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Caitlin I.J. Peeters, Menno Spits, Eric A.J. Reits, Sabine Schipper-Krom
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10.1016/s1474-4422(10)70245-3
10.1016/s1474-4422(10)70245-3
10.1038/s41582-020-0389-4
10.1038/s41582-020-0389-4
10.1016/j.prdoa.2020.100056
10.1016/j.prdoa.2020.100056
The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington’s disease
10.1038/ng0893-398 · 1993
10.3390/ijms25073845
10.3390/ijms25073845
Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington’s disease
10.1093/hmg/ddu504 · 2014
Lowering the HTT1a transcript as an effective therapy for Huntington’s disease in a knockin mouse model
10.1126/scitranslmed.adw2495 · 2026
Long somatic DNA-repeat expansion drives neurodegeneration in Huntington’s disease
10.1016/j.cell.2024.11.038 · 2025
10.1038/s41467-018-06281-3
10.1038/s41467-018-06281-3
10.1073/pnas.1221891110
10.1073/pnas.1221891110
10.1006/nbdi.1998.0168
10.1006/nbdi.1998.0168
Aggregation of truncated GST-HD exon 1 fusion proteins containing normal range and expanded glutamine repeats
10.1098/rstb.1999.0450 · 1999
10.1016/j.molcel.2016.07.022
10.1016/j.molcel.2016.07.022
10.1016/j.jmb.2011.12.010
10.1016/j.jmb.2011.12.010
Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer
10.1371/journal.pone.0155747 · 2016
Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR
10.1073/pnas.1821216116 · 2019
Quantitative NMR analysis of the kinetics of prenucleation oligomerization and aggregation of pathogenic huntingtin exon-1 protein
10.1073/pnas.2207690119 · 2022
A Targetable Self-association Surface of the Huntingtin exon1 Helical Tetramer Required for Assembly of Amyloid Pre-nucleation Oligomers
10.1016/j.jmb.2024.168607 · 2024
Mutant Huntingtin Fragments Form Oligomers in a Polyglutamine Length-dependent Manner in Vitro and in Vivo
10.1074/jbc.m109.093708 · 2010
Membrane Interactions Accelerate the Self-Aggregation of Huntingtin Exon 1 Fragments in a Polyglutamine Length-Dependent Manner
10.3390/ijms22136725 · 2021
10.1016/j.tibs.2025.08.005
10.1016/j.tibs.2025.08.005
10.1016/j.jmb.2005.10.053
10.1016/j.jmb.2005.10.053
10.1016/j.jmb.2007.09.023
10.1016/j.jmb.2007.09.023
10.1038/nsmb.1570
10.1038/nsmb.1570
Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation
10.1073/pnas.1320626110 · 2013
10.1038/s41594-023-00920-0
10.1038/s41594-023-00920-0
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre-Formed, Sparsely-Populated Tetramers
10.1002/advs.202309217 · 2024
10.1016/j.jmb.2018.03.017
10.1016/j.jmb.2018.03.017
Super-Resolution Fluorescence of Huntingtin Reveals Growth of Globular Species into Short Fibers and Coexistence of Distinct Aggregates
10.1021/cb500335w · 2014
Detection of Mutant Huntingtin Aggregation Conformers and Modulation of SDS-Soluble Fibrillar Oligomers by Small Molecules
10.3233/jhd-2012-129004 · 2012
Direct Observation of Secondary Nucleation in Huntingtin Amyloid Formation by High-Speed Atomic Force Microscopy
10.1021/jacs.5c05571 · 2025
Integrative determination of atomic structure of mutant huntingtin exon 1 fibrils implicated in Huntington disease
10.1038/s41467-024-55062-8 · 2024
Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
10.1038/s41467-021-24411-2 · 2021
10.1021/bi501010q
10.1021/bi501010q
10.1016/j.jmb.2020.06.021
10.1016/j.jmb.2020.06.021
In Situ Architecture and Cellular Interactions of PolyQ Inclusions
10.1016/j.cell.2017.08.009 · 2017
Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates
10.1038/s42003-021-02360-2 · 2021
Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies
10.1016/j.febslet.2013.11.023 · 2014
10.1016/j.expneurol.2011.12.013
10.1016/j.expneurol.2011.12.013
10.1038/nature02998
10.1038/nature02998
Epitope-specific antibodies can distinguish between soluble huntingtin exon-1 and its diverse cellular aggregates
10.1016/j.jbc.2025.111048 · doi-reference
Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment
10.1074/jbc.m109.016923 · doi-reference
10.1371/journal.pone.0005727
