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

There exists a phenomenon in aging research whereby early life stress can have positive
impacts on longevity. The mechanisms underlying these observations suggest a robust, long …

Protein secretion is an essential process for living organisms. In eukaryotes, this
encompasses numerous steps mediated by several hundred cellular proteins. The core …

The endoplasmic reticulum (ER) serves as a warehouse for factors that augment and control
the biogenesis of nascent proteins entering the secretory pathway. In turn, this compartment …

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

It remains unclear how misfolded membrane proteins are selected and destroyed during
endoplasmic reticulum-associated degradation (ERAD). For example, chaperones are …

Squalene monooxygenase (SM) is a vital sterol synthesis enzyme across eukaryotic life. In
yeast, it is a therapeutic target for treating certain fungal infections, and in mammals it is a …

Accumulation of misfolded protein in the endoplasmic reticulum (ER) causes stress. The
unfolded protein response (UPR), a transcriptional induction pathway, is activated to relieve …

Recognition and elimination of misfolded proteins are essential cellular processes. More
than thirty percent of the cellular proteins are proteins of the secretory pathway. They fold in …

Quality control systems facilitate polypeptide folding and degradation to maintain protein
homeostasis. Molecular chaperones promote folding, whereas the ubiquitin/proteasome …