{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Lin PH"],"funding":["Yen Tjing Ling Medical Foundation","National Science and Technology Council","Ministry of Education, Taiwan"],"pubmed_abstract":["Intrinsically disordered regions (IDRs) in proteins can undergo liquid-liquid phase separation (LLPS) for functional assembly, but this increases the chance of forming disease-associated amyloid fibrils. Not all amyloid fibrils form through LLPS however, and the importance of LLPS relative to other pathways in fibril formation remains unclear. We investigated this question in TDP-43, a motor neuron disease and dementia-causing protein that undergoes LLPS, using thioflavin T (ThT) fluorescence, NMR, transmission electron microscopy (TEM), and wide-angle X-ray scattering (WAXS) experiments. Using a fluorescence probe modified from ThT strategically designed for targeting protein assembly rather than β-sheets and supported by TEM images, we propose that the biphasic ThT signals observed under"],"journal":["ACS chemical neuroscience"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11488477"],"repository":["biostudies-literature"],"pubmed_title":["TDP-43 Amyloid Fibril Formation via Phase Separation-Related and -Unrelated Pathways."],"pmcid":["PMC11488477"],"funding_grant_id":["110-2113-M-A49A-504-MY3","112-2113-M-030-003","113-2113-M-A49-031-MY3","CI-110-16","CI-111-19"],"pubmed_authors":["Liu WM","Lin YH","Huang JR","Lin PH","Wu GW","Jeng US"],"additional_accession":[]},"is_claimable":false,"name":"TDP-43 Amyloid Fibril Formation via Phase Separation-Related and -Unrelated Pathways.","description":"Intrinsically disordered regions (IDRs) in proteins can undergo liquid-liquid phase separation (LLPS) for functional assembly, but this increases the chance of forming disease-associated amyloid fibrils. Not all amyloid fibrils form through LLPS however, and the importance of LLPS relative to other pathways in fibril formation remains unclear. We investigated this question in TDP-43, a motor neuron disease and dementia-causing protein that undergoes LLPS, using thioflavin T (ThT) fluorescence, NMR, transmission electron microscopy (TEM), and wide-angle X-ray scattering (WAXS) experiments. Using a fluorescence probe modified from ThT strategically designed for targeting protein assembly rather than β-sheets and supported by TEM images, we propose that the biphasic ThT signals observed under","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T09:33:47.4Z","creation":"2025-04-06T09:32:45.523Z"},"accession":"S-EPMC11488477","cross_references":{"pubmed":["39358890"],"doi":["10.1021/acschemneuro.4c00503"]}}