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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
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 
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
ProteomicsCharacterisation of cullin E3 ubiquitin ligases in trypanosomes
Trypanosomes have seven cullin paralogs, the majority lineage-specific. Six of those cullins (TbCul-A, TbCul-C, TbCul-D TbCul-E, TbCul-F and TbCul-G) were endogenously 3xHA-epitope tagged at the C-terminus. We used affinity capture/mass spectrometry to determine the composition of these cullin compl...
ORGANISM(S): Trypanosoma brucei 
2024-03-25 | PXD042022 | Pride
Cullin Evolution Affinity isolation Protein turnover Ubiquitin Cryomilling E3 ligase 
TranscriptomicsThe tumor antigen PRAME is a substrate recognition subunit of a Cul2-based ubiquitin ligase and is associated with active NFY promoters
The human tumor antigen PRAME (Preferentially expressed antigen of melanoma) is frequently overexpressed in tumors. High PRAME levels correlate with poor clinical outcome of several cancers, but the mechanisms by which PRAME could be involved in tumorigenesis remain largely elusive. We applied prote...
ORGANISM(S): Homo sapiens 
2011-07-29 | E-GEOD-26439 | biostudies-arrayexpress
UnknownCullin E3 Ligase Activity Is Required for Myoblast Differentiation.
Not available
S-EPMC5395100 | biostudies-literature
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
GenomicsThe E3 ubiquitin ligase mechanism specifying targeted microRNA degradation
The E3 ubiquitin ligase mechanism specifying targeted microRNA degradation
PRJNA1294290 | ENA
UnknownExploiting the Cullin E3 Ligase Adaptor Protein SKP1 for Targeted Protein Degradation.
Not available
S-EPMC10614948 | biostudies-literature
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