Intracellular deposition of aggregated and ubiquitylated proteins is a prominent
cytopathological feature of most neurodegenerative disorders. Whether protein aggregates …

▪ Abstract In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the
ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built …

The precise assembly and engineering of molecular machines capable of handling
biomolecules play crucial roles in most single-molecule methods. In this work we use …

The 26S proteasome is a 2.4 MDa multifunctional ATP-dependent proteolytic complex,
which degrades the majority of cellular polypeptides by an unusual enzyme mechanism …

Protein degradation is a necessity for many reasons: Homeostasis must be maintained while
cellular structures are continually rebuilt, in particular during development or in response to …

All intracellular proteins and many extracellular proteins are continually “turning over”; ie,
they are being hydrolyzed to their constituent amino acids and replaced by new synthesis …

▪ Abstract Major histocompatibility complex (MHC) class I molecules display on the cell
surface 8-to 10-residue peptides derived from the spectrum of proteins expressed in the …

Knowledge about the sizes of peptides generated by proteasomes during protein
degradation is essential to fully understand their degradative mechanisms and the …

Rising interest in the mechanism and function of the proteasomes and the ubiquitin system
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …

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 …