Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

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

Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC)
mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the …

Some nascent proteins that fold within the endoplasmic reticulum (ER) never reach their
native state. Misfolded proteins are removed from the folding machinery, dislocated from the …

Mistakes are part of our world and constantly occurring. Due to transcriptional and
translational failures, genomic mutations or diverse stress conditions like oxidation or heat …

Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated
in the endoplasmic reticulum. These adducts have many biological functions, including …

Eukaryotic cells must contend with a continuous stream of misfolded proteins that
compromise the cellular protein homeostasis balance and jeopardize cell viability. An …

The eukaryotic endoplasmic reticulum (ER) maintains protein homeostasis by eliminating
unwanted proteins through the evolutionarily conserved ER-associated degradation (ERAD) …

Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

Eukaryotic protein degradation by the proteasome and the lysosome is a dynamic and
complex process in which ubiquitin has a key regulatory role. The distinctive morphology of …