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GenomicsEffect of Fnip2 genetic variant in mouse tissues
Effect of Fnip2 genetic variant in mouse tissues
PRJNA825543 | ENA
UnknownWhole Transcriptome Analysis Reveals a Potential Regulatory Mechanism of LncRNA-FNIP2/miR-24-3p/FNIP2 Axis in Chicken Adipogenesis.
Not available
S-EPMC8265275 | biostudies-literature
TranscriptomicsEffect of Fnip2 genetic variant in mouse tissues
We have modeled the Fnip2 rs2291007 genetic variant in the mouse genome. In this study we aimed to investigate the effect of this genetic variant in the transcriptome of two metabolically relevant tissues: liver and white adipose tissue (WAT)
ORGANISM(S): Mus musculus 
2022-10-19 | GSE200620 | GEO
UnknownCryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex.
Not available
S-EPMC7008705 | biostudies-literature
UnknownFolliculin-interacting protein FNIP2 impacts on overweight and obesity through a polymorphism in a conserved 3' untranslated region.
Not available
S-EPMC9620695 | biostudies-literature
UnknownDirect regulation of FNIP1 and FNIP2 by MEF2 sustains MTORC1 activation and tumor progression in pancreatic cancer.
Not available
S-EPMC10936626 | biostudies-literature
TranscriptomicsAn mTORC1-mediated negative feedback loop constrains amino acid-induced FLCN-Rag activation downstream of TSC2 loss
The mechanistic target of rapamycin complex 1 (mTORC1) integrates inputs from growth factors and nutrients, but how mTORC1 autoregulates its activity remains unclear. The MiT/TFE transcription factors are phosphorylated and inactivated by mTORC1 following lysosomal recruitment by RagC/D GTPases in r...
ORGANISM(S): Homo sapiens 
2022-11-01 | GSE216545 | GEO
GenomicsFolliculin-interacting protein FNIP2 impacts on overweight and obesity through a polymorphism in a conserved 3’ untranslated region (SNP array)
Folliculin-interacting protein FNIP2 impacts on overweight and obesity through a polymorphism in a conserved 3’ untranslated region (SNP array)
PRJNA889010 | ENA
ProteomicsA specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand
Heat shock protein-90 chaperone machinery is involved in the stability and activity of its client proteins. The chaperone function of Hsp90 is regulated by co-chaperones and post-translational modifications. Although structural evidence exists for Hsp90 interaction with clients, our understanding of...
ORGANISM(S): Homo sapiens (Human) 
2023-05-30 | PXD030486 | Pride
Hsp90 Co-chaperone Chaperone Glucocorticoid receptor Tsc1 Fnip1 Fnip2 Steroid hormone receptors 
UnknownNutrient-induced FNIP degradation by SCFβ-TRCP regulates FLCN complex localization and promotes renal cancer progression.
Not available
S-EPMC5354783 | biostudies-literature
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