Results 31 to 40 of about 18,290,537 (258)
Up-regulation of ubiquitin–proteasome activity upon loss of NatA-dependent N-terminal acetylation
Life Science Alliance, 2022 Inactivation of N-terminal acetyltransferase A is found to alter Rpn4 as well as E3 ligase abundance, causing up-regulation of Ubiquitin–proteasome activity.
Ilia Kats +6 more
doaj +1 more source
Regulation of SCF Ubiquitin Ligases by Jab1/Csn5 and the Cop9 Signalosome [PDF]
, 2006 SCF ubiquitin ligases regulate the ubiquitin-dependent proteolysis of a myriad of substrate proteins, including p27, Cyclin E, and IkBa. To further gain insight into SCF regulation and function, we purified SCF from mammalian cells and found the Cop9 ...
Cope, Gregory Allan
core +1 more source
Ubiquitin-dependent and -independent proteasomal protein degradation.
, 2023 A. UPS protein degradation resulting from (1) ubiquitin system targeting followed by (2) proteasomal protein degradation. B. Proteins with ubiquitin-independent degrons are directly bound and degraded by the proteasome without ubiquitin system targeting.
Frank W. Albert (7879037) +2 more
core +1 more source
Journal of Cachexia, Sarcopenia and Muscle, 2020 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
Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system [PDF]
Open Biology, 2017 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
Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements [PDF]
, 2002 The subunit contacts in the regulatory complex of the Drosophila 26 S proteasome were studied through the cross-linking of closely spaced subunits of the complex, and analysis of the cross-linking pattern in an immunoblot assay with the use of subunit ...
Kapelari, Barbara +13 more
core +2 more sources
The Ubiquitin–Proteasome System in Immune Cells
Biomolecules, 2021 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
Site-Specific Proteasome Inhibitors
Biomolecules, 2021 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
Fluorescence-based proteasome activity profiling [PDF]
, 2011 With the proteasome emerging as a therapeutic target for cancer treatment, accurate tools for monitoring proteasome (inhibitor) activity are in demand.
Jong, A. +9 more
core +1 more source
Dual Function of USP14 Deubiquitinase in Cellular Proteasomal Activity and Autophagic Flux
Cell Reports, 2018 Summary: The ubiquitin-proteasome system and the autophagy-lysosome system are two major intracellular proteolytic pathways in eukaryotes. Although several biochemical mechanisms underlying the crosstalk between them have been suggested, little is known ...
Eunkyoung Kim +9 more
doaj +1 more source