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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
additional information
?
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
bifunctional enzyme catalyzes the forward and reverse reaction using different catalytic sites
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
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-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli, role in the progression of cancerous cells, antiproliferative effects during inhibitor incubation determined
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46)
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?
additional information
?
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the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
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?
additional information
?
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-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
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?
additional information
?
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PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
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?
additional information
?
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the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
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?
additional information
?
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expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
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?
additional information
?
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expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
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?
additional information
?
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expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
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?
additional information
?
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expression analysis in different tumor specimens with high and low malignity grades, high expression of the PFKFB3 protein as an explanation for high glycolytic flux and lactate production in these tumors
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?
additional information
?
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recombinant human PFKFB4 kinase activity is 4.3-fold greater than its phosphatase activity
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ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
additional information
?
-
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 plays a crucial role in the progression of cancerous cells by enabling their glycolytic pathways even under severe hypoxic conditions
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
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-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
-
-
r
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
-
regulation of glycolysis
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?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
the inducible enzyme is an important regulator of glycolysis that may be responsible for sustaining the high glycolytic flux of rapidly proliferating leukemia cells
-
?
ATP + beta-D-fructose 6-phosphate
ADP + beta-D-fructose 2,6-bisphosphate
PFKFB3 is a potent stimulator of glycolysis, up-regulated by inflammatory and hypoxic stimuli
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes the synthesis, 6-phosphofructo-2-kinase, and hydrolysis, fructose-2,6-bisphosphatase, of beta-D-fructose 2,6-bisphosphate, an activator of glycolysis and an inhibitor of gluconeogenesis
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-
?
additional information
?
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-
it is unlikely that protein kinase Czeta is required for activation of 6-phosphofructo-2-kinase by insulin in heart
-
-
?
additional information
?
-
-
PFKFB3 is activated by mitogenic inflammatory and hypoxic stimuli. PFKFB4 controls glycolytic flux to lactate and the nonoxidatibe pentose shunt, and is selectively required for the tumorigenic growth of ras-transformed cells
-
-
?
additional information
?
-
-
the expression of the inducible PFK2/FBPase is selectively necessary for the control of glycolytic flux in cells transformed with ras
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?
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3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
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(2E)-1-(pyridin-4-yl)-3-(quinolin-2-yl)prop-2-en-1-one
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(2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one
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1-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
-
2-(2-bromoacetamido)ethyl phosphate
an irreversible inhibitor of PFK-2 in several cancer cell lines
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
-
2-hydroxy-4-[(naphthalen-1-ylsulfonyl)amino]benzoic acid
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
3H-benzo[e]indol-2-yl(pyridin-4-yl)methanone
-
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
-
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
-
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
-
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
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5,6,7,8-tetrahydroxy-2-(4-hydroxyphenyl)-4H-chromen-4-one
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5,6,7,8-tetrahydroxy-2-(4-hydroxyphenyl)chromen-4-one
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-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
-
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
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5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
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5-(N-(8-methoxy-4-quinolyl)amino)pentyl nitrate
