Streptomycetes are the most abundant source of antibiotics. Typically, each species
produces several antibiotics, with the profile being species specific. Streptomyces coelicolor …

▪ 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 production of nitric oxide and other reactive nitrogen intermediates (RNI) by
macrophages helps to control infection by Mycobacterium tuberculosis (Mtb). However, the …

The proteasome is a cellular protease responsible for the selective degradation of the
majority of the intracellular proteome. It recognizes, unfolds, and cleaves proteins that are …

In eukaryotes, the 20 S proteasome is the proteolytic core of the 26 S proteasome, which
degrades ubiquitinated proteins in an ATP-dependent process. Archaebacteria lack …

In eukaryotic cells, the vast majority of proteins in the cytosol and nucleus are degraded via
the proteasome–ubiquitin pathway. The 26S proteasome is a huge protein degradation …

The striking identification of an apparent proteasome core in Mycobacteria and allied
actinomycetes suggested that additional elements of this otherwise strictly eukaryotic system …

Abstract 20S proteasomes constitute the proteolytic core of large protease complexes found
in all branches of life. Among these, the eukaryotic 26S proteasome ubiquitously poses as a …

The proteasome represents the major non-lysosomal proteolytic system in eukaryotes. It
confines proteolytic activity to an inner compartment that is accessible to unfolded proteins …

The 26 S proteasome is a large eukaryotic protease complex acting in ubiquitin-mediated
degradation of abnormal and many short-lived, regulatory proteins. Its cylinder-shaped 20 S …