Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic
reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated …

Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein
response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for …

The N‐end rule relates the regulation of the in vivo half‐life of a protein to the identity of its N‐
terminal residue. Degradation signals (degrons) that are targeted by the N‐end rule pathway …

Ferroptosis is a unique form of cell death caused by excessive iron-dependent lipid
peroxidation. The level of the anabolic reductant NADPH is a biomarker of ferroptosis …

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 …

Newly synthesized transmembrane proteins undergo a series of steps to ensure that only
the required amount of correctly folded protein is localized to the membrane. The regulation …

The retained N-terminal methionine (Met) residue of a nascent protein is often N-terminally
acetylated (Nt-acetylated). Removal of N-terminal Met by Met-aminopeptidases frequently …

The iodothyronine deiodinases initiate or terminate thyroid hormone action and therefore
are critical for the biological effects mediated by thyroid hormone. Over the years, research …

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 …

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 …