Results 11 to 20 of about 11,793 (291)
Deubiquitylating Enzymes in Cancer and Immunity
Advanced Science, 2023 Deubiquitylating enzymes (DUBs) maintain relative homeostasis of the cellular ubiquitome by removing the post‐translational modification ubiquitin moiety from substrates.
Jiang Ren +8 more
doaj +1 more source
Deubiquitinases in hematological malignancies
Biomarker Research, 2021 Deubiquitinases (DUBs) are enzymes that control the stability, interactions or localization of most cellular proteins by removing their ubiquitin modification.
Hu Lei +4 more
doaj +1 more source
Cellular Deubiquitylating Enzyme: A Regulatory Factor of Antiviral Innate Immunity
Frontiers in Microbiology, 2021 Deubiquitylating enzymes (DUBs) are proteases that crack the ubiquitin code from ubiquitylated substrates to reverse the fate of substrate proteins. Recently, DUBs have been found to mediate various cellular biological functions, including antiviral ...
Sijing Long +39 more
doaj +1 more source
Life, 2021 Deubiquitinase (DUB) is an essential component in the ubiquitin—proteasome system (UPS) by removing ubiquitin chains from substrates, thus modulating the expression, activity, and localization of many proteins that contribute to tumor development and ...
Sixuan Li, Hongquan Zhang, Xiaofan Wei
doaj +1 more source
Deubiquitinating enzymes and the proteasome regulate preferential sets of ubiquitin substrates
Nature Communications, 2022 Deubiquitinases (DUBs) remove ubiquitin from its target proteins. Here, authors compare the regulatory effects of the proteasome and DUBs on the ubiquitinated proteome.
Fredrik Trulsson +9 more
doaj +1 more source
Involvement of E3 Ligases and Deubiquitinases in the Control of HIF-α Subunit Abundance
Cells, 2019 The ubiquitin and hypoxia-inducible factor (HIF) pathways are cellular processes involved in the regulation of a variety of cellular functions. Enzymes called ubiquitin E3 ligases perform protein ubiquitylation.
Kateryna Kubaichuk, Thomas Kietzmann
doaj +1 more source
Frontiers in Synaptic Neuroscience, 2017 Posttranslational modification of proteins by ubiquitin regulates synapse development and synaptic transmission. Much progress has been made investigating the role of ubiquitin ligases at the synapse, however very little is known about the ...
Molly Hodul +3 more
doaj +1 more source
The business of deubiquitination – location, location, location [version 1; referees: 2 approved]
F1000Research, 2016 A majority of proteins in the cell can be modified by ubiquitination, thereby altering their function or stability. This ubiquitination is controlled by both ubiquitinating and deubiquitinating enzymes (DUBs). The number of ubiquitin ligases exceeds that
Erin S. Coyne, Simon S. Wing
doaj +1 more source
Hip sonography in Switzerland [PDF]
Exploration of Musculoskeletal DiseasesThe diagnosis of hip dysplasia has developed very differently in different countries over the last few decades. The development and current situation in Switzerland is described in this paper.
Beat Dubs
doaj +1 more source
Deubiquitinases (DUBs) and DUB inhibitors: a patent review [PDF]
Expert Opinion on Therapeutic Patents, 2015 Deubiquitinating-enzymes (DUBs) are key components of the ubiquitin-proteasome system (UPS). The fundamental role of DUBs is specific removal of ubiquitin from substrates. DUBs contribute to activation/deactivation, recycling and localization of numerous regulatory proteins, and thus play major roles in diverse cellular processes.
Pershang, Farshi +6 more
openaire +2 more sources