Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

Amyloid-like Fibrils from an Îą-Helical Transmembrane Protein.

Ultrasensitive Measurement of Ca(2+) Influx into Lipid Vesicles Induced by Protein Aggregates.

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.

Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.

Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.

The Amyloid Phenomenon and Its Links with Human Disease.

Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants.

Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.

Corrigendum: Structural basis of synaptic vesicle assembly promoted by Îą-synuclein.

Inhibition of Îą-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between Îą-Synuclein Species.

Widespread Proteome Remodeling and Aggregation in Aging C. elegans.

A natural product inhibits the initiation of Îą-synuclein aggregation and suppresses its toxicity.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.