Results 31 to 40 of about 133,567 (215)
SUMO-targeted ubiquitin ligases
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability of its substrate proteins.
R. Jürgen Dohmen +1 more
openaire +3 more sources
RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. [PDF]
PLoS ONE, 2015 In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis.
Thorsten Pfirrmann +5 more
doaj +1 more source
G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase [PDF]
Journal of Biological Chemistry, 2009 Emerging evidence suggests that ubiquitination serves as a protein trafficking signal in addition to its well characterized role in promoting protein degradation. The yeast G protein α subunit Gpa1 represents a rare example of a protein that undergoes both mono- and poly-ubiquitination.
Brian Kuhlman +6 more
openaire +3 more sources
Hepatology Communications, 2021 We aimed to identify a microRNA (miRNA)‐E3 ubiquitin ligase regulatory network for protein substrates enriched in cell death pathways and investigate the underlying molecular mechanisms in alcohol‐associated hepatitis (AH).
Xiude Fan +8 more
doaj +1 more source
Regulation of the CRL4Cdt2 Ubiquitin Ligase and Cell-Cycle Exit by the SCFFbxo11 Ubiquitin Ligase [PDF]
Molecular Cell, 2013 F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression ...
Moritz Horn +11 more
openaire +5 more sources
RING Domain E3 Ubiquitin Ligases [PDF]
Annual Review of Biochemistry, 2009 E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J. +1 more
openaire +4 more sources
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 ...
Matthew Locke +3 more
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E3-ubiquitin ligases and recent progress in osteoimmunology
Frontiers in Immunology, 2023 Ubiquitin-mediated proteasomal degradation is a post-transcriptional protein modification that is comprised of various components including the 76-amino acid protein ubiquitin (Ub), Ub-activating enzyme (E1), Ub-conjugating enzyme (E2), ubiquitin ligase (
Yosuke Asano +8 more
doaj +1 more source
Phosphorylation of Arabidopsis SINA2 by CDKG1 affects its ubiquitin ligase activity
BMC Plant Biology, 2018 Background SEVEN IN ABSENTIA (SINA) is a RING domain-containing ubiquitin ligase involved in Drosophila eye formation. SINA-like proteins in plants are involved in several signaling pathways.
Yang Chen +5 more
doaj +1 more source
CRL4 antagonizes SCFFbxo7-mediated turnover of cereblon and BK channel to regulate learning and memory. [PDF]
PLoS Genetics, 2018 Intellectual disability (ID), one of the most common human developmental disorders, can be caused by genetic mutations in Cullin 4B (Cul4B) and cereblon (CRBN).
Tianyu Song +12 more
doaj +1 more source