Eberhard Scherzinger

TL;DR: In this paper, the authors observed that mice transgenic for exon 1 of the human HD gene carrying (CAG)115 to 157 repeat expansions develop pronounced neuronal intranuclear inclusions, containing the proteins huntingtin and ubiquitin, prior to developing a neurological phenotype.

TL;DR: In this study, it is shown that the proteolytic cleavage of a GST-huntingtin fusion protein leads to the formation of insoluble high molecular weight protein aggregates only when the polyglutamine expansion is in the pathogenic range.

TL;DR: It is reported that the formation of amyloid-like huntingtin aggregates in vitro not only depends on poly(Q) repeat length but also critically depends on protein concentration and time, and the in vitro aggregation of huntingtin can be seeded by preformed fibrils.

TL;DR: In 293 Tet-Off cells, inclusion body formation resulted in cell toxicity and dramatic ultrastructural changes such as indentations and disruption of the nuclear envelope, which support the hypothesis that the ATP-dependent ubiquitin-proteasome system is a potential target for therapeutic interventions in glutamine repeat disorders.

TL;DR: This article showed that the formation of amyloid-like peptides in vitro not only depends on poly(Q) repeat length but also critically depends on protein concen- tration and time.