Results 31 to 40 of about 327,531 (416)
Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads
BMC Pharmacology and Toxicology, 2017 Background Protein ubiquitylation is an important post-translational regulation, which has been shown to be necessary for life cycle progression and survival of Plasmodium falciparum.
Jagrati Jain +3 more
doaj +1 more source
Cell, 2016 Ubiquitination is a post-translational modification of proteins involved in a variety of cellular processes. Ubiquitination requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases).
Helen Walden, Francesca E. Morreale
openaire +3 more sources
Adaptors as the regulators of HECT ubiquitin ligases [PDF]
Cell Death & Differentiation, 2021 The HECT (homologous to E6AP C-terminus) ubiquitin ligases (E3s) are a small family of highly conserved enzymes involved in diverse cellular functions and pathological conditions. Characterised by a C-terminal HECT domain that accepts ubiquitin from E2 ubiquitin conjugating enzymes, these E3s regulate key signalling pathways.
Sonia Shalini Shah, Sharad Kumar
openaire +5 more sources
Frontiers in Endocrinology, 2023 E3 ubiquitin ligases are important components of the ubiquitin protease system. This family includes many proteins, which can catalyze the ubiquitination of a variety of protein substrates and promote the degradation of them by the proteasome system ...
Jun Feng +7 more
doaj +1 more source
Selective targeting of activating and inhibitory Smads by distinct WWP2 ubiquitin ligase isoforms differentially modulates TGFβ signalling and EMT [PDF]
, 2011 Ubiquitin-dependent mechanisms have emerged as essential regulatory elements controlling cellular levels of Smads and TGFß-dependent biological outputs such as epithelial–mesenchymal transition (EMT). In this study, we identify a HECT E3 ubiquitin ligase
A Chantry +35 more
core +1 more source
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
core +2 more sources
The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets
Journal of Cell Biology, 2019 Mysterin, also known as RNF213, is an intracellular protein that forms large toroidal oligomers. Mysterin was originally identified in genetic studies of moyamoya disease (MMD), a rare cerebrovascular disorder of unknown etiology. While mysterin is known
Munechika Sugihara +7 more
semanticscholar +1 more source
The E3 ubiquitin ligase Pellino2 mediates priming of the NLRP3 inflammasome
Nature Communications, 2018 The NLRP3 inflammasome has an important function in inflammation by promoting the processing of pro-IL-1β and pro-IL-18 to their mature bioactive forms, and by inducing cell death via pyroptosis.
Fiachra Humphries +8 more
semanticscholar +1 more source
Dysregulation of ubiquitin ligases in cancer [PDF]
Drug Resistance Updates, 2015 Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs ...
Ze'ev Ronai, Jianfei Qi
openaire +2 more sources
Self‐regulating ubiquitin ligases [PDF]
The EMBO Journal, 2017 Occasional auto‐modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published in The EMBO Journal now show that in the case of Rsp5/Nedd4, auto‐ubiquitylation instead triggers oligomerization and concomitant reduction of ligase activity. This novel mechanism therefore creates silenced ligases that remain
Spencer Hill, Gary Kleiger
openaire +2 more sources