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Human 6-phosphofructo-2-Kinase/fructose-2,6-Biphosphatase 3 (PFKFB3) interaction partners

1. data suggesting that p53 (show TP53 Proteins) promotes nucleotide biosynthesis in response to DNA damage by repressing the expression of the phosphofructokinase-2 (PFK2) isoform 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 (PFKFB3), a rate-limiting enzyme that promotes glycolysis.

2. Study provides evidence that PFKFB3 overexpression occupied a dominant position in sorafenib resistance of hepatocellular carcinoma cells.

3. This work has uncovered a novel function of the enzymes PFKFB3 and PFKFB4 (show PFKFB4 Proteins) in ovarian cancer cells during mitotic arrest

4. PFK-2 seems to be a strategic element that links NADPH oxidase (show NOX1 Proteins) activation and glycolysis modulation, and, as such, is proposed as a potential therapeutic target in inflammatory diseases.

5. Data suggest that hepatic glucokinase (show GCK Proteins) activity is regulated by reversible binding to specific inhibitor protein glucokinase regulatory protein (GKRP (show GCKR Proteins)) and by binding to activator proteins such as 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK2/FBP2 (show KHSRP Proteins)); changes in glucokinase (show GCK Proteins) expression and activity are associated with poorly controlled type 2 diabetes and nonalcoholic fatty liver disease. [REVIEW]

6. PFKFB3 was a novel downstream substrate of mTOR (show FRAP1 Proteins) signaling pathway as PFKFB3 level was augmented after knocking down TSC2 in THP1 and OCI-AML3 (show RUNX2 Proteins) acute myeloid leukemia (show BCL11A Proteins) cells.

7. Taken together, our study identifies PFKFB3 as a key TGFbeta1 (show TGFB1 Proteins) effector protein that mediates TGFbeta1 (show TGFB1 Proteins)'s effect on Snail (show SNAI1 Proteins) expression, invasion, and glycolysis.

8. we investigate the crosstalk between PFKFB3 and TIGAR (TP53-Induced Glycolysis and Apoptosis Regulator), a protein known to protect cells from oxidative stress. Our results show consistent TIGAR induction in HeLa cells in response to PFKFB3 knockdown

9. Knockdown of PFKFB3 by siRNAs significantly inhibited the proliferation and migration abilities of gastric cancer cells. Our data suggest that PFKFB3 might be a potential biomarker for gastric cancer and anti-neoplastic targeting gene.

10. The targeting of MCT1 (show CMA1 Proteins) and PFKFB3 regulated cell proliferation.

Mouse (Murine) 6-phosphofructo-2-Kinase/fructose-2,6-Biphosphatase 3 (PFKFB3) interaction partners

1. HG significantly increased PFKFB3 promoter transcription activity compared with LG.

2. The PFKFB3-driven glycolysis selectively promotes the extrinsic antiviral capacity of macrophages, via metabolically supporting the engulfment and removal of virus-infected cells.

3. Blockage of glycolysis by targeting PFKFB3 alleviates sepsis-related acute lung injury via suppressing inflammation and apoptosis of alveolar epithelial cells.

4. overexpression of PFKFB3 in HEK293 cells potentiated insulin (show INS Proteins)-dependent phosphorylation of Akt (show AKT1 Proteins) and Akt (show AKT1 Proteins) substrates

5. Data show that inhibition of AMP (show TMPRSS5 Proteins)-Activated kinase (AMPK (show PRKAA1 Proteins)) or 6-phosphofructo-2-kinase-fructose-2,6-biphosphatase 3 (PFKFB3) results in enhanced cell death in mitosis.

6. Shear stress-mediated repression of endothelial cell metabolism via KLF2 (show KLF2 Proteins) and PFKFB3 controls endothelial cell phenotype.

7. PFKFB3 is a promising target for the reduction of endothelial glycolysis and its related pathological angiogenesis

8. PFKFB3/iPFK2 responds to re-feeding, which in turn stimulates hypothalamic glycolysis and decreases hypothalamic AMPK (show PRKAA1 Proteins) phosphorylation and alters neuropeptide expression in a pattern that is associated with suppression of food intake.

9. High-fat diet feeding stimulates intestine 6-phosphofructo-2-kinase expression and induces intestine inflammatory response.

10. Study showed that endothelial cells (ECs)relied on glycolysis rather than on oxidative phosphorylation for ATP production and that loss of the glycolytic activator PFKFB3 in ECs impaired vessel formation.

Zebrafish 6-phosphofructo-2-Kinase/fructose-2,6-Biphosphatase 3 (PFKFB3) interaction partners

1. Study showed that endothelial cells (ECs)relied on glycolysis rather than on oxidative phosphorylation for ATP production and that loss of the glycolytic activator PFKFB3 in ECs impaired vessel formation.