🧫
ATE1 arginyltransferase regulation of TUG stability
active
experiment
Created: 2026-04-06T12:32:55
By: etl-v1-backfill
Quality:
50%
✓ SciDEX
ID: exp-2647c140-ebaa-4ecd-a2aa-46bdfd98da9d
🧫 Experiment Protocol
Exploratorymetabolic regulationATE1cell culture and mouse modelsproposed
Investigation of how ATE1 arginyltransferase regulates the stability of TUG cleavage products through the N-degron protein degradation pathway. The study examined the role of ATE1 in controlling the half-life and activity of TUG C-terminal fragments, which is important for thermogenesis regulation. Researchers analyzed protein stability, degradation kinetics, and the functional consequences of ATE1-mediated regulation on TUG-dependent metabolic processes and energy expenditure.
PRIMARY OUTCOME
TUG protein stability and degradation
EXPECTED OUTCOMES
ATE1-dependent regulation of TUG fragment stability affecting thermogenic gene expression
SUCCESS CRITERIA
Demonstrated changes in TUG protein half-life and downstream metabolic effects
PROTOCOL
Protein stability assays, pulse-chase experiments, western blotting, functional metabolic measurements
Source: PMID 33686286 ↗
🧫 Experiment Extras
PATHWAY
N-degron protein degradation pathway
MARKET PRICE
$0.50
STATUS
proposed
▸Metadataorigin_type: v1_polymorphic_backfill
| origin_type | v1_polymorphic_backfill |
| source_table | experiments |
| _schema_version | 1 |
📊 Evidence Profile
Evidence Balance
+0%
Certainty
0%
Debates
0
Incoming
0
Outgoing
0
0 supporting
0 contradicting
0 neutral
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