A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.

An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation.

Lymph-Node Palpation--No Laughing Matter.

Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.

Alpha-Synuclein Oligomers Interact with Metal Ions to Induce Oxidative Stress and Neuronal Death in Parkinson's Disease.

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.

Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.

Molecular mechanisms of protein aggregation from global fitting of kinetic models.

Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the Îą-synuclein-elicited immune response.

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.

Hamiltonian Dynamics of Protein Filament Formation.

Solvent exposure of Tyr10 as a probe of structural differences between monomeric and aggregated forms of the amyloid-β peptide.

Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins.

Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants.

SOD1 protein aggregates stimulate macropinocytosis in neurons to facilitate their propagation.