The selective degradation of many short-lived proteins in eukaryotic cells is carried out by
the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent …

The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic
proteome and is accordingly endowed with specialized machinery to ensure that proteins …

A growing amount of evidence suggests that ubiquitination and deubiquitination of
programmed death 1 (PD-1)/programmed death-ligand 1 (PD-L1) play crucial roles in the …

3-hydroxy-3-methylglutaryl-CoA reductase (HMG-R), a key enzyme of sterol synthesis, is an
integral membrane protein of the endoplasmic reticulum (ER). In both humans and yeast …

HMG-CoA reductase (HMGR), a highly conserved, membrane-bound enzyme, catalyzes a
rate-limiting step in sterol and isoprenoid biosynthesis and is the primary target of …

▪ Abstract The modification of proteins by chains of ubiquitin has long been known to
mediate targeting of cytosolic and nuclear proteins for degradation by proteasomes. In this …

The ER-associated degradation (ERAD) pathway directs ubiquitin-mediated degradation of
a variety of ER-associated misfolded and normal proteins. Recent studies have delineated …

Studies on sterol biosynthesis in the yeast, Saccharomyces cerevisiae, and in strains
auxotrophic for the fungal sterol, ergosterol, suggest that sterol plays significant …

In eukaryotes, endoplasmic reticulum-associated degradation (ERAD) functions in cellular
quality control and regulation of normal ER-resident proteins. ERAD proceeds by the …

Carotenoids occur universally in photosynthetic organisms but sporadically in
nonphotosynthetic bacteria and eukaryotes. The primordial carotenogenic organisms were …