Results 211 to 220 of about 47,607 (250)
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Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
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The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
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RBR E3 ubiquitin ligases in tumorigenesis
Seminars in Cancer Biology, 2020RING-in-between-RING (RBR) E3 ligases are one class of E3 ligases that is characterized by the unique RING-HECT hybrid mechanism to function with E2s to transfer ubiquitin to target proteins for degradation. Emerging evidence has demonstrated that RBR E3 ligases play essential roles in neurodegenerative diseases, infection, inflammation and cancer ...
Peter, Wang +4 more
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The Role of Ubiquitin E3 Ligase in Atherosclerosis
Current Medicinal Chemistry, 2020Atherosclerosis is a chronic inflammatory vascular disease. Atherosclerotic cardiovascular disease is the main cause of death in both developed and developing countries. Many pathophysiological factors, including abnormal cholesterol metabolism, vascular inflammatory response, endothelial dysfunction and vascular smooth muscle cell proliferation and ...
Zhi-Xiang Zhou +8 more
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Science's STKE, 2004
Protein degradation plays a key role in progression through the cell cycle. The anaphase-promoting complex (APC) is best known for its role as an E3 ubiquitin ligase that contributes to the degradation of proteins that allow exit from mitosis.
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Protein degradation plays a key role in progression through the cell cycle. The anaphase-promoting complex (APC) is best known for its role as an E3 ubiquitin ligase that contributes to the degradation of proteins that allow exit from mitosis.
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E3 ubiquitin ligases for MHC molecules
Current Opinion in Immunology, 2009Recently, novel E3 ubiquitin ligases that target MHC molecules for lysosomal degradation have been discovered by several groups. All these E3s are membrane-bound and possess a variant type RING domain, termed the RING-CH or RING variant (RINGv) domain. They belong to a new E3 family designated Modulator of Immune Recognition (MIR), based on the name of
Satoshi, Ishido +3 more
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Autoantigen Ro52 is an E3 ubiquitin ligase
Biochemical and Biophysical Research Communications, 2006Anti-Ro/SSA antibodies are classic autoantibodies commonly found in patients with Sjögren's syndrome, a chronic autoimmune disease characterized by dryness of the eyes and mouth. The autoantibodies recognize a RING-finger protein, Ro52, whose function is still unknown.
Keiji, Wada, Tetsu, Kamitani
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HECT-Type E3 Ubiquitin Ligases in Cancer
Trends in Biochemical Sciences, 2019Ubiquitination, a post-translational modification that involves a covalent attachment of ubiquitin to a protein substrate, is essential for cellular homeostatic maintenance. At the end of a three-enzyme cascade, E3 ubiquitin ligases (E3s) recruit substrates and promote or directly catalyze ubiquitin transfer to targets.
Francesca Bernassola +2 more
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Pseudophosphatase as E3 ubiquitin ligase inhibitor
Science Signaling, 2017The pseudophosphatase STYX prevents the substrate recognition subunit FBXW7 from binding the catalytic E3 ubiquitin ligase complex.
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Notch Interacts with an E3 Ligase
Science Signaling, 2001The membrane protein Notch transduces signals from the cell surface to the transcription machinery by deploying its cleaved intracellular (IC) domain to the nucleus. It is less clear how Notch action is turned off once its mission is fulfilled in the nucleus.
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Discovery, characterization and engineering of ligases for amide synthesis
Nature, 2021Jason Micklefield +2 more
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