HSP110 remains still an enigmatic chaperone, and its functional spectrum is not very well understood. Of note, the disaggregation activity of neurodegenerative disease-associated amyloid fibrils showed both beneficial and detrimental outcomes in vivo. To gain a more comprehensive under"],"journal":["Journal of neurochemistry"],"pubmed_title":["HSP110 is a modulator of amyloid beta (Aβ) aggregation and proteotoxicity."],"pmcid":["PMC11657929"],"funding_grant_id":["KI1988/3-2","KI1988/7‐1","KI1988/7-1","KI1988/3‐2"],"pubmed_authors":["Kelkar A","Basilicata L","Kirstein J","Kulkarni N","Secker L","Pigazzini ML","Baskaran S","Montresor S","Sleiman M","Adhikari G","Jacob N","Spellerberg P","Kalsi GK","Ehlert Y"],"additional_accession":[]},"is_claimable":false,"name":"HSP110 is a modulator of amyloid beta (Aβ) aggregation and proteotoxicity.","description":"Chaperones safeguard protein homeostasis by promoting folding and preventing aggregation. HSP110 is a cytosolic chaperone that functions as a nucleotide exchange factor for the HSP70 cycle. Together with HSP70 and a J-domain protein (JDP), HSP110 maintains protein folding and resolubilizes aggregates. Interestingly, HSP110 is vital for the HSP70/110/JDP-mediated disaggregation of amyloidogenic proteins implicated in neurodegenerative diseases (i.e., α-synuclein, HTT, and tau). However, despite its abundance, HSP110 remains still an enigmatic chaperone, and its functional spectrum is not very well understood. Of note, the disaggregation activity of neurodegenerative disease-associated amyloid fibrils showed both beneficial and detrimental outcomes in vivo. To gain a more comprehensive under","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2025-04-04T21:45:39.285Z","creation":"2025-04-04T21:45:39.285Z"},"accession":"S-EPMC11657929","cross_references":{"pubmed":["39180255"],"doi":["10.1111/jnc.16214"]}}