-
-
7,8-dihydroxy-3-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
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-
7,8-dihydroxy-3-(4-hydroxyphenyl)-4H-chromen-4-one
-
AZ67
potent and specific PFKFB3 inhibitor
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beta-D-fructose 6-phosphate
modeling of beta-D-fructose 6-phosphate as inhibitor
ethyl 1-(6-oxo-1-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)-1,6-dihydropyridazin-4-yl)-1H-1,2,3-triazole-4-carboxylate
-
ethyl 7-hydroxy-2-oxo-2H-1-benzopyran-3-carboxylate
-
-
N-bromoacetylethanolamine phosphate
-
PFK-15
i.e. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
PFK-158
potent and specific inhibitor
-
phosphoenolpyruvate
HBP1 and HBP2, the bifunctional enzyme is regulated via inhibition by phosphoenolpyruvate, uncompetitive against ATP, noncompetitive against beta-D-fructose 6-phosphate
1-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
1-(3-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
-
1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one
the inhibitor causes a rapid induction of apoptosis in transformed cells, has adequate pharmacokinetic properties, suppresses the glucose uptake and growth of Lewis lung carcinomas in syngeneic mice and yields anti-tumor effects in three human xenograft models of cancer in athymic mice that are comparable to FDA-approved chemotherapeutic agents
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
-
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
(3PO), small-molecule inhibitor, mixed inhibition mechanism, both competitive and uncompetitive inhibition, suppresses glycolytic flux and is cytostatic to neoplastic cells, inhibits activity of recombinantly expressed PFKFB3
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
3PO, a weak competitive inhibitor of PFKFB3, reduces the glucose metabolism and proliferation of cancer cells
3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
the PFKFB3 inhibitor, 3PO, increases p27 protein in Lewis lung carcinoma cells in vitro and in vivo
additional information
phosphorylation site: Ser-32
-
additional information
enzyme structure-activity relationships, screening of a small-molecule library, and design and synthesis of 5-triazolo-2-arylpyridazinone analogus inhibitors, molecular docking using the X-ray structure for human PFKFB3, PDB ID 2AXN, overview
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additional information
synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
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additional information
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synthesis and screening of 3PO inhibitor derivatives for inhibitory potency against isozyme PFKFB3, overview. 1-(4-pyridinyl)-3-(2-quinolinyl)-2-propen-1-one displays improved pharmacokinetic properties relative to 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
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additional information
not inhibited by up to 0.75 mM 3-(3-pyridinyl)-1-(4-pyridinyl)-2-propen-1-one
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Anemia
Erythrocyte fructose 2,6-bisphosphate content in congenital hemolytic anemias.
Aortic Valve Stenosis
Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes.
Arthritis, Rheumatoid
Inhibition of 6-phosphofructo-2-kinase suppresses fibroblast-like synoviocytes-mediated synovial inflammation and joint destruction in rheumatoid arthritis.
Breast Neoplasms
Inhibition of 6-phosphofructo-2-kinase (PFKFB3) suppresses glucose metabolism and the growth of HER2+ breast cancer.
Breast Neoplasms
Overexpression of miR-206 suppresses glycolysis, proliferation and migration in breast cancer cells via PFKFB3 targeting.
Carcinogenesis
PFKFB3 Control of Cancer Growth by Responding to Circadian Clock Outputs.
Carcinoma
Wortmannin influences hypoxia-inducible factor-1 alpha expression and glycolysis in esophageal carcinoma cells.
Carcinoma, Hepatocellular
Characterization of the binding sites for [3H]glibenclamide in rat liver membranes.
Carcinoma, Hepatocellular
Glucose response elements in a gene that codes for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
Carcinoma, Hepatocellular
Rat hepatoma (HTC) cell 6-phosphofructo-2-kinase differs from that in liver and can be separated from fructose-2,6-bisphosphatase.
Colonic Neoplasms
Phosphofructokinase 2 and glycolysis in HT29 human colon adenocarcinoma cell line. Regulation by insulin and phorbol esters.
Coma
Fructose 2,6-bisphosphate in hypoglycemic rat brain.
Heart Failure
Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes.
Infections
Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses.
Insulin Resistance
Adipocyte inducible 6-phosphofructo-2-kinase suppresses adipose tissue inflammation and promotes macrophage anti-inflammatory activation.
Insulin Resistance
Disruption of inducible 6-phosphofructo-2-kinase ameliorates diet-induced adiposity but exacerbates systemic insulin resistance and adipose tissue inflammatory response.
Insulin Resistance
Targeted overexpression of inducible 6-phosphofructo-2-kinase in adipose tissue increases fat deposition but protects against diet-induced insulin resistance and inflammatory responses.
Myocardial Ischemia
[Effect of electroacupuncture preconditioning of "Neiguan"(PC6) on myocardial LKB1/AMPK/PFK2 pathway in myocardial ischemia rats].
Neoplasms
A Glycolysis Outsider Steps into the Cancer Spotlight.
Neoplasms
Activation of p53 mediated glycolytic inhibition-oxidative stress-apoptosis pathway in Dalton's lymphoma by a ruthenium (II)-complex containing 4-carboxy N-ethylbenzamide.
Neoplasms
An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect.
Neoplasms
GM-CSF Enhances Macrophage Glycolytic Activity In Vitro and Improves Detection of Inflammation In Vivo.
Neoplasms
Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues.
Neoplasms
PFKFB3 Control of Cancer Growth by Responding to Circadian Clock Outputs.
