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The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain

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The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain

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N-terminal mutant huntingtin deposition correlates with CAG repeat length and symptom onset, but not neuronal loss in Huntington's disease

A New Chemoenzymatic Semisynthetic Approach Provides Insight into the Role of Phosphorylation beyond Exon1 of Huntingtin and Reveals N-Terminal Fragment Length-Dependent Distinct Mechanisms of Aggregation

New Methods for the Integrative Dynamic Modeling of Biomolecular Structures

Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13

Reconstruction Methods for Cryo-Electron Microscopy: From Model-based to Data-driven

Multicolor single-particle reconstruction of protein complexes

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths

Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models