Results 21 to 30 of about 105,668 (286)

From Drosophila to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease

Cells, 2022
The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes.
Valérie C. Cabana, Marc P. Lussier
doaj   +1 more source

Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer

Pathology and Oncology Research, 2023
Gastric cancer (GC) is one of the most pernicious gastrointestinal tumors with extraordinarily high incidence and mortality. Ubiquitination modification of cellular signaling proteins has been shown to play important roles in GC tumorigenesis ...
Aiqin Sun, Aiqin Sun, Xianyan Tian, Yifei Chen, Wannian Yang, Qiong Lin   +5 more
doaj   +1 more source

Comprehensive analysis of the expression and prognosis for RBR E3 ubiquitin ligases in lung adenocarcinoma

Thoracic Cancer, 2022
Background Lung adenocarcinoma (LUAD) is the most common subtype of non‐small cell lung cancer and has a poor prognosis. RBR E3 ubiquitin ligases are a special class of E3 ubiquitin ligases which contain three zinc‐bing domains that catalyze ubiquitin to
Hao Ding, Yuxin Wang, Yuan Cui, Zhike Chen, Yu Li, Jian Yang, Yang Yang, Tengfei Chen, Dian Xia, Chang Li, Chun Xu, Cheng Ding, Jun Zhao   +12 more
doaj   +1 more source

Structural Diversity of Ubiquitin E3 Ligase [PDF]

Molecules, 2021
The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1),
Toma-Fukai, Sachiko, Shimizu, Toshiyuki
openaire   +3 more sources

Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity

Biomolecules, 2022
In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu, Julia Fux, Evan Mallette, Nathaniel Petersen, Wei Zhang   +4 more
doaj   +1 more source

Classification of barley U-box E3 ligases and their expression patterns in response to drought and pathogen stresses

BMC Genomics, 2019
Background Controlled turnover of proteins as mediated by the ubiquitin proteasome system (UPS) is an important element in plant defense against environmental and pathogen stresses.
Moon Young Ryu, Seok Keun Cho, Yourae Hong, Jinho Kim, Jong Hum Kim, Gu Min Kim, Yan-Jun Chen, Eva Knoch, Birger Lindberg Møller, Woo Taek Kim, Michael Foged Lyngkjær, Seong Wook Yang   +11 more
doaj   +1 more source

Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity. [PDF]

Int J Mol Sci
Doxorubicin (Dox) is a widely used anti-cancer drug. It has proven efficacy against various cancers, although the clinical application of Dox has been limited due to dose-dependent, irreversible, and fatal Dox-induced cardiotoxicity (DIC).
Tachibana S, Otaki Y, Goto J, Watanabe T, Watanabe M.   +4 more
europepmc   +2 more sources

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. [PDF]

, 2013
Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 ...
Bullock, AN, Canning, P, Marsden, BD, Gileadi, Opher, Gileadi, O, Krojer, Tobias, Pike, AC, von Delft, F, Hojzan, V, Thangaratnarajah, C, Murray, James W., Cooper, CD, Keates, Tracy, Thangaratnarajah, Chancievan, Bullock, Alex N., Knapp, Stefan, Marsden, Brian D., Knapp, S, Hojzan, Viktorija, Murray, JW, von Delft, Frank, Chaikuad, A, Keates, T, Ayinampudi, Vikram, Ayinampudi, V, Pike, Ashley C.W., Chaikuad, Apirat, Krojer, T, Canning, Peter, Cooper, Christopher D.O., Bullock, Alexander   +30 more
core   +1 more source

Nt-acetylation-independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases [PDF]

, 2023
The acetylation-dependent (Ac/)N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by E3 ligases called Ac/N-recognins. To date, specific Ac/N-recognins have not been defined in plants.
Bailey, Mark, Juliet C Coates, Cao, Xulyu, Cao, X., Meinnel, T., Giglione, C., Wirtz, Markus, Thierry Meinnel, Daniel J Gibbs, Gibbs, Daniel, Armbruster, L., Coates, Juliet, Boyer, Jean-Baptiste, Etherington, Ross, Laura Armbruster, Xulyu Cao, Carmela Giglione, Wirtz, M., Bailey, M., Meinnel, Thierry, Jean-Baptiste Boyer, Gibbs, D. J., Markus Wirtz, Armbruster, Laura, Boyer, J-B., Gibbs, Daniel; id_orcid, Ross D Etherington, Mark Bailey, Etherington, R. D., Coates, J. C., Giglione, Carmela   +30 more
core   +1 more source

Exploration of Aberrant E3 Ligases Implicated in Alzheimer’s Disease and Development of Chemical Tools to Modulate Their Function

Frontiers in Cellular Neuroscience, 2021
The Ubiquitin Proteasome System (UPS) is responsible for the degradation of misfolded or aggregated proteins via a multistep ATP-dependent proteolytic mechanism. This process involves a cascade of ubiquitin (Ub) transfer steps from E1 to E2 to E3 ligase.
Frances M. Potjewyd, Alison D. Axtman
doaj   +1 more source