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ProteomicsProteomic Profiling of cFeimin Interaction Proteins
In this study, we undertook a comprehensive characterization of proteins interacting with cFeimin. Through rigorous analysis of mass spectrometry data, we discerned candidates for potential interaction partners of cFeimin. Notably, the protein Foxc2 emerged with heightened possibilities of being a b...
ORGANISM(S): Homo sapiens (Human) 
2024-10-10 | PXD045263 | Pride
Human Foxc2 Cfeimin Hskmc 
ProteomicsIdentification of cFeimin-interacting proteins in brown adipocytes
This project aims to identify proteins that interact with cFeimin in brown adipocytes. Cells were infected with cFeimin–3×FLAG adenovirus or control virus at differentiation onset. Following 4 days of differentiation, adipocytes were treated with ISO and A769662 for 12 hours to stimulate signaling p...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-02 | PXD070046 | Pride
Brown adipocytes Cfeimin Immunoprecipitation 
ProteomicsIdentification of phosphorylation sites in cFeimin
Our investigation encompassed a comprehensive profiling of phosphorylation sites within the cFeimin protein. Notably, the acquired mass spectrometry data pinpointed a specific phosphorylation site, Threonine 128, demonstrating distinct associations with AMPK-mediated phosphorylation processes. This ...
ORGANISM(S): Mus musculus (Mouse) 
2024-10-10 | PXD045323 | Pride
Cfeimin Mouse Phosphorylation 
GenomicsMus musculus strain:C57BL/6
Transcriptomic profiling of skeletal muscle in cFeimin MKO mice during exercise
PRJNA916296 | ENA
TranscriptomicsCellular Feimin enhances exercise performance by suppressing muscle thermogenesis
Exercise can rapidly increase core body temperature, and research has indicated that elevated internal body temperature can independently contribute to fatigue during physical activity. However, the precise mechanisms responsible for regulating thermogenesis in muscles during exercise have remained ...
ORGANISM(S): Mus musculus 
2024-11-01 | GSE280845 | GEO
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