Results 41 to 50 of about 164,141 (292)
Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system [PDF]
Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state
Piotr Bragoszewski +2 more
doaj +1 more source
Ubiquitination and proteasomal degradation of ATG12 regulates its proapoptotic activity [PDF]
During macroautophagy, conjugation of ATG12 to ATG5 is essential for LC3 lipidation and autophagosome formation. Additionally, ATG12 has ATG5-independent functions in diverse processes including mitochondrial fusion and mitochondrial-dependent apoptosis.
Debnath, Jayanta +8 more
core +4 more sources
The nuclear ubiquitin-proteasome system [PDF]
In eukaryotes, thousands of genes have to be organized and expressed in the cell nucleus. Conformational and kinetic instability of nuclear structure and components appear to enable cells to use the encoded information selectively. The ubiquitin-proteasome system is active in distinct nuclear domains and plays a major role controlling the initial steps
openaire +2 more sources
Background Statins are the cornerstone of pharmacotherapy for atherosclerotic cardiovascular disease. While these drugs are generally safe, treatment adherence is not optimal in a considerable proportion of patients because of the adverse effects on ...
Amirhossein Sahebkar +9 more
doaj +1 more source
Viral entry and the ubiquitin‐proteasome system [PDF]
Viruses confiscate cellular components of the ubiquitin-proteasome system (UPS) to facilitate many aspects of the infectious cycle. The 26S proteasome is an ATP-dependent, multisubunit proteolytic machine present in all eukaryotic cells. The proteasome executes the controlled degradation of functional proteins, as well as the hydrolysis of aberrantly ...
Seth M. Schneider +2 more
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The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. [PDF]
p53 and its major E3 ligase Mdm2 are both ubiquitinated and targeted to the proteasome for degradation. Despite the importance of this in regulating the p53 pathway, little is known about the mechanisms of proteasomal recognition of ubiquitinated p53 and
A Arlt +93 more
core +3 more sources
The ubiquitin‐proteasome system in Alzheimer's disease [PDF]
Introduction Biology of the UPS The involvement of the UPS in AD pathogenesis The UPS as a link between Aβ and tau interaction Conclusions AbstractAccumulation of proteins is a recurring event in many neurodegenerative diseases, including Alzheimer's disease (AD).Evidence has suggested that protein accumulation may result from a dysfunction in the ...
openaire +3 more sources
Site-Specific Proteasome Inhibitors
Proteasome is a multi-subunit protein degradation machine, which plays a key role in the maintenance of protein homeostasis and, through degradation of regulatory proteins, in the regulation of numerous cell functions. Proteasome inhibitors are essential
Alexei F. Kisselev
doaj +1 more source
Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster [PDF]
The regulatory complex of the 26S proteasome is responsible for the selective recognition and binding of multiubiquitinated proteins. It was earlier shown that the subunit S5a/Rpn10/p54 of the regulatory complex is the only cellular protein capable of ...
Andó, István +7 more
core +1 more source
The Ubiquitin–Proteasome System in Immune Cells
The ubiquitin–proteasome system (UPS) is the major intracellular and non-lysosomal protein degradation system. Thanks to its unique capacity of eliminating old, damaged, misfolded, and/or regulatory proteins in a highly specific manner, the UPS is ...
Gonca Çetin +4 more
doaj +1 more source

