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
In eukaryotic cells, the vast majority of proteins in the cytosol and nucleus are degraded via the p...
In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteas...
International audienceAll living organisms require protein degradation to terminate biological proce...
The 26S proteasome represents a major, energy-dependent and self-compartmentalizing protease system ...
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...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It confines prot...
In eukaryotes protein degradation is performed by the ubiquitin-proteasome system. The 26S proteasom...
In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteas...
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domai...
Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein...
Significant progress has been made over the past few years in elucidating the structural principles ...
In eukaryotic cells, the vast majority of proteins in the cytosol and nucleus are degraded via the p...
In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteas...
International audienceAll living organisms require protein degradation to terminate biological proce...
The 26S proteasome represents a major, energy-dependent and self-compartmentalizing protease system ...
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...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It confines prot...
In eukaryotes protein degradation is performed by the ubiquitin-proteasome system. The 26S proteasom...
In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteas...
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic...
The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein degradation...
Proteasomes are the major energy-dependent proteolytic machines in the eukaryotic and archaeal domai...
Background: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of protein...
Significant progress has been made over the past few years in elucidating the structural principles ...
In eukaryotic cells, the vast majority of proteins in the cytosol and nucleus are degraded via the p...
In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteas...
International audienceAll living organisms require protein degradation to terminate biological proce...