Oligomeric assemblies formed from a variety of disease-associated peptides and proteins
have been strongly associated with toxicity in many neurodegenerative conditions, such as …

Multiple human diseases are associated with a liquid-to-solid phase transition resulting in
the formation of amyloid fibers or protein aggregates. Here, we present an alternative …

In recent genome-wide association studies, the extracellular chaperone protein, clusterin,
has been identified as a newly-discovered risk factor in Alzheimer's disease. We have …

… b Correlation of toxicity estimates between replicates 1 and 2 for single and double amino
acid (AA) mutants shown separately for each library (290–332; 332–373). The Pearson …

The conversion of α-synuclein from its intrinsically disordered monomeric state into the
fibrillar cross-β aggregates characteristically present in Lewy bodies is largely unknown. The …

How many copies of a protein can be made before it becomes toxic to the cell?

Amyloidosis associated to hemodialysis is caused by persistently high β 2 -microglobulin (β
2 m) serum levels. β 2 m is an intrinsically amyloidogenic protein whose capacity to …

Recent evidence indicates that specific RNAs promote the formation of ribonucleoprotein
condensates by acting as scaffolds for RNA-binding proteins (RBPs). We systematically …

Increasing evidence indicates that RNA plays an active role in a number of neurodegenerative
diseases. We recently introduced a theoretical framework, catRAPID, to predict the …

… (B) Correlation of nucleation scores for biological replicates 1 and 2 for single and double
amino acid (aa) mutants. Pearson correlation coefficient and p-value are indicated (Figure 1—…