Neoplasms
PFKFB3 gene silencing decreases glycolysis, induces cell-cycle delay and inhibits anchorage-independent growth in HeLa cells.
Neoplasms
Small-molecule inhibition of 6-phosphofructo-2-kinase activity suppresses glycolytic flux and tumor growth.
Neoplasms
Targeted disruption of inducible 6-phosphofructo-2-kinase results in embryonic lethality.
Neoplasms
Targeting 6-phosphofructo-2-kinase (PFKFB3) as a therapeutic strategy against cancer.
Neoplasms
Targeting the sugar metabolism of tumors with a first-in-class 6-phosphofructo-2-kinase (PFKFB4) inhibitor.
Neoplasms
The role of 6-phosphofructo-2-kinase (PFK-2)/fructose 2,6-bisphosphatase (FBPase-2) in metabolic reprogramming of cancer cells.
Neoplasms
Upregulation of 6-phosphofructo-2-kinase (PFKFB3) by hyperactivated mammalian target of rapamycin complex 1 is critical for tumor growth in tuberous sclerosis complex.
pyruvate kinase deficiency
Erythrocyte fructose 2,6-bisphosphate content in congenital hemolytic anemias.
Sarcoma, Avian
Expression of the v-src or v-fps oncogene increases fructose 2,6-bisphosphate in chick-embryo fibroblasts. Novel mechanism for the stimulation of glycolysis by retroviruses.
Sepsis
Hepatic phosphofructokinase-1 activity and fructose 2,6-bisphosphate levels in patients with abdominal sepsis.
Starvation
Changes in rat hepatic fructose 2,6-bisphosphate and 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase activity during three days of consumption of a high protein diet or starvation.
Starvation
Molecular cloning of a cDNA encoding 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from liver of Sparus aurata: nutritional regulation of enzyme expression.
Starvation
Starvation or diabetes decreases the content but not the mRNA of 6-phosphofructo-2-kinase in rat liver.
Tuberous Sclerosis
Upregulation of 6-phosphofructo-2-kinase (PFKFB3) by hyperactivated mammalian target of rapamycin complex 1 is critical for tumor growth in tuberous sclerosis complex.
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0.026
(2E)-3-(pyridin-3-yl)-1-(pyridin-4-yl)prop-2-en-1-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
2-((5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)amino)acetamide
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
2-(5-bromo-6-oxo-1-phenyl-1,6-dihydropyridazin-4-yl)-1,2,3,4-tetrahydroisoquinoline-5-carbonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.027
2-hydroxy-4-[(naphthalen-1-ylsulfonyl)amino]benzoic acid
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
3H-benzo[e]indol-2-yl(pyridin-4-yl)methanone
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0084
4-(4-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-5-bromo-6-oxopyridazin-1(6H)-yl)benzonitrile
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(((tetrahydrofuran-2-yl)methyl)amino)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-2-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)pyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
1
4-bromo-5-morpholino-2-phenylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0034
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzyl-4-bromopyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
10
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-2-benzylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.011
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(3-phenylpropyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-((2-(dimethylamino)ethyl)-amino)benzyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0091
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-(trifluoromethoxy)phenyl)-pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.007
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-chlorophenyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0087
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(4-iodobenzyl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0096
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-(pyrimidin-5-yl)pyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0026
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenethylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.0074
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-bromo-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.026
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-chloro-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
1
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-ethoxy-2-phenylpyridazin-3(2H)-one
Homo sapiens
above, pH 7.5, 30°C, recombinant GST-tagged enzyme
