Oxidation Promotes Distinct Huntingtin Aggregates in the Presence and Absence of Membranes.

Expansion of a polyglutamine (polyQ) domain within the first exon of the huntingtin (htt) protein is the underlying cause of Huntington's disease, a genetic neurodegenerative disorder. PolyQ expansion triggers htt aggregation into oligomers, fibrils, and inclusions. The 17 N-terminal amino acids (Nt17) of htt-exon1, which directly precede the polyQ domain enhances polyQ fibrillization and functions as a lipid-binding domain.

Many Moving Pieces: Virtual Preoperative Surgical Planning for Traumatic Occlusal Splints.

Introduction: Achieving anatomic reduction and re-establishing premorbid occlusion in patients with complex maxillomandibular fractures is challenging even for seasoned surgeons. Historically, surgeons have utilized occlusal splints to help establish occlusal relationships before fracture reduction and fixation. These acrylic splints are fabricated from dental impressions and require manual repositioning of tooth bearing segments along the fracture line to reapproximate premorbid occlusion.

Macromolecular crowding in solution alters huntingtin interaction and aggregation at interfaces.

Huntington's disease (HD) is a fatal neurodegenerative disease caused by an extended polyglutamine (polyQ) domain within the first exon of the huntingtin protein (htt). PolyQ expansion directly invokes the formation of a heterogenous mixture of toxic htt aggregates, including fibrils and oligomers. While htt is a cytosolic protein, it also associates with numerous membranous surfaces within the cell, leading to altered organelle morphology and dysfunction.