Research graph
References from Chaperone-mediated remodelling of mutant huntingtin. Local targets link to admitted publications; unresolved targets remain external evidence.
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
10.1016/0092-8674(93)90585-e · 1993 · External reference
Glutamine repeats and neurodegeneration
10.1146/annurev.neuro.23.1.217 · 2000 · External reference
Interrupting sequence variants and age of onset in Huntington's disease: clinical implications and emerging therapies
10.1016/s1474-4422(20)30343-4 · 2020 · External reference
Somatic expansion of the Huntington's disease CAG repeat in the brain is associated with an earlier age of disease onset
10.1093/hmg/ddp242 · 2009 · External reference
Genetic polymorphisms adjacent to the CAG repeat influence clinical features at onset in Huntington's disease
10.1136/jnnp.64.6.758 · 1998 · External reference
Huntington's disease
10.1016/s0140-6736(07)60111-1 · 2007 · External reference
The biology of huntingtin
10.1016/j.neuron.2016.02.003 · 2016 · External reference
Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
10.1016/j.cell.2006.04.026 · 2006 · External reference
Regulatory mechanisms of incomplete huntingtin mRNA splicing
10.1038/s41467-018-06281-3 · 2018 · External reference
Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
10.1126/science.277.5334.1990 · 1997 · External reference
Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
10.1016/s0092-8674(00)80513-9 · 1997 · External reference
Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
10.1016/s0092-8674(00)81369-0 · 1996 · External reference
Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
10.1016/s0092-8674(00)80514-0 · 1997 · External reference
Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
10.1038/nature01301 · 2003 · External reference
Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
10.1074/jbc.m205809200 · 2002 · External reference
Acetylation within the first 17 residues of huntingtin exon 1 alters aggregation and lipid binding
10.1016/j.bpj.2016.06.018 · 2016 · External reference
The emerging role of the first 17 amino acids of huntingtin in Huntington's disease
10.1515/bmc-2015-0001 · 2015 · External reference
Structure and dynamics of the Huntingtin exon-1 N-terminus: a solution NMR perspective
10.1021/jacs.6b10893 · 2017 · External reference
Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect
10.1016/j.bpj.2009.07.062 · 2009 · External reference
Critical role of the proline-rich region in huntingtin for aggregation and cytotoxicity in yeast
10.1074/jbc.m605558200 · 2006 · External reference
Oligoproline effects on polyglutamine conformation and aggregation
10.1016/j.jmb.2005.10.053 · 2006 · External reference
The structure and function of proline-rich regions in proteins
10.1042/bj2970249 · 1994 · External reference
PPII propensity of multiple-guest amino acids in a proline-rich environment
10.1021/jp203874f · 2011 · External reference
The importance of being proline: the interaction of proline-rich motifs in signalling proteins with their cognate domains
10.1096/fasebj.14.2.231 · 2000 · External reference
Protein sequences encode safeguards against aggregation
10.1002/humu.20905 · 2009 · External reference
An expanded polyproline domain maintains mutant huntingtin soluble in vivo and during aging
10.3389/fnmol.2021.721749 · 2021 · External reference
Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin
2013 · External reference
Flanking regions determine the structure of the poly-glutamine in huntingtin through mechanisms common among glutamine-rich Human proteins
2020 · External reference
Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
10.1021/bi992933h · 2000 · External reference
Mechanism of prion propagation: amyloid growth occurs by monomer addition
10.1371/journal.pbio.0020321 · 2004 · External reference
Kinetics and thermodynamics of amyloid fibril assembly
10.1021/ar050069h · 2006 · External reference
Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides
10.1016/j.bpc.2011.04.006 · 2011 · External reference
Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties
10.1021/bi3000929 · 2012 · External reference
Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation
2013 · External reference
A liquid to solid phase transition underlying pathological huntingtin Exon1 aggregation
10.1016/j.molcel.2018.04.007 · 2018 · External reference
Amyloid fibril polymorphism: structural mechanisms of assembly and the links to disease
10.1016/j.sbi.2026.103245 · 2026 · External reference
A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
10.1016/j.celrep.2014.09.042 · 2014 · External reference
Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs
10.1016/0022-2836(74)90447-1 · 1974 · External reference
Chaperone proteins: universal roles in surviving environmental stress
10.1007/s12192-022-01312-x · 2023 · External reference
Molecular chaperone functions in protein folding and proteostasis
10.1146/annurev-biochem-060208-092442 · 2013 · External reference
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
10.1038/nrm2941 · 2010 · External reference
Guidelines for the nomenclature of the human heat shock proteins
10.1007/s12192-008-0068-7 · 2009 · External reference
The general concept of molecular chaperones
10.1098/rstb.1993.0023 · 1993 · External reference
Pathways of chaperone-mediated protein folding in the cytosol
10.1038/nrm1492 · 2004 · External reference
Disassembly of tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species
10.1074/jbc.ra120.013478 · 2020 · External reference
Molecular dissection of amyloid disaggregation by human Hsp70
10.1038/s41586-020-2904-6 · 2020 · External reference
Complete suppression of HTT fibrilization and disaggregation of HTT fibrils by a trimeric chaperone complex
10.15252/embj.201797212 · 2018 · External reference
Crucial Hsp70 co-chaperone complex unlocks metazoan protein disaggregation
10.1038/nature14884 · 2015 · External reference
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
10.1016/j.cell.2010.11.050 · 2011 · External reference
Molecular chaperones as therapeutic target: hallmark of neurodegenerative disorders
10.1007/s12035-023-03846-2 · 2024 · External reference
Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing
10.1038/nrd.2018.109 · 2018 · External reference
The S/T-rich motif in the DNAJB6 chaperone delays polyglutamine aggregation and the onset of disease in a mouse model
10.1016/j.molcel.2016.03.017 · 2016 · External reference
Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila
10.1093/hmg/9.19.2811 · 2000 · External reference
