Results 11 to 20 of about 47,607 (250)

RBR E3‐ligases at work [PDF]

open access: yesThe EMBO Reports, 2014
The RING-in-between-RING (RBR) E3s are a curious family of ubiquitin E3-ligases, whose mechanism of action is unusual in several ways. Their activities are auto-inhibited, causing a requirement for activation by protein-protein interactions or posttranslational modifications.
Judith J, Smit, Titia K, Sixma
openaire   +2 more sources

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity [PDF]

open access: yesNature, 2018
Ubiquitination is initiated by transfer of ubiquitin (Ub) from a ubiquitin-activating enzyme (E1) to a ubiquitin-conjugating enzyme (E2), producing a covalently linked intermediate (E2-Ub) 1 . Ubiquitin ligases (E3s) of the 'really interesting new gene' (RING) class recruit E2-Ub via their RING domain and then mediate direct transfer of ubiquitin to ...
Pao, Kuan-Chuan   +9 more
openaire   +3 more sources

The role of E3 ubiquitin ligases and deubiquitinases in bladder cancer development and immunotherapy

open access: yesFrontiers in Immunology, 2023
Bladder cancer is one of the common malignant urothelial tumors. Post-translational modification (PTMs), including ubiquitination, acetylation, methylation, and phosphorylation, have been revealed to participate in bladder cancer initiation and ...
Xuemei Wang   +4 more
doaj   +1 more source

The involvement of E3 ubiquitin ligases in the development and progression of colorectal cancer

open access: yesCell Death Discovery, 2023
To date, colorectal cancer (CRC) still has limited therapeutic efficacy and poor prognosis and there is an urgent need for novel targets to improve the outcome of CRC patients.
Jie Chen   +8 more
doaj   +1 more source

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

open access: yesCells, 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

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

open access: yesThoracic 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   +12 more
doaj   +1 more source

Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer

open access: yesPathology 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   +5 more
doaj   +1 more source

Structural Diversity of Ubiquitin E3 Ligase [PDF]

open access: yesMolecules, 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

open access: yesBiomolecules, 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   +4 more
doaj   +1 more source

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

open access: yesFrontiers 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

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