Results 21 to 30 of about 393,592 (390)
Cellular quality control by the ubiquitin-proteasome system and autophagy
Science, 2019 To achieve homeostasis, cells evolved dynamic and self-regulating quality control processes to adapt to new environmental conditions and to prevent prolonged damage.
C. Pohl, I. Dikič
semanticscholar +1 more source
Regulation of the neuronal proteasome by Zif268 (Egr1) [PDF]
, 2006 Most forms of neuronal plasticity are associated with induction of the transcription factor Zif268 (Egr1/Krox24/NGF-IA). In a genomewide scan, we obtained evidence for potential modulation of proteasome subunit and regulatory genes by Zif268 in neurons,
Conway, A.M., James, A.B., Morris, B.J.
core +2 more sources
Phosphatase UBLCP1 controls proteasome assembly [PDF]
Open Biology, 2017 Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase.
Shuangwu Sun +7 more
doaj +1 more source
Structure and Function of the 26S Proteasome.
Annual Review of Biochemistry, 2018 As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The proteasome's cellular functions range from general protein homeostasis and
J. Bard +5 more
semanticscholar +1 more source
Downregulation of 26S proteasome catalytic activity promotes epithelial-mesenchymal transition. [PDF]
, 2016 The epithelial-mesenchymal transition (EMT) endows carcinoma cells with phenotypic plasticity that can facilitate the formation of cancer stem cells (CSCs) and contribute to the metastatic cascade.
Banno, Asoka +15 more
core +2 more sources
In vitro Reconstitution Assays of Arabidopsis 20S Proteasome
Bio-Protocol, 2021 The majority of cellular proteins are degraded by the 26S proteasome in eukaryotes. However, intrinsically disordered proteins (IDPs), which contain large portions of unstructured regions and are inherently unstable, are degraded via the ubiquitin ...
Yanjun Li +4 more
doaj +1 more source
Proteasome as a Molecular Target of Microcystin-LR
Toxins, 2015 Proteasome degrades proteins in eukaryotic cells. As such, the proteasome is crucial in cell cycle and function. This study proved that microcystin-LR (MC-LR), which is a toxic by-product of algal bloom, can target cellular proteasome and selectively ...
Zhu Zhu, Li Zhang, Guoqing Shi
doaj +1 more source
Regulation of TRIB1 abundance in hepatocyte models in response to proteasome inhibition
Scientific Reports, 2023 Tribbles related homolog 1 (TRIB1) contributes to lipid and glucose homeostasis by facilitating the degradation of cognate cargos by the proteasome. In view of the key metabolic role of TRIB1 and the impact of proteasome inhibition on hepatic function ...
Sébastien Soubeyrand +2 more
doaj +1 more source
Molecular Cell, 2011 Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access.
Stadtmueller, Beth M. +1 more
openaire +2 more sources
Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins [PDF]
, 2008 Background: The delivery of ubiquitinated proteins to the proteasome for degradation is a key step in the regulation of the ubiquitin-proteasome pathway, yet the mechanisms underlying this step are not understood in detail.
Deshaies, Raymond J. +6 more
core +6 more sources