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The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

Amyloid-β oligomers associated with Alzheimer’s disease interact with dynein motors to impair retrograde transport of autophagic vesicles in neurons.

Oligomeric Amyloid-β and Tau, two proteins involved in Alzheimer's disease pathogenesis, require Amyloid Precursor Protein to enter neurons and exert their detrimental effect on synaptic plasticity and memory.

A rationally designed small molecule ATP-mimetic activates IRE1 and PERK signaling in cells by inducing conformational changes that template the assembly of higher-order enzymatically active structures.

The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.

Solution NMR provides structural and kinetic information about oligomers on pathway to amyloid fibrils that are precisely structured but not cytotoxic.

Aβ inhibitors effectively block its aggregation, while also reducing seeding of tau aggregation from Aβ, tau, and AD derived fibrils, suggesting the two share a structurally related disease relevant interface.

The high affinity α-synuclein-monomer binder AS69 converts into a strong sub-stoichiometric inhibitor of nucleation processes upon formation of the AS69-α-synuclein complex, achieving reduced aggregation in vitro and in vivo.

The McsB kinase is critical for protein quality control in Gram-positive bacteria, assembling a gated phosphorylation chamber during heat-shock conditions to selectively mark misfolded proteins for degradation.

Genetic analysis of a CLN4 Drosophila model suggests that the disease-causing alleles act as dominant gain of function mutations that cause CSPα oligomerization and impair secretory and prelysosomal trafficking.