Activation of the p53 protein protects the organism against the propagation of cells that carry
damaged DNA with potentially oncogenic mutations. MDM2, a p53-specific E3 ubiquitin …

The proteasome is an abundant multi-enzyme complex that provides the main pathway for
degradation of intracellular proteins in eukaryotic cells. As such, it controls the levels of …

Controlling Proteolysis process. through Compartmentalization Self-compartmentalizing
proteases are common in all Protein degradation is a necessity for many reasons: three …

Secretion of proteins is initiated by their uptake into the endoplasmic reticulum (ER), which
possesses a proteolytic system able to degrade misfolded and nonassembled proteins. The …

Proteasomes are present in the cytoplasm and in the nuclei of all eukaryotic cells, however
their relative abundance within those compartments is highly variable. In the cytoplasm …

Intermediate filament proteins (IFs) maintain cell and tissue integrity, based on evidence of
their polymerization and mechanical properties, abundance and disease-associated …

Proteasomes can exist in several different molecular forms in mammalian cells. The core
20S proteasome, containing the proteolytic sites, binds regulatory complexes at the ends of …

DNA–protein crosslinks (DPC) involving all major histones are the dominant form of DNA
damage in formaldehyde-exposed cells. In order to understand the repair mechanisms for …

Proteasomes are proteolytic complexes involved in non‐lysosomal degradation which are
localized in both the cytoplasm and the nucleus. The dynamics of proteasomes in living cells …

Proteasomes are high‐molecular‐mass multisubunit complexes which are believed, either
by themselves or as a part of the 26S proteinase complex, to play a central role in …