Results 341 to 350 of about 393,592 (390)
Some of the next articles are maybe not open access.
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction.
Physiological Reviews, 2002Between the 1960s and 1980s, most life scientists focused their attention on studies of nucleic acids and the translation of the coded information. Protein degradation was a neglected area, considered to be a nonspecific, dead-end process.
M. Glickman, A. Ciechanover
semanticscholar +1 more source
Proteasome and myogenesis [PDF]
Molecular Biology Reports, 1997 In this report, we examine the involvement of the ubiquitin-proteasome pathway during fusion and differentiation of myoblast primary cell cultures. Up-regulation of proteasome was observed at the maximum fusion rate and was preceded by an increase of unidentified ubiquitin-conjugates.
Valérie Montel +3 more
openaire +2 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 +3 more sources
The 26S proteasome: a molecular machine designed for controlled proteolysis.
Annual Review of Biochemistry, 1999In 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 from approximately 31 different subunits, which catalyzes protein degradation.
D. Voges, P. Zwickl, W. Baumeister
semanticscholar +1 more source
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
Yeast 26S proteasome bound to ubiquitinated substrate (1D* motor state)
, 2018The 26S proteasome is the primary eukaryotic degradation machine and thus is critically involved in numerous cellular processes. The heterohexameric adenosine triphosphatase (ATPase) motor of the proteasome unfolds and translocates targeted protein ...
A. H. D. L. Pena +4 more
semanticscholar +1 more source
Science, 1995
The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway.
M. Pagano +8 more
semanticscholar +1 more source
The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway.
M. Pagano +8 more
semanticscholar +1 more source