Curcumin regulates gene expression via PPARa activation and exhibits biological activities involved in amyloidosis, peroxisome proliferation, lipid metabolism, and hepatocyte hypertrophy.

Identifying the patient-specific mutation that shifted the antibody light chain to the deadly fibrillar species provides new insight in the molecular pathogenesis of AL amyloidosis.

Toxic IAPP intermediates have some molecular features that are similar to, and others that are distinct from, toxic species reported for other amyloidogenic polypeptides.

The causal link between capillary amyloid‑β accumulation in the brain and cerebrovascular dysfunction, previously established in the Tg‑SwDI mouse model, is to be mitigated and remains to be fully uncovered.

Ligands that bind dimers of light chain variable domains inhibit the formation of amyloid fibrils.

Age-dependent protein aggregation closely resembles protein aggregation associated with neurodegenerative diseases and other amyloidoses, and initiates early functional decline in different tissues.

Novel designed alpha-sheet peptides inhibit amyloidosis in two different systems and preferentially bind the toxic oligomer.

SAA removes toxic products of lipolysis of the cell membrane by sPLA₂, indicating that SAA and sPLA₂ act synergistically to clear debris from injured sites, as required for tissue healing.

Small molecule proteostasis regulators that activate the unfolded protein response transcription factor ATF6 reduce the secretion of amyloid disease-associated proteins.

Cell division imposes a limit on proteostasis capacity by reducing chaperone accumulation, but chaperone-substrate interactions reverse these events to allow clearance of even chronically misfolded protein amyloids.