Results 261 to 270 of about 211,577 (291)
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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
openaire +2 more sources
NEDD4 E3 ligase: Functions and mechanism in human cancer.
Seminars in Cancer Biology, 2020A growing amount of evidence indicates that the neuronally expressed developmentally downregulated 4 (NEDD4, also known as NEDD4-1) E3 ligase plays a critical role in a variety of cellular processes via the ubiquitination-mediated degradation of multiple
Zhi-wei Wang +5 more
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E3 ligase RCHY1 negatively regulates HDAC2
Biochemical and Biophysical Research Communications, 2020HDAC2, one of the class I histone deacetylase regulates epigenetic landscape through histone modification. Because HDAC2 is overexpressed in many cancers, cancer therapeutics against HDAC2 have been developed. Here we show novel mechanism of HDAC2 regulation by E3 ligase RCHY1.
Mina Choi +5 more
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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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PROTAC-mediated crosstalk between E3 ligases
Chemical Communications, 2019Small-molecule heterobifunctional degraders can effectively control protein levels and are useful research tools.
Christian Steinebach +10 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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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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Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex
Nature Chemical Biology, 2019D. Bussiere +26 more
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