Results 341 to 350 of about 411,261 (379)
Inhibition of Proteasome LMP2 Activity Suppresses <i>Chil3</i> Expression in Mouse Colon Adenocarcinoma Tissue and Restrains Tumor Growth. [PDF]
Oncol ResAstakhova TM +9 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
The proteasome and proteasome inhibitors in multiple myeloma
Cancer and Metastasis Reviews, 2017Proteasome inhibitors are one of the most important classes of agents to have emerged for the treatment of multiple myeloma in the past two decades, and now form one of the backbones of treatment. Three agents in this class have been approved by the United States Food and Drug Administration-the first-in-class compound bortezomib, the second-generation
S. Gandolfi +5 more
semanticscholar +3 more sources
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.
W, Baumeister, A, Lupas
openaire +2 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.
W, Baumeister, A, Lupas
openaire +2 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
THE PROTEASOME AND PROTEASOME INHIBITORS IN CANCER THERAPY
Annual Review of Pharmacology and Toxicology, 2006▪ Abstract The proteasome, a multicatalytic proteinase complex, is responsible for the majority of intracellular protein degradation. Pharmacologic inhibitors of the proteasome possess in vitro and in vivo antitumor activity, and bortezomib, the first such agent to undergo clinical testing, has significant efficacy against multiple myeloma and non ...
Peter M, Voorhees, Robert Z, Orlowski
openaire +2 more sources
Cellular and Molecular Life Sciences, 2014
In eukaryotic cells, proteasomes are highly conserved protease complexes and eliminate unwanted proteins which are marked by poly-ubiquitin chains for degradation. The 26S proteasome consists of the proteolytic core particle, the 20S proteasome, and the 19S regulatory particle, which are composed of 14 and 19 different subunits, respectively ...
Zhu Chao, Gu, Cordula, Enenkel
openaire +2 more sources
In eukaryotic cells, proteasomes are highly conserved protease complexes and eliminate unwanted proteins which are marked by poly-ubiquitin chains for degradation. The 26S proteasome consists of the proteolytic core particle, the 20S proteasome, and the 19S regulatory particle, which are composed of 14 and 19 different subunits, respectively ...
Zhu Chao, Gu, Cordula, Enenkel
openaire +2 more sources
Essays in Biochemistry, 2005
The major enzyme system catalysing the degradation of intracellular proteins is the proteasome system. A central inner chamber of the cylinder-shaped 20 S proteasome contains the active site, formed by N-terminal threonine residues. The 20 S proteasomes are extremely inefficient in degrading folded protein substrates and therefore one or two ...
openaire +2 more sources
The major enzyme system catalysing the degradation of intracellular proteins is the proteasome system. A central inner chamber of the cylinder-shaped 20 S proteasome contains the active site, formed by N-terminal threonine residues. The 20 S proteasomes are extremely inefficient in degrading folded protein substrates and therefore one or two ...
openaire +2 more sources
Molecular Biology Reports, 1997
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease ...
A, Lupas +6 more
openaire +2 more sources
Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease ...
A, Lupas +6 more
openaire +2 more sources
2023
The proteasome is a multi-subunit proteolytic complex that functions to degrade normal proteins for physiological regulation and to eliminate abnormal proteins for cellular protection. Generally, the proteasome targets substrate proteins that are marked by attachment of multiple ubiquitin molecules.
Hegde, Ashok N. +3 more
openaire +3 more sources
The proteasome is a multi-subunit proteolytic complex that functions to degrade normal proteins for physiological regulation and to eliminate abnormal proteins for cellular protection. Generally, the proteasome targets substrate proteins that are marked by attachment of multiple ubiquitin molecules.
Hegde, Ashok N. +3 more
openaire +3 more sources