Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates. - Wikidata - wikimedia - TriplyDB

Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.

Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.

http://www.wikidata.org/entity/Q39426587

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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion Huntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Inhibition of Huntingtin Exon-1 Aggregation by the Molecular Tweezer CLR01.Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Structural features and domain organization of huntingtin fibrils.CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.Studying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtin Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism.Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding.Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.Experimental models for identifying modifiers of polyglutamine-induced aggregation and neurodegeneration.A serendipitous survey of prediction algorithms for amyloidogenicity.Advances in huntington disease drug discovery: novel approaches to model disease phenotypes.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Discovery of Therapeutic Approaches for Polyglutamine Diseases: A Summary of Recent Efforts.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Assessing a peptidylic inhibitor-based therapeutic approach that simultaneously suppresses polyglutamine RNA- and protein-mediated toxicities in patient cells and Drosophila.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.Aggregation behavior of chemically synthesized, full-length huntingtin exon1.Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.A brain-targeting lipidated peptide for neutralizing RNA-mediated toxicity in Polyglutamine Diseases.Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation.Biodegradable delivery system containing a peptide inhibitor of polyglutamine aggregation: a step toward therapeutic development in Huntington's disease.Sedimentation Velocity Analysis with Fluorescence Detection of Mutant Huntingtin Exon 1 Aggregation in Drosophila melanogaster and Caenorhabditis elegans.Assembly of Huntingtin headpiece into α-helical bundles.Selection pressure on human STR loci and its relevance in repeat expansion disease.Mechanical properties of amyloid-like fibrils defined by secondary structures.

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Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.

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Ashwani K Thakur

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Bartholomew P Roland

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Elizabeth Landrum

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Irene Arduini

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Murali Jayaraman

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Rakesh Mishra

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Ravindra Kodali

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Ronald Wetzel

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Timothy Fullam

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SUMO modification of Huntingtin and Huntington's disease pathology

Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity

The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation

The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor

Huntingtin aggregation and toxicity in Huntington's disease

Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

Analysis of molecular recognition features (MoRFs)

Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Time course of early motor and neuropathological anomalies in a knock-in mouse model of Huntington's disease with 140 CAG repeats

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