0.013
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-iodo-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.5
5-(4-acetyl-5-methyl-1H-1,2,3-triazol-1-yl)-4-isopropyl-2-phenylpyridazin-3(2H)-one
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
0.055
ethyl 1-(6-oxo-1-phenyl-5-(2-oxa-6-azaspiro[3.3]heptan-6-yl)-1,6-dihydropyridazin-4-yl)-1H-1,2,3-triazole-4-carboxylate
Homo sapiens
pH 7.5, 30°C, recombinant GST-tagged enzyme
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physiological function
role of PFKFB proteins in the control of cancer metabolism. Liver, muscle and fetal isoform variants of PFKFB1 (L-PFK2, M-PFK2 and F-PFK2 respectively) are transcribed from the same gene, but only L-PFK2 contains a serine residue in position 32 of its C-terminal regulatory domain. This is consistent with its specific physiological role as liver cells need to modulate Fru-2,6-P2 levels to facilitate the production of glucose to fulfill the metabolic demand of other tissues. Response to glucagon, cyclic AMP-dependent protein kinase (PKA) phosphorylates Ser32 in the liver isoform of PFKFB1, leads to inactivation of its PFK-2 activity while activating its FBPase-2 function. This decreases glycolytic flux while increasing gluconeogenesis in liver cells While phosphorylation of L-PFK2 results in a decrease in its kinase activity, phosphorylation of H-PFK2 results in an increase in this activity
metabolism
expression level of some PFKFB and PFK1 genes in normoxic and hypoxic conditions in glioma cells is mediated by ERN1 signaling system of endoplasmic reticulum stress. Effect of hypoxia on the expression of genes encoded different 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3 and PFKFB4) and 6-phosphofructo-1-kinase (PFKL, PFKM and PFKP) as well as lactate dehydrogenase in glioma U-87 cells and its subline with suppressed function of ERN1 signaling enzyme, overview
metabolism
fructose 2,6-bisphosphate is an important metabolite for the dynamic regulation of glycolytic flux by allosterically activating the rate-limiting enzyme of glycolysis phosphofructokinase-1, fructose 2,6-bisphosphate is a powerful allosteric activator of phosphofructokinase 1, PFK-1
malfunction
PFKFB3 enzymes are activated in human cancers
malfunction
Akt inactivation blocks PFKFB2 phosphorylation and fructose 2,6-bisphosphate production
malfunction
knockdown of PFKFB4 in prostate cancer cells increases p62 and reactive oxygen species, but surprisingly increases autophagic flux. Addition of the reactive oxygen species scavenger N-acetyl cysteine prevents p62 accumulation in PFKFB4-depleted cells. PFKFB4 depletion acts upstream of ATG7 consistent with increased oxidative stress that induces autophagy and p62 upregulation
malfunction
PFKFB4 inhibition in H-460 cells reduces glycolytic flux to lactate and glutamate. PFKFB4 inhibition in H-460 cells increases apoptosis under normoxic and hypoxic conditions
malfunction
silencing of PFKFB4 results in increased levels of Fru-2,6-P2 in prostate cancer cells, knockdown of PFKFB4 blocks prostate cancer cell growth and remarkably induced regression of prostate tumor xenografts
malfunction
siRNA silencing of endogenous PFKFB3 inhibits Cdk1 activity, which in turn stabilizes p27 protein levels causing cell cycle arrest at G1/S and increased apoptosis in HeLa cells. PFKFB3 inhibition completely suppresses cell proliferation and results in increased early and late apoptotic cells. PFKFB3 inhibition results in increased nuclear and cytoplasmic p27 protein but has no effect on p57 or p21. Blockade of cell cycle progression and stimulation of apoptosis by PFKFB3 inhibition is mediated by p27
malfunction
enzyme knockdown inhibits clonogenic growth and enhances paclitaxel sensitivity in ovarian and breast cancer cell lines with wild type TP53
metabolism
cancer cells use control of PFKFB3 of the important glycolytic pathway to generate ATP
metabolism
expression level of some PFKFB and PFK1 genes in normoxic and hypoxic conditions in glioma cells is mediated by ERN1 signaling system of endoplasmic reticulum stress. Effect of hypoxia on the expression of genes encoded different 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3 and PFKFB4) and 6-phosphofructo-1-kinase (PFKL, PFKM and PFKP) as well as lactate dehydrogenase in glioma U-87 cells and its subline with suppressed function of ERN1 signaling enzyme, overview
metabolism
