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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
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
ProteomicsBioE3 enables the identification of bona fide targets of E3 ligases
The post-translational modification of proteins by ubiquitination is a highly regulated process that involves a dynamic, three-step enzymatic cascade, where more than 600 E3 ligases play a critical role in recognizing specific substrates for modification. Separating bona fide targets of E3s from E3-...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD041685 | Pride
E3-ligases Bioe3 Ubiquitination Proteomics 
ProteomicsZNRF3 and RNF43 are active monomeric E3 ligases that self-associate
Crosslinking mass spectrometry was used to identify the site of dimerization in the RING domain of ZNRF3. The two proteins, ZNRF3 and RNF43 have a key role in regulating the number of Frizzled (FZD) receptor on cells and their inactivation causes cancer. This is because they are RING E3 ligases that...
ORGANISM(S): Homo sapiens (Human) 
2026-07-30 | PXD070424 | Pride
Znrf3 e3 ligase Cross-linking Ring dimerization 
UnknownCullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.
Not available
S-EPMC7205596 | biostudies-literature
ProteomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
The majority of current therapeutics targeting plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. Typical mammalian proteins, however, consist of multiple domains executing discrete but coordinated activities, and saturating inhibition of one functional domain...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-25 | MSV000089542 | MassIVE
UnknownRING-Between-RING E3 Ligases: Emerging Themes amid the Variations.
Not available
S-EPMC5675740 | biostudies-literature
UnknownNEDD8 and ubiquitin ligation by cullin-RING E3 ligases.
Not available
S-EPMC8096640 | biostudies-literature
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 
ProteomicsPhotocrosslinking Activity-Based Probes to Capture the Dynamics of Ubiquitin RING E3 Ligase Interactions
Almost all cellular processes are influenced by ubiquitination. A large family of enzymes known as E3 ligases provide the specificity for ubiquitination, with the largest class among them, the RING E3s, comprising over 600 members in humans. RING E3s facilitate transfer of ubiquitin to substrates by...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD075613 | Pride
Ubiquitin n-maleimido-diazirine e3 ligase activity-based probe 
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