The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
10.1038/ncb1477 · 2006 · External reference
Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110
10.1038/cddis.2013.351 · 2013 · External reference
Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation
10.1074/jbc.m114.603332 · 2015 · External reference
The Hsp40 cochaperone DNAJC7 regulates polyglutamine aggregation and exhibits context-dependent effects on polyglycine aggregation
10.1016/j.jbc.2026.111292 · 2026 · External reference
Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT
10.1038/s41467-022-32370-5 · 2022 · External reference
Dual role of ribosome-binding domain of NAC as a potent suppressor of protein aggregation and aging-related proteinopathies
10.1016/j.molcel.2019.03.012 · 2019 · External reference
Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
10.1038/ncb1478 · 2006 · External reference
Function, evolution, and structure of J-domain proteins
10.1007/s12192-018-0948-4 · 2019 · External reference
Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins
2023 · External reference
Formation and structure of wild type huntingtin exon-1 fibrils
10.1021/acs.biochem.7b00138 · 2017 · External reference
HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
10.1016/j.cub.2005.04.058 · 2005 · External reference
Suppression of protein aggregation by chaperone modification of high molecular weight complexes
10.1093/brain/aws022 · 2012 · External reference
Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3
10.1371/journal.pone.0019763 · 2011 · External reference
Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease
10.1038/sj.mt.6300163 · 2007 · External reference
Two novel DNAJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington's disease related aggregates
10.1038/s41598-024-71065-3 · 2024 · External reference
ER stress causes widespread protein aggregation and prion formation
10.1083/jcb.201612165 · 2017 · External reference
A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
10.1016/j.molcel.2010.01.001 · 2010 · External reference
The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides
10.1074/jbc.m112.421685 · 2013 · External reference
DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios
10.1007/s12192-013-0448-5 · 2014 · External reference
Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
10.1038/emm.2014.117 · 2015 · External reference
A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy
10.1038/s41556-025-01747-1 · 2025 · External reference
Human Hsp70 disaggregase reverses Parkinson's-linked α-synuclein amyloid fibrils
10.1016/j.molcel.2015.07.012 · 2015 · External reference
The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species
10.15252/embj.2019103954 · 2020 · External reference
Autophagy preferentially degrades non-fibrillar polyQ aggregates
10.1016/j.molcel.2024.04.018 · 2024 · External reference
Differential roles for DNAJ isoforms in HTT-polyQ and FUS aggregation modulation revealed by chaperone screens
10.1038/s41467-022-27982-w · 2022 · External reference
Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
2000 · External reference
Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle
10.1074/jbc.m110.160218 · 2010 · External reference
The ATPase VCP/p97 functions as a disaggregase against toxic huntingtin-exon1 aggregates
10.1002/1873-3468.13213 · 2018 · External reference
Processive extrusion of polypeptide loops by a Hsp100 disaggregase
10.1038/s41586-020-1964-y · 2020 · External reference
The nascent polypeptide-associated complex is a key regulator of proteostasis
10.1038/emboj.2013.87 · 2013 · External reference
The nascent polypeptide-associated complex (NAC) as regulatory hub on ribosomes
10.1515/hsz-2025-0114 · 2025 · External reference
Protein folding: versatility of the cytosolic chaperonin TRiC/CCT
10.1016/s0960-9822(00)00432-2 · 2000 · External reference
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
10.1016/j.tcb.2004.09.015 · 2004 · External reference
The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
10.1038/nsmb.1700 · 2009 · External reference
Hspb7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones
10.1093/hmg/ddq398 · 2010 · External reference
The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation
10.15252/embj.2020107568 · 2021 · External reference
Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity
10.1016/j.cell.2010.07.020 · 2010 · External reference
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation
10.1107/s2052252524006341 · 2024 · External reference
Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity
10.1038/s42003-023-05142-0 · 2023 · External reference
The noncanonical small heat shock protein HSP-17 from Caenorhabditis elegans is a selective protein aggregase
10.1074/jbc.ra119.011185 · 2020 · External reference
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
10.1083/jcb.201106037 · 2011 · External reference
YocM a small heat shock protein can protect Bacillus subtilis cells during salt stress
10.1111/mmi.14164 · 2019 · External reference
Mining disaggregase sequence space to safely counter TDP-43, FUS, and α-synuclein proteotoxicity
10.1016/j.celrep.2019.07.069 · 2019 · External reference
Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events
10.1016/j.cell.2013.11.047 · 2014 · External reference
Tuning Hsp104 specificity to selectively detoxify α-synuclein
10.1016/j.molcel.2023.07.029 · 2023 · External reference
PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
10.1083/jcb.200304111 · 2004 · External reference
Engineering a membrane protein chaperone to ameliorate the proteotoxicity of mutant huntingtin
10.1038/s41467-025-56030-6 · 2025 · External reference
HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species
10.1038/s41467-024-46538-8 · 2024 · External reference
Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease
10.1007/s12017-013-8275-5 · 2014 · External reference
Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
10.1186/1471-2202-6-1 · 2005 · External reference
Neuroprotective effects of phenylbutyrate in the N171-82Q transgenic mouse model of Huntington's disease
10.1074/jbc.m410210200 · 2005 · External reference
Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress
10.1038/s41467-025-58691-9 · 2025 · External reference
Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy
2000 · External reference
Engineered antibody therapies to counteract mutant huntingtin and related toxic intracellular proteins
10.1016/j.pneurobio.2011.11.004 · 2012 · External reference
HSP110 is a modulator of amyloid beta (Aβ) aggregation and proteotoxicity
10.1111/jnc.16214 · 2024 · External reference