Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum
Scientific Reports, 2021 The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma +2 more
doaj +1 more source
RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]
, 2014 The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S. +2 more
core +1 more source
The ubiquitin–protein ligase Itch regulates p73 stability [PDF]
The EMBO Journal, 2005 p73, a member of the p53 family of transcription factors, is upregulated in response to DNA damage, inducing cell cycle arrest and apoptosis. Besides indications that this p73 response is post-transcriptional, little is known about the underlying molecular mechanisms of p73 protein degradation.
Gianni Cesareni +10 more
openaire +3 more sources
Genome-Wide Identification and Expression of Xenopus F-Box Family of Proteins. [PDF]
PLoS ONE, 2015 Protein degradation via the multistep ubiquitin/26S proteasome pathway is a rapid way to alter the protein profile and drive cell processes and developmental changes.
Banu Saritas-Yildirim +3 more
doaj +1 more source
The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]
, 2018 Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren +4 more
core +1 more source
Research Progress on the Role of E3 Ubiquitin Ligases in Regulating the Growth, Development and Stress Response of Fruits and Vegetables [PDF]
Shipin KexueProtein ubiquitination, an important post-translational modification, plays a wide role in the life activities of eukaryotic cells. E3 ubiquitin ligases specifically recognize target proteins in the ubiquitin-proteasome degradation system and play a ...
DING Jun, LI Fujun, LI Xiao’an, ZHANG Xinhua
doaj +1 more source
Computational and Structural Biotechnology Journal, 2022 Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou +7 more
doaj +1 more source
RNF125 is a Ubiquitin-Protein Ligase that Promotes p53 Degradation [PDF]
Cellular Physiology and Biochemistry, 2015 Background/Aims: Although early studies show that Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. Here, we investigated the role of RNF125, a non-Mdm2 ubiquitin-protein ligase, in the regulation of p53.
Zhanhui Miao +6 more
openaire +4 more sources
E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration
Frontiers in Molecular Neuroscience, 2017 Cells regularly synthesize new proteins to replace old or damaged proteins. Deposition of various aberrant proteins in specific brain regions leads to neurodegeneration and aging.
Arun Upadhyay +6 more
doaj +1 more source
E3Miner: a text mining tool for ubiquitin-protein ligases [PDF]
Nucleic Acids Research, 2008 Ubiquitination is a regulatory process critically involved in the degradation of >80% of cellular proteins, where such proteins are specifically recognized by a key enzyme, or a ubiquitin-protein ligase (E3). Because of this important role of E3s, a rapidly growing body of the published literature in biology and biomedical fields reports novel findings
Lee, H +2 more
openaire +4 more sources