Results 31 to 40 of about 47,607 (250)
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
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Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control
Molecules, 2021 Skeletal muscle loss is a detrimental side-effect of numerous chronic diseases that dramatically increases mortality and morbidity. The alteration of protein homeostasis is generally due to increased protein breakdown while, protein synthesis may also be
Dulce Peris-Moreno +4 more
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Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA
Frontiers in Plant Science, 2021 Protein modification by the small ubiquitin-like modifier (SUMO) plays an important role in multiple plant processes, including growth, development, and the response to abiotic stresses.
Souleimen Jmii, Laurent Cappadocia
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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
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TRIM32 is an E3 ubiquitin ligase for dysbindin [PDF]
Human Molecular Genetics, 2009 Mutations in the gene encoding tripartite motif protein 32 (TRIM32) cause two seemingly diverse diseases: limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11(BBS11). Although TRIM32 is involved in protein ubiquitination, its substrates and the molecular consequences of disease-causing ...
Locke, Matthew +3 more
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Entropy-Driven Mechanism of an E3 Ligase [PDF]
Biochemistry, 2011 Ubiquitin-like modifications are macromolecular chemistry for which our understanding of the enzymatic mechanisms is lacking. Most E3 ligases in ubiquitin-like modifications do not directly participate in chemistry but are thought to confer allosteric effects; however, the nature of the allosteric effects has been elusive.
Khue, Truong +3 more
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Small Molecule Modulators of RING-Type E3 Ligases: MDM and Cullin Families as Targets
Frontiers in Pharmacology, 2018 Ubiquitin–proteasome system (UPS) is a primary signaling pathway for regulation of intracellular protein levels. E3 ubiquitin ligases, substrate-specific members of the UPS, represent highly attractive protein targets for drug discovery.
Emil Bulatov +4 more
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WWP2 is an E3 ubiquitin ligase for PTEN [PDF]
Nature Cell Biology, 2011 PTEN, a lipid phosphatase, is one of the most frequently mutated tumour suppressors in human cancer. Several recent studies have highlighted the importance of ubiquitylation in regulating PTEN tumour-suppressor function, but the enzymatic machinery required for PTEN ubiquitylation is not clear.
Subbareddy, Maddika +6 more
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Frontiers in Cell and Developmental BiologyE3 ubiquitin ligases are key determinants of substrate specificity within the ubiquitin–proteasome system and have emerged as important regulators of skeletal biology.
Yutong Zhao +4 more
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Regulating the human HECT E3 ligases [PDF]
Cellular and Molecular Life Sciences, 2018 Ubiquitination, the covalent attachment of ubiquitin to proteins, by E3 ligases of the HECT (homologous to E6AP C terminus) family is critical in controlling diverse physiological pathways. Stringent control of HECT E3 ligase activity and substrate specificity is essential for cellular health, whereas deregulation of HECT E3s plays a prominent role in ...
Sluimer, Jasper, Distel, Ben
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