<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>6(1)</volume><submitter>Pacheco S</submitter><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</pubmed_abstract><journal>JACS Au</journal><pagination>343-356</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12848675</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Phosphorylation of α‑Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR.</pubmed_title><pmcid>PMC12848675</pmcid><pubmed_authors>Siemer AB</pubmed_authors><pubmed_authors>Li S</pubmed_authors><pubmed_authors>Chen J</pubmed_authors><pubmed_authors>Velloor G</pubmed_authors><pubmed_authors>Pacheco S</pubmed_authors><pubmed_authors>Zhang Q</pubmed_authors><pubmed_authors>Reselammal DS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Phosphorylation of α‑Synuclein Fibrils at S129 Changes DNAJB1 Binding as Probed by Solid-State NMR.</name><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</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Jan</publication><modification>2026-06-14T06:01:31.957Z</modification><creation>2026-06-14T03:16:38.204Z</creation></dates><accession>S-EPMC12848675</accession><cross_references><pubmed>41614174</pubmed><doi>10.1021/jacsau.5c01266</doi></cross_references></HashMap>