title: Limited proteolysis: DisRUPting proteasomal inhibition.
abstract: The 26S proteasome is a protease complex that completely degrades substrate proteins marked with a chain of ubiquitins, but is also able to perform endoproteolytic cleavage. A new study now demonstrates that regulated ubiquitin-proteasome-dependent processing ameliorates proteasomal inhibition.
authors.affiliation: Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Joseph Stelzmann Str. 26, 50931 Cologne, Germany. Electronic address: thorsten.hoppe@uni-koeln.de.
authors.forename: Thorsten
authors.initials: T
authors.lastname: Hoppe
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D051266:Nuclear Respiratory Factor 1 / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D061988:Proteasome Inhibitors / Q000494:pharmacology*
chemical_list: D051266:Nuclear Respiratory Factor 1; D061988:Proteasome Inhibitors; D046988:Proteasome Endopeptidase Complex