The proteasome is an intricate molecular machine, which serves to degrade proteins
following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19 …

Abstract The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led
to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic …

Protein modifications provide cells with exquisite temporal and spatial control of protein
function. Ubiquitin is among the most important modifiers, serving both to target hundreds of …

The 20S proteasome functions in protein degradation in eukaryotes together with the 19S
ATPases or in archaea with the homologous PAN ATPase complex. These ATPases contain …

The 26S proteasome is the most complex ATP-dependent protease machinery, of~ 2.5 MDa
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …

The implication of reduced proteasomal function in neurodegenerative diseases combined
with studies showing the protective effects of increasing proteasome activity in animal …

Substrates enter the cylindrical 20S proteasome through a gated channel that is regulated
by the ATPases in the 19S regulatory particle in eukaryotes or the homologous PAN ATPase …

Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and
thereby are essential for many aspects of cellular function. Because the proteolytic sites are …

The proteasome refers to a collection of complexes centered on the 20S proteasome core
particle (20S CP), a complex of 28 subunits that houses proteolytic sites in its hollow interior …

Large macromolecular assemblies, so-called molecular machines, are critical to ensuring
proper cellular function. Understanding how proper function is achieved at the atomic level …