{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6(1)"],"submitter":["Pacheco S"],"pubmed_abstract":["Amyloid fibrils formed by the protein α-synuclein are implicated in the pathogenesis of synucleinopathies. In addition to their rigid cross-β core, these fibrils have intrinsically disordered regions on their surface, which are important for interactions with other cellular components, such as chaperones. Chaperones play a vital role in preventing and reversing amyloid formation in neurodegenerative diseases. How they recognize misfolded proteins is an active field of research. DNAJB1 is a cochaperone that recognizes fibrils and recruits other chaperones such as Hsp70 and Apg2, which collectively disaggregate fibrils formed by α-synuclein, tau, and huntingtin. Because DNAJB1 was reported to bind the C-terminus of α-synuclein and S129 in this C-terminus is predominantly phosphorylated in pa"],"journal":["JACS Au"],"pagination":["343-356"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12848675"],"repository":["biostudies-literature"],"pubmed_title":["Phosphorylation of α‑Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR."],"pmcid":["PMC12848675"],"pubmed_authors":["Siemer AB","Li S","Chen J","Velloor G","Pacheco S","Zhang Q","Reselammal DS"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation of α‑Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR.","description":"Amyloid fibrils formed by the protein α-synuclein are implicated in the pathogenesis of synucleinopathies. In addition to their rigid cross-β core, these fibrils have intrinsically disordered regions on their surface, which are important for interactions with other cellular components, such as chaperones. Chaperones play a vital role in preventing and reversing amyloid formation in neurodegenerative diseases. How they recognize misfolded proteins is an active field of research. DNAJB1 is a cochaperone that recognizes fibrils and recruits other chaperones such as Hsp70 and Apg2, which collectively disaggregate fibrils formed by α-synuclein, tau, and huntingtin. Because DNAJB1 was reported to bind the C-terminus of α-synuclein and S129 in this C-terminus is predominantly phosphorylated in pa","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-14T06:01:31.957Z","creation":"2026-06-14T03:16:38.204Z"},"accession":"S-EPMC12848675","cross_references":{"pubmed":["41614174"],"doi":["10.1021/jacsau.5c01266"]}}