Results 31 to 40 of about 49,650 (285)
RING domain E3 ubiquitin ligases
Annual Review of Biochemistry, 2009 E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate.
Joazeiro, Claudio A. P. +1 more
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The role of E3 ubiquitin ligases and deubiquitinases in bladder cancer development and immunotherapy
Frontiers 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
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
E3 ubiquitin ligases in signaling, disease, and therapeutics. [PDF]
Trends Biochem SciThe 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
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 +12 more
doaj +1 more source
Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins
Frontiers in Immunology, 2021 Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins.
Haoran Cui +7 more
doaj +1 more source
TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions
Computational 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
E3 ubiquitin ligases: styles, structures and functions
Molecular 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
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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
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