expression level of some PFKFB and PFK1 genes in normoxic and hypoxic conditions in glioma cells is mediated by ERN1 signaling system of endoplasmic reticulum stress. Effect of hypoxia on the expression of genes encoded different 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3 and PFKFB4) and 6-phosphofructo-1-kinase (PFKL, PFKM and PFKP) as well as lactate dehydrogenase in glioma U-87 cells and its subline with suppressed function of ERN1 signaling enzyme, overview. Increased expression of PFKFB3 and PFKFB4 under hypoxic conditions correlates with strong induction of PFKL expression in control glioma cells only
metabolism
fructose 2,6-bisphosphate is an important metabolite for the dynamic regulation of glycolytic flux by allosterically activating the rate-limiting enzyme of glycolysis phosphofructokinase-1, fructose 2,6-bisphosphate is a powerful allosteric activator of phosphofructokinase 1, PFK-1
metabolism
the family of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFB1-4) comprises well established regulators of glucose metabolism via their synthesis of fructose-2,6 bisphosphate, a potent allosteric activator of 6-phosphofructo-1-kinase. But PFKFB3 and fructose-2,6 bisphosphate function not only as regulators of Pfk-1 but also of Cdk1 activity, and therefore serve to couple glucose metabolism with cell proliferation and survival in transformed cells
metabolism
upregulation of p62 and autophagy is a response to oxidative stress caused by PFKFB4. PFKFB4 is an autophagy regulator
metabolism
enzyme PFKFB3 is an essential target of epidermal growth factor receptor signaling. PFKFB3 activation is required for glycolysis stimulation upon epidermal growth factor receptor activation. PFKFB3 has a key role in mediating glucose metabolism and survival of NSCLC cells in response to epidermal growth factor receptor signaling
metabolism
PFKFB3 has the highest kinase:phosphatase ratio (710:1) to shunt glucose toward glycolysis, whereas PFKFB4 has more fructose-2,6-bisphosphatase-2 activity (kinase:phosphatase ratio of 4.6:1), redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species. Co-expression of PFKFB3 and PFKFB4 provides sufficient glucose metabolism to satisfy the bioenergetics demand and redox homeostasis requirements of cancer cells
metabolism
PFKFB3 has the highest kinase:phosphatase ratio (710:1) to shunt glucose toward glycolysis, whereas PFKFB4 has more fructose-2,6-bisphosphatase-2 activity (kinase:phosphatase ratio of 4.6:1), redirecting glucose toward the pentose phosphate pathway, providing reducing power for lipid biosynthesis and scavenging reactive oxygen species. Co-expression of PFKFB3 and PFKFB4 provides sufficient glucose metabolism to satisfy the bioenergetics demand and redox homeostasis requirements of cancer cells. PFKFB4 acts as a protein kinase, regulates steroid receptor coactivator-3 activity and is involved in transcriptional regulation
metabolism
the enzyme binds and activates glucokinase
physiological function
PFKFB3 has a role in nuclear signaling
physiological function
enzyme is required to balance glycolytic activity and antioxidant production to maintain cellular redox balance in prostate cancer cells. Depletion of the enzyme inhibits tumor growth in a xenograft model, indicating that it is required under physiologic nutrient levels. Enzyme mRNA expression is greater in metastatic prostate cancer compared with primary tumors
physiological function
enzyme PFKFB3 belongs to the family of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFBs) that controls the conversion of fructose-6-phosphate to and from fructose-2,6-bisphosphate, a key regulator of the glycolytic enzyme phosphofructokinase-1
physiological function
in human cancers, loss of PTEN, stabilization of HIF-1alpha and activation of Ras and AKT converge to increase the activity of a key regulator of glycolysis, 6-phosphofructo-2-kinase(PFKFB3). This enzyme synthesizes fructose 2,6-bisphosphate, which is an activator of 6-phosphofructo-1-kinase, a key step of glycolysis
physiological function
isozyme PFKFB4 expressed in multiple transformed cells and tumors functions to synthesize fructose 2,6-bisphosphate, PFKFB4 is required for cancer cell survival during the metabolic response to hypoxia, presumably to enable glycolytic production of ATP when the electron transport chain is not fully operational. Isozyme PFKFB4 is overexpressed in human cancers, induced by hypoxia and required for survival and growth of several cancer cell lines
physiological function
PFKFB3 is overexpressed in human cancers, regulated by HIF-1alpha, Akt and PTEN, and required for the survival and growth of multiple cancer types. Role of PFKFB3 in regulating Cdk1- and p27-mediated G1/S blockade and apoptosis
