Our understanding of the ubiquitin code has greatly evolved from conventional E1, E2 and
E3 enzymes that modify Lys residues on specific substrates with a single type of ubiquitin …

Maintaining proteome integrity is essential for long-term viability of all organisms and is
overseen by intrinsic quality control mechanisms. The secretory pathway of eukaryotes …

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

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

Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are two diseases
that form a broad neurodegenerative continuum. Considerable effort has been made to …

The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is
usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have …

Amyloid-like aggregates of the microtubule-associated protein Tau are associated with
several neurodegenerative disorders including Alzheimer's disease. The existence of …

The 26S proteasome is involved in degrading and regulating the majority of proteins in
eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity. In this …

ATPases associated with diverse cellular activities (AAA+ proteins) are macromolecular
machines that convert the chemical energy contained in ATP molecules into powerful …

The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER
protein homeostasis is essential for the coordination of its diverse functions and depends on …