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Specificities and redundancies in the NEL family of bacterial E3 ubiquitin ligases of Salmonella enterica serovar Typhimurium. [PDF]
Front ImmunolBullones-Bolaños A +4 more
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Regulation of the water channel aquaporin-2 by cullin E3 ubiquitin ligases.
Am J Physiol Renal PhysiolMurali SK, McCormick JA, Fenton RA.
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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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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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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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An expanded lexicon for the ubiquitin code
Nature Reviews Molecular Cell Biology, 2022Ivan Đikić, Brenda A Schulman
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