The proteasome, a large multi-subunit protease that degrades proteins, must be able to distinguish between substrates deemed for destruction and accessory proteins that should be spared. The shuttle factor Rad23 operates in close proximity to the proteasome in order to deliver proteins for their degradation. While its cargo is efficiently degraded, the shuttle factor itself remains unharmed. Rad23 is protected by its C-terminal ubiquitin-associated (UBA)-2 domain that has been identified to be a cisacting stabilization signal. A major aim of the work presented in this dissertation has been to decipher the mode of action responsible for this protective effect. Another protein that is targeted to the proteasome but resists degradation was st...
The ubiquitin proteasome pathway (UPP) is the primary proteolytic system for the spatial and tempora...
SummaryIt has been suggested that degradation of polyubiquitylated proteins is coupled to dissociati...
AbstractIt is shown that proteasomes from the archaebacterium Thermoplasma acidophilum selectively d...
AbstractMost proteasome substrates are marked for degradation by ubiquitin conjugation, but some are...
AbstractIn the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent ...
SummaryUbiquitin chains serve as a recognition motif for the proteasome, a multisubunit protease, wh...
Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step i...
The ubiquitin–proteasome system is responsible for the bulk of protein degradation in eukaryotic cel...
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates....
AbstractThe ubiquitin proteasome system is responsible for the controlled degradation of a vast numb...
The proteasome is the main intracellular proteolytic machinery. It is involved in all major cellular...
The ubiquitin receptors Rad23 and Dsk2 deliver polyubiquitylated substrates to the proteasome for de...
The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated ...
Substrates are targeted for proteasomal degradation through the attachment of ubiquitin chains that ...
SummaryThe ubiquitin ligase Hul5 was recently identified as a component of the proteasome, a multisu...
The ubiquitin proteasome pathway (UPP) is the primary proteolytic system for the spatial and tempora...
SummaryIt has been suggested that degradation of polyubiquitylated proteins is coupled to dissociati...
AbstractIt is shown that proteasomes from the archaebacterium Thermoplasma acidophilum selectively d...
AbstractMost proteasome substrates are marked for degradation by ubiquitin conjugation, but some are...
AbstractIn the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent ...
SummaryUbiquitin chains serve as a recognition motif for the proteasome, a multisubunit protease, wh...
Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step i...
The ubiquitin–proteasome system is responsible for the bulk of protein degradation in eukaryotic cel...
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates....
AbstractThe ubiquitin proteasome system is responsible for the controlled degradation of a vast numb...
The proteasome is the main intracellular proteolytic machinery. It is involved in all major cellular...
The ubiquitin receptors Rad23 and Dsk2 deliver polyubiquitylated substrates to the proteasome for de...
The 26S proteasome is responsible for the selective, ATP-dependent degradation of polyubiquitinated ...
Substrates are targeted for proteasomal degradation through the attachment of ubiquitin chains that ...
SummaryThe ubiquitin ligase Hul5 was recently identified as a component of the proteasome, a multisu...
The ubiquitin proteasome pathway (UPP) is the primary proteolytic system for the spatial and tempora...
SummaryIt has been suggested that degradation of polyubiquitylated proteins is coupled to dissociati...
AbstractIt is shown that proteasomes from the archaebacterium Thermoplasma acidophilum selectively d...