10.1371/journal.pone.0005727 · doi-reference
A human single-chain Fv intrabody preferentially targets amino-terminal Huntingtin’s fragments in striatal models of Huntington’s disease
10.1016/j.nbd.2004.11.003 · doi-reference
Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington’s disease
10.1186/s40478-021-01172-z · doi-reference
10.1038/s41467-023-36096-w
10.1038/s41467-023-36096-w · doi-reference
Cellular Inclusion Bodies of Mutant Huntingtin Exon 1 Obscure Small Fibrillar Aggregate Species
10.1038/srep00895 · doi-reference
Detecting protein aggregation and interaction in live cells: A guide to number and brightness
10.1016/j.ymeth.2017.12.001 · doi-reference
A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis
10.1016/j.bpj.2010.02.058 · doi-reference
Mapping the number of molecules and brightness in the laser scanning microscope
10.1529/biophysj.107.114645 · doi-reference
Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo
10.1007/978-1-4939-2978-8_5 · doi-reference
10.1074/jbc.m704789200
10.1074/jbc.m704789200 · doi-reference
FLIM-FRET Investigation of Heterogeneous Huntingtin Aggregation in HeLa Cells
10.1007/978-1-0716-2597-2_36 · doi-reference
Visualization of cell-to-cell transmission of mutant huntingtin oligomers
10.1371/currents.rrn1210 · doi-reference
10.1016/s0896-6273(03)00697-4
10.1016/s0896-6273(03)00697-4 · doi-reference
Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies
10.1038/s41598-018-19538-0 · doi-reference
10.1093/hmg/ddt625
10.1093/hmg/ddt625 · doi-reference
Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging
10.1038/s41467-025-60912-0 · doi-reference
High throughput quantification of mutant huntingtin aggregates
10.1016/j.jneumeth.2008.02.007 · doi-reference
Mutant huntingtin expression in clonal striatal cells: dissociation of inclusion formation and neuronal survival by caspase inhibition
10.1523/jneurosci.19-03-00964.1999 · doi-reference
10.1016/s0092-8674(00)81782-1
10.1016/s0092-8674(00)81782-1 · doi-reference
10.1074/jbc.ra118.004621
10.1074/jbc.ra118.004621 · doi-reference
Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity
10.1074/jbc.m513507200 · doi-reference
10.3233/jhd-200465
10.3233/jhd-200465 · doi-reference
10.3389/fchem.2020.00485
10.3389/fchem.2020.00485 · doi-reference
Interaction of huntingtin with PRMTs and its subsequent arginine methylation affects HTT solubility, phase transition behavior and neuronal toxicity
10.1093/hmg/ddab351 · doi-reference
Global Proteome and Ubiquitinome Changes in the Soluble and Insoluble Fractions of Q175 Huntington Mice Brains
10.1074/mcp.ra119.001486 · doi-reference
10.1016/j.bpc.2025.107473
10.1016/j.bpc.2025.107473 · doi-reference
10.1371/journal.pone.0298323
10.1371/journal.pone.0298323 · doi-reference
Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress
10.1038/s41467-025-58691-9 · doi-reference
10.1016/j.bbapap.2010.04.001
10.1016/j.bbapap.2010.04.001 · doi-reference
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
10.1016/0003-2697(89)90046-8 · doi-reference
10.1111/febs.16312
10.1111/febs.16312 · doi-reference
Recent advances in fluorescent probes development for interrogating protein misfolding and aggregation
10.1016/j.trac.2024.118066 · doi-reference
A method for the analysis of the oligomerization profile of the Huntington’s disease-associated, aggregation-prone mutant huntingtin protein by isopycnic ultracentrifugation
10.3389/fmolb.2024.1420691 · doi-reference
Site-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects
10.1073/pnas.2007667117 · doi-reference
Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging
10.1371/journal.pone.0044457 · doi-reference
10.1074/jbc.m111.252577
10.1074/jbc.m111.252577 · doi-reference
Sensitive biochemical aggregate detection reveals aggregation onset before symptom development in cellular and murine models of Huntington’s disease
10.1111/j.1471-4159.2007.05032.x · doi-reference
Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
10.3791/838 · doi-reference