Results 11 to 20 of about 411,261 (379)
Modelling Proteasome and Proteasome Regulator Activities [PDF]
Biomolecules, 2014 Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes.
Juliane Liepe +4 more
doaj +6 more sources
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 +8 more sources
Deubiquitination Reactions on the Proteasome for Proteasome Versatility [PDF]
International Journal of Molecular Sciences, 2020 The 26S proteasome, a master player in proteolysis, is the most complex and meticulously contextured protease in eukaryotic cells. While capable of hosting thousands of discrete substrates due to the selective recognition of ubiquitin tags, this protease complex is also dynamically checked through diverse regulatory mechanisms.
Ji Yeong Shin +5 more
openaire +3 more sources
The ubiquitin‐proteasome pathway and proteasome inhibitors [PDF]
Medicinal Research Reviews, 2001 AbstractThe ubiquitin‐proteasome pathway has emerged as a central player in the regulation of several diverse cellular processes. Here, we describe the important components of this complex biochemical machinery as well as several important cellular substrates targeted by this pathway and examples of human diseases resulting from defects in various ...
J, Myung, K B, Kim, C M, Crews
openaire +2 more sources
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
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
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
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
Proteasome in action: substrate degradation by the 26S proteasome [PDF]
Biochemical Society Transactions, 2021 Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S proteasome. Additionally, a disordered segment on the substrate — either intrinsic or induced — is critical for proteasome engagement. The proteasome is geared to interact with both of these substrate features and prepare it for degradation.
Indrajit Sahu, Michael H. Glickman
openaire +2 more sources