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Engineered antibody therapies to counteract mutant huntingtin and related toxic intracellular proteins
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Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress
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Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
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Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
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Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease
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HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species
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Engineering a membrane protein chaperone to ameliorate the proteotoxicity of mutant huntingtin
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PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
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Tuning Hsp104 specificity to selectively detoxify α-synuclein
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Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events
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Mining disaggregase sequence space to safely counter TDP-43, FUS, and α-synuclein proteotoxicity
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YocM a small heat shock protein can protect Bacillus subtilis cells during salt stress
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Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
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The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase
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Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity
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Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation
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Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity
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The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation
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Hspb7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones
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The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
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Protein folding: versatility of the cytosolic chaperonin TRiC/CCT
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The nascent polypeptide-associated complex (NAC) as regulatory hub on ribosomes
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The nascent polypeptide-associated complex is a key regulator of proteostasis
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Processive extrusion of polypeptide loops by a Hsp100 disaggregase
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The ATPase VCP/p97 functions as a disaggregase against toxic huntingtin-exon1 aggregates
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Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle
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Differential roles for DNAJ isoforms in HTT-polyQ and FUS aggregation modulation revealed by chaperone screens
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Autophagy preferentially degrades non-fibrillar polyQ aggregates
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The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species
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Human Hsp70 disaggregase reverses Parkinson's-linked α-synuclein amyloid fibrils
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A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy
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Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
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DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios
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The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides
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A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
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ER stress causes widespread protein aggregation and prion formation
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Two novel DNAJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington's disease related aggregates
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Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease
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