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ProteomicsPull-Down of UCHL1 from living cells with small molecule probes GK13S, GK13R, and GK16S (1 uM)
UCHL1 was enriched from HEK293 cells (Homo Sapiens) using a probe (PullDown via NeutrAvidin beads). Protein enrichment as a function of substance addition was studied in comparison to a DMSO control.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-08-01 | MSV000090045 | MassIVE
UnknownRetinoic acid regulates the ubiquitin-proteasome system in a middle cerebral artery occlusion animal model.
Not available
S-EPMC9102573 | biostudies-literature
UnknownThe ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila.
Not available
S-EPMC10713573 | biostudies-literature
ProteomicsUbiquitin Thioesterase OTUB2 is An Endoplasmic Reticulum Stress-associated β Cell Autoantigen Targeted by CD8+ T cells in Type 1 Diabetes
Autoreactive CD8+ T cell plays a key role in the pathogenesis of Type 1 diabetes (T1D), but the antigen spectrum that activate autoreactive CD8+ T cells is still not completely clear. Endoplasmic reticulum stress（ERS）has been implicated in the generation of β cell autoantigens and the enhanced immun...
ORGANISM(S): Mus musculus (Mouse) 
2024-05-24 | PXD041227 | Pride
Otub2 Endoplasmic reticulum stress Type 1 diabetes Cd8+ t-cell. 
ProteomicsThe deubiquitinase TRABID stabilises the K29/K48-specific E3 ubiquitin ligase HECTD1
The OTU deubiquitinase TRABID is highly tuned for the recognition and cleavage of K29 and K33-linked ubiquitin chains. Yet the cellular functions of these atypical ubiquitin signals remain unclear. Here, we compared the interactome of two different catalytically-dead TRABID constructs, one that lack...
ORGANISM(S): Homo sapiens (Human) 
2021-06-23 | PXD022703 | Pride
Ubiquitin K29/k48-linked polyubiquitin chain Ubiquitin thioesterase E3 ubiquitin ligase Deubiquitination Trabid Hectd1 Lc-ms/ms Polyubiquitin chain Protein degradation 
ProteomicsCellular Validation of Chemically Improved Inhibitor Identifies Monoubiquitination on OTUB2
Ubiquitin thioesterase OTUB2, a cysteine protease from the ovarian tumor (OTU) deubiquitinase superfamily, is associated with enhanced expression during tumor progression and metastasis. Development of OTUB2 inhibitors is therefore believed to be therapeutically important, yet potent and selective s...
ORGANISM(S): Homo sapiens (Human) 
2023-06-27 | PXD041346 | Pride
Otub2 Small-molecule inhibitor Monoubiquitination 
UnknownIdentification of differentially expressed genes in human mesenchymal stem cell-derived neurons.
Not available
S-EPMC3834464 | biostudies-literature
UnknownCellular Validation of a Chemically Improved Inhibitor Identifies Monoubiquitination on OTUB2.
Not available
S-EPMC10510154 | biostudies-literature
ProteomicsOpen-source electrophilic fragment screening platform for UCHL1 covalent inhibitors
Data in support of the manuscript "Open-source electrophilic fragment screening platform for UCHL1 covalent inhibitors"
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-12-06 | MSV000096608 | MassIVE
UnknownInteractome and Ubiquitinome Analyses Identify Functional Targets of Herpes Simplex Virus 1 Infected Cell Protein 0.
Not available
S-EPMC9062659 | biostudies-literature
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