Martin L. Duennwald

A network of protein interactions determines polyglutamine toxicity.

Flanking sequences profoundly alter polyglutamine toxicity in yeast.

Chaperone-dependent amyloid assembly protects cells from prion toxicity.

Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs.

Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity.

A synergistic small-molecule combination directly eradicates diverse prion strain structures.

Countering amyloid polymorphism and drug resistance with minimal drug cocktails.

Monitoring polyglutamine toxicity in yeast.

Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes.

Polyglutamine misfolding in yeast: Toxic and protective aggregation.

Yeast as a platform to explore polyglutamine toxicity and aggregation.

A Toolbox for Rapid Quantitative Assessment of Chronological Lifespan and Survival in Saccharomyces cerevisiae.

Saccharomyces cerevisiae Tti2 Regulates PIKK Proteins and Stress Response.

CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins.

Polyglutamine toxicity in yeast uncovers phenotypic variations between different fluorescent protein fusions.

Candida albicans Is Resistant to Polyglutamine Aggregation and Toxicity.

Cellular stress responses in protein misfolding diseases.

Visualizing tRNA-dependent mistranslation in human cells.

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.