The disease-associated aggregation of polyglutamine begins in a single molecule with a specific structure.

Structural and biochemical analysis of full-length huntingtin protein illuminates the impact of the polyglutamine region on its structure and function.

Pathogenesis in Spinocerebellar Ataxia Type 3 is enhanced by the heat-shock protein family member, Hsc70-4, uncovering new mechanisms of toxicity for this disease and suggesting pleiotropic roles for chaperones.

Nemo-like kinase is a key protein promoting the pathogenesis of spinal and bulbar muscular atrophy.

Amino acid limitation triggers preferential uncharging of glutamine-specific tRNAs and depletes polyglutamine tract-containing proteins from mammalian cells, revealing a potential role for polyglutamine tracts as sensors of glutamine sufficiency.

A combination of single-cell analysis, genomics, and simulations shows that a glutamine-rich low-complexity sequence in the SWI/SNF chromatin remodeling complex senses transient intracellular acidification as a signal for cells to switch their global transcriptional program.

Polyglutamine expansion in mutant huntingtin disrupts a novel transcription-coupled DNA repair complex, providing an undescribed mechanism of neuronal toxicity and degeneration in Huntington's disease.

Noncanonical usage of stop codons in ciliates expands structurally flexible Q-rich domains and coevolves with codon usage biases to avoid triplet repeat disorders mediated by CAG/GTC replication slippage.

A genome-wide screen in yeast reveals that key proteins in ribosome quality control also regulate mutant Huntingtin aggregation and toxicity.

Cryo-electron tomography reveals how a chaperone protein called TRiC reduces the ability of pathogenic mutant huntingtin proteins to form aggregates.