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 …

Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Protein aggregation is a hallmark of multiple human pathologies. Autophagy selectively
degrades protein aggregates via aggrephagy. How selectivity is achieved has been elusive …

Stress granules are mRNA-protein granules that form when translation initiation is limited,
and they are related to pathological granules in various neurodegenerative diseases. Super …

Chaperones are central to the proteostasis network (PN) and safeguard the proteome from
misfolding, aggregation, and proteotoxicity. We categorized the human chaperome of 332 …

Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

The protein components of eukaryotic cells face acute and chronic challenges to their
integrity. Eukaryotic protein homeostasis, or proteostasis, enables healthy cell and …

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 …

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 …