Proteasome inhibition elicits an evolutionarily conserved response wherein proteasome
subunit mRNAs are upregulated, resulting in recovery (ie,'bounce-back') of proteasome …

Background Proteasome inhibitors are widely used in the treatment of multiple myeloma and
as research tools. Additionally, diminished proteasome function may contribute to neuronal …

In Saccharomyces cerevisiae, chemical or genetic inhibition of proteasome activity induces
new proteasome synthesis promoted by the transcription factor RPN4. This ensures that …

In response to proteasome dysfunction, mammalian cells upregulate proteasome gene
expression by activating Nrf1. Nrf1 is an endoplasmic reticulum-resident transcription factor …

Protein folding is a substantively error prone process, especially when it occurs in the
endoplasmic reticulum (ER). The highly exquisite machinery in the ER controls secretory …

The ability to adapt to acute oxidative stress (eg H 2 O 2, peroxynitrite, menadione, and
paraquat) through transient alterations in gene expression is an important component of …

Coordinated regulation of the ubiquitin-proteasome system (UPS) is crucial for the cell to
adjust its protein degradation capacity to changing proteolytic requirements. We have shown …

The 26S proteasome is a multisubunit complex that catalyzes the degradation of
ubiquitinated proteins. The proteasome comprises 33 distinct subunits, all of which are …

Proteasome inhibition is used therapeutically to induce proteotoxic stress and trigger
apoptosis in cancer cells that are highly dependent on the proteasome. As a mechanism of …

Nrf1 is a member of the nuclear erythroid 2-like family of transcription factors that regulate
stress-responsive gene expression in animals. Newly synthesized Nrf1 is targeted to the …