Sort   by:  
 Page size 
TranscriptomicsE2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets by cascades of E1, E2, and E3 enzymes. The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). CRLs are activated...
ORGANISM(S): Mus musculus 
2009-03-23 | E-GEOD-14088 | biostudies-arrayexpress
ProteomicsActivity-based profiling of cullin-RING ligase networks by conformation-specific probes
The cullin-RING E3 ligase (CRL) network comprises over 300 unique complexes that switch from inactive to activated conformations upon site-specific cullin modification by the ubiquitin-like protein NEDD8. Assessing cellular repertoires of activated CRL complexes is critical for understanding eukaryo...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-09-02 | PXD039649 | Pride
Ligase Cullin Nedd8 Ring Ubiquitin E3 
ProteomicsSupporting raw MS data for paper (doi:10.1038/s41589-025-01894-4) by Raiff A., Zhao Z. et al (2025), titled "TOM20-Driven E3 Ligase Recruitment Regulates Mitochondrial Dynamics Through PLD6"
Supporting raw MS data for paper (doi:10.1038/s41589-025-01894-4) by Raiff A., Zhao Z. et al (2025), titled "TOM20-Driven E3 Ligase Recruitment Regulates Mitochondrial Dynamics Through PLD6". Index of MS files and labels Supplementary Table 1 - HEK293T - Proteome (CZ-1-23 | Unimod:35; 737; 4 | 126 -...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-08-23 | MSV000095689 | MassIVE
TranscriptomicsThe Hace1 E3 Ligase Modulates the Activity of Multiple Tumor Suppressive CRL E3 Ligases by binding to CAND1
The Hace1 E3 ligase is a tumor suppressor in stressed cells. Through unknown mechanisms, Hace1 indirectly targets the cyclin D1 proto-oncogene for proteasomal degradation during nutrient depletion. We now show that Hace1 targets HIF1alpha for VHL-dependent degradation during hypoxia. To better under...
ORGANISM(S): Homo sapiens 
2011-07-01 | E-GEOD-25452 | biostudies-arrayexpress
ProteomicsARIH2 is a novel Vif-dependent regulator of CUL5-mediated APOBEC3G degradation in HIV infection
Discovery of novel host-virus interactions leads to a better understanding of mechanisms underlying infection and points to potential therapeutic targets at the interface between virus and host proteins. Recently, global, virus-host interaction networks have been mapped using affinity purification-m...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-01-29 | MSV000084855 | MassIVE
ProteomicsNoncanonical assembly, neddylation, and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex
Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, "cullin-RING" and "RBR", are individually found in several hundred E3 ligases in humans, and collaborate with E2 enzymes to catalyze ubiquitylation. However, the vertebrate-specific CUL9 complex with RBX1 (a...
ORGANISM(S): Homo sapiens (Human) 
2024-04-09 | PXD047229 | Pride
Ubiquitin Rbx1 Tp53 Apex2 Nedd8 Rbr Cullin Cul9 E3-ligase 
ProteomicsHDX-MS of CSN-CRL2 complexes - Structural basis of Cullin 2 RING E3 ligase regulation by the COP9 signalosome
Cullin-Ring E3 Ligases (CRLs) regulate a multitude of cellular pathways through specific substrate receptors. The COP9 signalosome (CSN) deactivates CRLs by removing NEDD8 (N8) from activated Cullins. The structure of stable CSN-CRL can be used to understand this mechanism of regulation. Here we pre...
ORGANISM(S): Homo sapiens (Human) 
2019-09-13 | PXD013001 | Pride
E3 ligase Structural biology Biological Conformational dynamics Protein-protein interactions Cop9 signalosome 
UnknownCullin-RING E3 ubiquitin ligase 4 regulates neurite morphogenesis during neurodevelopment.
Not available
S-EPMC10839267 | biostudies-literature
UnknownTargeting Cullin-RING E3 Ubiquitin Ligase 4 by Small Molecule Modulators.
Not available
S-EPMC8486283 | biostudies-literature
UnknownNoncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex.
Not available
S-EPMC11257990 | biostudies-literature
Sort   by:  
 Page size