AbstractThe two genes encoding the constituent subunits of the Thermoplasma acidophilum proteasome were expressed in Escherichia coli yielding fully assembled molecules as shown by electron microscopy. The recombinant proteasomes were purified to homogeneity and ware shown to have proteolytic activity indistinguishable from proteasomes isolated from T. acidophilum
We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophil...
AbstractThe final destination of the majority of proteins that have to be selectively degraded in eu...
Proteasome assembly is a rapid and highly sequential process that occurs through a series of interme...
The two genes encoding the constituent subunits of the Thermoplasma acidophilum proteasome were expr...
In this study we describe, the construction of a co-expression vector allowing simultaneous producti...
AbstractThe 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis str...
Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assemb...
AbstractBackground: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of...
AbstractThe 20 S proteasome, found in eukaryotes and in the archaebacterium Thermoplasma acidophilum...
The proteasome or multicatalytic proteinase is a high molecular mass multisubunit complex ubiquitous...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
AbstractThe proteasome is not simply a “garbage disposal unit” but also has functions in the control...
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 26S proteasome contains a proteolytic core, 20S proteasome, and its regulatory particle,...
We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophil...
AbstractThe final destination of the majority of proteins that have to be selectively degraded in eu...
Proteasome assembly is a rapid and highly sequential process that occurs through a series of interme...
The two genes encoding the constituent subunits of the Thermoplasma acidophilum proteasome were expr...
In this study we describe, the construction of a co-expression vector allowing simultaneous producti...
AbstractThe 20S proteasome, isolated from the nocardioform actinomycete Rhodococcus erythropolis str...
Coexpression of both subunits of the Thermoplasma proteasome in Escherichia coli yields fully assemb...
AbstractBackground: The 26S proteasome is the central protease of the ubiquitin-dependent pathway of...
AbstractThe 20 S proteasome, found in eukaryotes and in the archaebacterium Thermoplasma acidophilum...
The proteasome or multicatalytic proteinase is a high molecular mass multisubunit complex ubiquitous...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
AbstractThe proteasome is not simply a “garbage disposal unit” but also has functions in the control...
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 26S proteasome contains a proteolytic core, 20S proteasome, and its regulatory particle,...
We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophil...
AbstractThe final destination of the majority of proteins that have to be selectively degraded in eu...
Proteasome assembly is a rapid and highly sequential process that occurs through a series of interme...