Ageing is a major risk factor for the development of many diseases, prominently including
neurodegenerative disorders such as Alzheimer disease and Parkinson disease. A hallmark …

The manner in which a newly synthesized chain of amino acids transforms itself into a
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …

Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

Intracellular deposition of aggregated and ubiquitylated proteins is a prominent
cytopathological feature of most neurodegenerative disorders. Whether protein aggregates …

The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic
feature of more than 20 degenerative conditions affecting either the central nervous system …

The accumulation of β-sheet–rich amyloid fibrils or aggregates is a complex, multistep
process that is associated with cellular toxicity in a number of human protein misfolding …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the
assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein …

This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …

Stress granules (SGs) are membraneless cell compartments formed in response to different
stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other …