The 26S proteasome represents a major, energy-dependent and self-compartmentalizing protease system in eukaryotes. The proteolytic core of this complex, the 20S proteasome, is also ubiquitous in archaea. Although absent from most eubacteria, this multi-subunit protease was recently discovered in Rhodococcus and appears to be confined to actinomycetes. The eubacterial 20S proteasome represents an attractive complementary system to study proteasome assembly, quaternary structure, and catalytic mechanism. In addition, it is likely to contribute substantially to our understanding of the role of various self-compartmentalizing proteases in bacterial cells. [References: 27
Frankia is an actinomycete that fixes atmospheric nitrogen in symbiotic association with the root sy...
The proteasome is a macromolecular assembly that is designed to confine proteolytic activity to an i...
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domai...
The 26S proteasome represents a major, energy-dependent and self-compartmentalizing protease system ...
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome o...
Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein...
The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It confines prot...
AbstractBackground: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of...
AbstractProteasomes reach their mature active state via a complex cascade of folding, assembly and p...
The 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis strain NI86...
AbstractThe 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis str...
Proteasomes reach their mature active state via a complex cascade of folding, assembly and processin...
Doctor of PhilosophyDepartment of BiologyJeroen RoelofsProteasomes are large, multimeric proteases t...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
International audienceFrankia is an actinomycete that fixes atmospheric nitrogen in symbiotic associ...
Frankia is an actinomycete that fixes atmospheric nitrogen in symbiotic association with the root sy...
The proteasome is a macromolecular assembly that is designed to confine proteolytic activity to an i...
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domai...
The 26S proteasome represents a major, energy-dependent and self-compartmentalizing protease system ...
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome o...
Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein...
The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It confines prot...
AbstractBackground: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of...
AbstractProteasomes reach their mature active state via a complex cascade of folding, assembly and p...
The 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis strain NI86...
AbstractThe 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis str...
Proteasomes reach their mature active state via a complex cascade of folding, assembly and processin...
Doctor of PhilosophyDepartment of BiologyJeroen RoelofsProteasomes are large, multimeric proteases t...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
International audienceFrankia is an actinomycete that fixes atmospheric nitrogen in symbiotic associ...
Frankia is an actinomycete that fixes atmospheric nitrogen in symbiotic association with the root sy...
The proteasome is a macromolecular assembly that is designed to confine proteolytic activity to an i...
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domai...