ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum
(ER) within lysosomes or vacuoles. It is part of the self-digestion (ie, autophagic) programs …

Protein folding is inherently error prone, especially in the endoplasmic reticulum (ER). Even
with an elaborate network of molecular chaperones and protein folding facilitators …

Advances over the past 25 years have revealed much about how the structural properties of
membranes and associated proteins are linked to the thermodynamics and kinetics of …

One evident hallmark of Alzheimer's disease (AD) is the irregular accumulation of proteins
due to changes in proteostasis involving endoplasmic reticulum (ER) stress. To alleviate ER …

About 40% of the eukaryotic cell's proteins are inserted co-or post-translationally in the
endoplasmic reticulum (ER), where they attain the native structure under the assistance of …

Misfolded proteins compromise cellular homeostasis. This is especially problematic in the
endoplasmic reticulum (ER), which is a high-capacity protein-folding compartment and …

Endoplasmic reticulum (ER) proteostasis is maintained by various catabolic pathways.
Lysosomes clear entire ER portions by ER‐phagy, while proteasomes selectively clear …

Recent evidence demonstrates that novel protein-coding genes can arise de novo from non-
genic loci. This evolutionary innovation is thought to be facilitated by the pervasive …

The unfolded protein response (UPR) is a highly conserved molecular machinery, which
protects the cells against a diverse variety of stimuli. Activation of this element has been …

Background The protein homeostasis (proteostasis) network maintains balanced protein
synthesis, folding, transport, and degradation within a cell. Failure to maintain proteostasis is …