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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
ProteomicsUbiquitin Proteomics Analysis of Systemic Sclerosis Lung Fibroblasts with or without KLHL42 knockdown
Systemic scleroderma (SSc) is an autoimmune disease which results in fibrotic production in the lung. Resultant SSC-pulmonary fibrosis is the main cause of mortality among SSc patients. From high throughput RNAi screening, we uncovered the ubiquitin E3 ligase KLHL42 as a potential pro-fibrotic media...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-01-14 | MSV000084800 | MassIVE
TranscriptomicsMerlin/NF2 Suppresses Tumorigenesis by Inhibiting the E3 Ubiquitin Ligase CRL4DCAF1 in the Nucleus
Current models imply that the FERM domain protein Merlin, encoded by the tumor suppressor NF2, inhibits mitogenic signaling at or near the plasma membrane. Here, we show that the closed, growth inhibitory form of Merlin accumulates in the nucleus, binds to the E3 ubiquitin ligase CRL4DCAF1, and supp...
ORGANISM(S): Mus musculus 
2010-03-09 | E-GEOD-19305 | biostudies-arrayexpress
GenomicsCombinatorial mapping of E3 ubiquitin ligases to their target substrates
Combinatorial mapping of E3 ubiquitin ligases to their target substrates
PRJNA982147 | ENA
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
GenomicsSIAH ubiquitin E3 ligases as modulators of inflammatory gene expression
SIAH ubiquitin E3 ligases as modulators of inflammatory gene expression
PRJNA742677 | ENA
GenomicsRepurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
Repurposing E3 ubiquitin ligases as cell surface protein degraders using Proteolysis Targeting Antibodies
PRJNA859706 | ENA
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 
TranscriptomicsExpression Profile Of A Caenorhabditis Elegans Model Of Adult Onset Neuronal Ceroid Lipofuscinosis Reveals Down Regulation Of Ubiquitin E3 Ligase Components.
Transcriptional profiling of two C. elegans mutants of dnj-14, the worm homolog of cysteine string protein (CSP), compared to two control strains N2 (Bristol) and CZ1200. CSP is a neuroprotective protein and the C. elegans mutants, tm3223 and ok237, are used to model the neurodegenerative disease, a...
ORGANISM(S): Caenorhabditis elegans 
2015-12-04 | E-MTAB-3147 | biostudies-arrayexpress
ProteomicsUFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER
Supporting MS data for paper (doi: 10.1038/s41586-024-07073-0) by DaRosa P.A., Penchev I. et al., titled "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER". Index of MS supporting files uploaded: Related to Related to Fig. 1b, c (xb01004(UFM1), xb01005(SBP-UFM1): LFQ IP-MS (Un...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-12-22 | MSV000093721 | MassIVE
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