Results 261 to 270 of about 197,780 (305)
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E3 ligase RCHY1 negatively regulates HDAC2

Biochemical and Biophysical Research Communications, 2020
HDAC2, 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
openaire   +2 more sources

RBR E3 ubiquitin ligases in tumorigenesis

Seminars in Cancer Biology, 2020
RING-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
openaire   +2 more sources

E3 ubiquitin ligases for MHC molecules

Current Opinion in Immunology, 2009
Recently, 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
openaire   +2 more sources

PROTAC-mediated crosstalk between E3 ligases

Chemical Communications, 2019
Small-molecule heterobifunctional degraders can effectively control protein levels and are useful research tools.
Christian Steinebach   +10 more
openaire   +2 more sources

Dueling E3 Ligases

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.
openaire   +1 more source

HECT-Type E3 Ubiquitin Ligases in Cancer

Trends in Biochemical Sciences, 2019
Ubiquitination, 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
openaire   +4 more sources

Pseudophosphatase as E3 ubiquitin ligase inhibitor

Science Signaling, 2017
The pseudophosphatase STYX prevents the substrate recognition subunit FBXW7 from binding the catalytic E3 ubiquitin ligase complex.
openaire   +2 more sources

Systemwide disassembly and assembly of SCF ubiquitin ligase complexes

Cell, 2023
Kheewoong Baek   +2 more
exaly  

E3 Ubiquitin Ligases

2012
Uwe Proske   +27 more
openaire   +1 more source

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