Results 101 to 110 of about 76,539 (287)
Advanced Science, EarlyView.Porcine deltacoronavirus (PDCoV) infection induces severe intestinal inflammation and acute diarrhea in piglets, yet the molecular mechanism remains incompletely understood. The M protein activates NLRP3 inflammasome through dual mechanisms: direct binding to the NLRP3 LRR domain and disruption of TRIM31‐mediated K48‐linked ubiquitination.
Jinhui Hou +11 more
wiley +1 more source
Toward an atomic model of the 26S proteasome [PDF]
Current Opinion in Structural Biology, 2009 Since the discovery of the 26S proteasome, much progress has been made in determining the structure of this large dynamic protein complex. Until now, a vast amount of structural information of the proteasome has been obtained from all kinds of structure determination techniques, and the function of the protease core is well understood at atomic detail.
openaire +2 more sources
Proteins interacting with the 26S proteasome.
, 2004 Udgivelsesdato: 2004-JulThe 26S proteasome is the multi-protein protease that recognizes and degrades ubiquitinylated substrates targeted for destruction by the ubiquitin pathway.
Gordon, C, Hartmann-Petersen, R
core +1 more source
Advanced Science, EarlyView.Depression is increasingly recognized as a risk factor for chronic diseases, yet its biological impact on cancer remains unclear. Using data from more than 490 000 participants across three international cohorts, we show that depression significantly increases the risk of liver cancer.
Ruijiang Zeng +10 more
wiley +1 more source
Proteasome-associated HECT-type ubiquitin ligase activity is required for plant immunity.
PLoS Pathogens, 2018 Regulated degradation of proteins by the 26S proteasome plays important roles in maintenance and signalling in eukaryotic cells. Proteins are marked for degradation by the action of E3 ligases that site-specifically modify their substrates by adding ...
James J Furniss +6 more
doaj +1 more source
Redox regulation of the proteasome via S-glutathionylation
Redox Biology, 2014 The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis.
Marilene Demasi +9 more
doaj +1 more source
Parkin Directly Modulates 26S Proteasome Activity
, 2010 Parkinson's disease (PD) is a common neurodegenerative disease that involves the deterioration of dopaminergic neurons in the substantia nigra pars compacta.
Boram Min +10 more
core +1 more source
Reversible 26S proteasome disassembly upon mitochondrial stress [PDF]
, 2014 In eukaryotic cells, proteasomes exist primarily as 26S holoenzymes, the most efficient configuration for ubiquitinated protein degradation. Here, we show that acute oxidative stress caused by environmental insults or mitochondrial defects results in ...
Cohen, Mickael +23 more
core +1 more source
Advanced Science, EarlyView.USP10 binds to and stabilizes PFKFB4, enhancing glycolytic ATP production, which activates the urea cycle and elevates fumarate. This inhibits histone demethylase KDM1A, leading to increased H3K4me1 enrichment at the Rad51 promoter and direct activation of Rad51 transcription, which confers lung cancer radioresistance. The PFKFB4 inhibitor 5MPN targets
Yunshang Chen +7 more
wiley +1 more source
Autoregulation of the 26S proteasome by in situ ubiquitination
Molecular Biology of the Cell, 2014 The 26S proteasome degrades ubiquitinated proteins, and proteasomal degradation controls various cellular events. Here we report that the human 26S proteasome is ubiquitinated, by which the ubiquitin receptors Adrm1 and S5a, the ATPase subunit Rpt5, and the deubiquitinating enzyme Uch37 are ubiquitinated in situ by proteasome-associating ubiquitination
Jacobson, Andrew D. +4 more
openaire +2 more sources