Results 211 to 220 of about 198,410 (265)
Proteasome subunit PSMD1 is a key therapeutic target in multiple myeloma.
Du T +18 more
europepmc +1 more source
Temporal- and sex-specific changes in proteasome-dependent and independent polyubiquitination in the amygdala during fear memory formation. [PDF]
Brown B +5 more
europepmc +1 more source
Thymic cortical epithelial Psmb11-encoded β5t in mouse and human. [PDF]
Yang MT +11 more
europepmc +1 more source
The accessory adapters FAF1, FAF2, and UBXN7 accelerate proteasomal degradation by increasing prior p97-mediated substrate unfolding. [PDF]
Kracht M +6 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Annual Review of Biophysics and Biomolecular Structure, 1999
▪ Abstract Proteasomes are large multisubunit proteases that are found in the cytosol, both free and attached to the endoplasmic reticulum, and in the nucleus of eukaryotic cells. Their ubiquitous presence and high abundance in these compartments reflects their central role in cellular protein turnover.
M, Bochtler +4 more
openaire +2 more sources
▪ Abstract Proteasomes are large multisubunit proteases that are found in the cytosol, both free and attached to the endoplasmic reticulum, and in the nucleus of eukaryotic cells. Their ubiquitous presence and high abundance in these compartments reflects their central role in cellular protein turnover.
M, Bochtler +4 more
openaire +2 more sources
Current Opinion in Structural Biology, 1997
The proteasome is a macromolecular assembly that is designed to confine proteolytic activity to an inner cavity. Access to the central proteolytic nanocompartment is restricted to unfolded proteins, which necessitates a functional coupling of the 20S proteasome to a substrate-recognition and unfolding machinery.
Baumeister, W., Lupas, A.
openaire +4 more sources
The proteasome is a macromolecular assembly that is designed to confine proteolytic activity to an inner cavity. Access to the central proteolytic nanocompartment is restricted to unfolded proteins, which necessitates a functional coupling of the 20S proteasome to a substrate-recognition and unfolding machinery.
Baumeister, W., Lupas, A.
openaire +4 more sources
Seminars in Oncology, 2004
The proteasome is an abundant multicatalytic enzyme complex present in the cytoplasm and nucleus of all eukaryotic cells. The primary function of the proteasome is to degrade proteins. While it was once thought to act primarily as a cellular "garbage disposal" that removed damaged or misfolded proteins from cells, the proteasome is now known to also ...
openaire +4 more sources
The proteasome is an abundant multicatalytic enzyme complex present in the cytoplasm and nucleus of all eukaryotic cells. The primary function of the proteasome is to degrade proteins. While it was once thought to act primarily as a cellular "garbage disposal" that removed damaged or misfolded proteins from cells, the proteasome is now known to also ...
openaire +4 more sources

