Results 11 to 20 of about 47,588 (257)

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

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

E3 ubiquitin ligases: styles, structures and functions

open access: yesMolecular Biomedicine, 2021
E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Quan Yang   +3 more
doaj   +1 more source

TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions

open access: yesComputational and Structural Biotechnology Journal, 2023
Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou   +7 more
doaj   +1 more source

Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex

open access: yesComputational 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

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

E3 ubiquitin ligases in signaling, disease, and therapeutics. [PDF]

open access: yesTrends Biochem Sci
The ubiquitin-proteasome system (UPS) is a central regulator of protein turnover and signaling, with E3 ubiquitin ligases conferring substrate specificity and chain-type control. Recent advances have revealed new mechanistic classes of E3 ligases and expanded our understanding of their roles in disease, including cancer, neurodegeneration, and immune ...
Ebadi P, Stratton CM, Olsen SK.
europepmc   +3 more sources

Activation of the E3 ubiquitin ligase Parkin [PDF]

open access: yesBiochemical Society Transactions, 2015
The PINK1 (phosphatase and tensin homologue-induced putative kinase 1)/Parkin-dependent mitochondrial quality control pathway mediates the clearance of damaged organelles, but appears to be disrupted in Parkinson's disease (PD) [Springer and Kahle (2011) Autophagy 7, 266–278].
Thomas R, Caulfield   +2 more
openaire   +2 more sources

E3 Ubiquitin Ligases in Breast Cancer Metastasis: A Systematic Review of Pathogenic Functions and Clinical Implications

open access: yesFrontiers in Oncology, 2021
Female breast cancer has become the most commonly occurring cancer worldwide. Although it has a good prognosis under early diagnosis and appropriate treatment, breast cancer metastasis drastically causes mortality.
Yingshuang Wang   +8 more
doaj   +1 more source

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