physiological function
possible role of different isozyme PFKFB4 splice variants in cell-specific and/or tissue-specific regulation of glycolysis, role of PFKFB proteins in the control of cancer metabolism. PFKFB4 may be important for cancer cell survival, PFKFB4 plays an essential role in the survival of glioma stem-like cells and of prostate cancer cells. PFKFB4 is known to be a component of the HIF-mediated response to hypoxia, hypoxic induction of PFKFB4 is mediated by a hypoxia response element (HRE) in the promoter region of the PFKFB4 gene
physiological function
role of PFKFB proteins in the control of cancer metabolism
physiological function
role of PFKFB proteins in the control of cancer metabolism. PFKFB3 is known to be a component of the HIF-mediated response to hypoxia. PFKFB3 is a hypoxia-inducible gene that is stimulated through the interaction of HIF-1alpha with a consensus HRE within its promoter region
physiological function
the putative autophagy stimulator, isozyme PFKFB4, drives flux through pentose phosphate pathway. PFKFB4 suppresses oxidative stress and p62 accumulation, without which autophagy is stimulated likely as a reactive oxygen species detoxification response. Genes whose loss enhanced p62 elimination are putative negative regulators of autophagy and the bi-functional enzyme PFKFB4 highly inhibits p62 elimination. PFKFB4 is an autophagy regulator. PFKFB4 suppresses autophagy and p62 accumulation by mitigating reactive oxygen species
physiological function
both a PFKFB3 inhibitor or PFKFB3 silencing by siRNA suppress the basal and the H2O2-induced autophagy concomitantly with the inhibition of AMPK activity. Overexpression of wild-type PFKFB3 promotes H2O2-induced autophagy, but mutant K472/473A, which lost nuclear localizing property, inhibits the autophagic process. The K472/473A mutant stimulates more lactate production, and decreases the activity of AMPK compared to the wild-type
physiological function
overexpression of microRNA miR-26b represses PFKFB3 mRNA and protein levels followed by modulation of the expression of glycolytic components such as LDHA, GLUT-1 and markers of invasion and cell cycle such as MMP-9, MMP-2, cyclin D1 and p27. The binding site for miR-26b is predicted in the 3'-untranslated region of the PFKFB3 gene
physiological function
Transforming growth factor TGFbeta1 induces isoform PFKFB3 expression and stimulates glycolysis in Panc1 cells. siRNA silencing of PFKFB3 prevents the stimulation of glycolysis and in vitro invasion ability of Panc1 cells by TGFbeta1. PFKFB3 silencing suppresses the TGFbeta1-mediated induction of the Snail protein
physiological function
tumor suppressor p53 regulates the expression of PFKFB4 and p53-deficient cancer cells are highly dependent on the function of the enzyme. Depletion of PFKFB4 from p53-deficient cancer cells increases levels of fructose-2,6-bisphosphate, leading to increased glycolytic activity but decreased routing of metabolites through the oxidative arm of the pentose-phosphate pathway. PFKFB4 is also required to support the synthesis and regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in p53-deficient cancer cells. Depletion of PFKFB4-attenuates cellular biosynthetic activity and results in the accumulation of reactive oxygen species and cell death in the absence of p53. Silencing of PFKFB4-induces apoptosis in p53-deficient cancer cells in vivo and interferes with tumor growth
physiological function
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase-2 regulates TP53-dependent paclitaxel sensitivity in ovarian and breast cancers
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Sakakibara, R.; Uemura, M.; Hirata, T.; Okamura, N.; Kato, M.
Human placental fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase: its isozymic form, expression and characterization
Biosci. Biotechnol. Biochem.
61
1949-1952
1997
Homo sapiens
brenda
Sakakibara, R.; Kato, M.; Okamura, N.; Nakagawa, T.; Komada, Y.; Tominaga, N.; Shimojo, M.; Fukasawa, M.
Characterization of a human placental fructose-6-phosphate,2-kinase fructose-2,6-bisphosphatase
J. Biochem.
122
122-128
1997
Homo sapiens
brenda
Lange, A.J.; Li, L.; Vargas, A.M.; Pilkis, S.J.
Expression of human liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in Escherichia coli. Role of N-2 proline in degradation of the protein
J. Biol. Chem.
268
8078-8084
1993
Homo sapiens, Rattus norvegicus
brenda
Lee, Y.H.; Li, Y.; Uyeda, K.; Hasemann, C.A.
Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
J. Biol. Chem.
278
523-530
2003
Homo sapiens (P16118)
brenda
Sakakibara, R.; Okudaira, T.; Fujiwara, K.; Kato, M.; Hirata, T.; Yamanaka, S.; Naito, M.; Fukasawa, M.
Tissue distribution of placenta-type 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Biochem. Biophys. Res. Commun.
257
177-181
1999
Homo sapiens, Rattus norvegicus
brenda
Chesney, J.; Mitchell, R.; Benigni, F.; Bacher, M.; Spiegel, L.; Al-Abed, Y.; Han, J.H.; Metz, C.; Bucala, R.
An inducible gene product for 6-phosphofructo-2-kinase with an AU-rich instability element: role in tumor cell glycolysis and the Warburg effect
Proc. Natl. Acad. Sci. USA
96
3047-3052
1999
Faxonius limosus, Homo sapiens (Q16875), Homo sapiens
brenda
Manes, N.P.; El-Maghrabi, M.R.
The kinase activity of human brain 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is regulated via inhibition by phosphoenolpyruvate
Arch. Biochem. Biophys.
438
125-136
2005
Homo sapiens (Q16875)
brenda
Kim, S.G.; Manes, N.P.; El-Maghrabi, M.R.; Lee, Y.H.
Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3): a possible new target for cancer therapy
J. Biol. Chem.
281
2939-2944
2006
Homo sapiens (P16118), Homo sapiens
brenda
Mouton, V.; Vertommen, D.; Bertrand, L.; Hue, L.; Rider, M.H.
Evaluation of the role of protein kinase Czeta in insulin-induced heat 6-phosphofructo-2-kinase activation
Cell. Signal.
19
52-61
2007
Homo sapiens
brenda
Chesney, J.
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase and tumor cell glycolysis
Curr. Opin. Clin. Nutr. Metab. Care
9
535-539
2006
Homo sapiens
brenda
Telang, S.; Yalcin, A.; Clem, A.L.; Bucala, R.; Lane, A.N.; Eaton, J.W.; Chesney, J.
Ras transformation requires metabolic control by 6-phosphofructo-2-kinase
Oncogene
25
7225-7234
2006
Homo sapiens, Mus musculus
brenda
Kessler, R.; Bleichert, F.; Warnke, J.P.; Eschrich, K.
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3) is up-regulated in high-grade astrocytomas
J. Neurooncol.
86
257-264
2008
Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877)
brenda
Duran, J.; Navarro-Sabate, A.; Pujol, A.; Perales, J.C.; Manzano, A.; Obach, M.; Gomez, M.; Bartrons, R.
Overexpression of ubiquitous 6-phosphofructo-2-kinase in the liver of transgenic mice results in weight gain
Biochem. Biophys. Res. Commun.
365
291-297
2008
Homo sapiens (Q16875)
brenda
Clem, B.; Telang, S.; Clem, A.; Yalcin, A.; Meier, J.; Simmons, A.; Rasku, M.A.; Arumugam, S.; Dean, W.L.; Eaton, J.; Lane, A.; Trent, J.O.; Chesney, J.
Small-molecule inhibition of 6-phosphofructo-2-kinase activity suppresses glycolytic flux and tumor growth
Mol. Cancer Ther.
7
110-120
2008
Homo sapiens (Q16875), Homo sapiens
brenda
Yalcin, A.; Clem, B.F.; Simmons, A.; Lane, A.; Nelson, K.; Clem, A.L.; Brock, E.; Siow, D.; Wattenberg, B.; Telang, S.; Chesney, J.
Nuclear targeting of 6-phosphofructo-2-kinase (PFKFB3) increases proliferation via cyclin-dependent kinases
J. Biol. Chem.
284
24223-24232
2009
Homo sapiens (Q16875), Homo sapiens
brenda
Ros, S.; Santos, C.R.; Moco, S.; Baenke, F.; Kelly, G.; Howell, M.; Zamboni, N.; Schulze, A.
Functional metabolic screen identifies 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 as an important regulator of prostate cancer cell survival
Cancer Discov.
2
328-343
2012
Homo sapiens (Q16877)
brenda
Brooke, D.G.; van Dam, E.M.; Watts, C.K.; Khoury, A.; Dziadek, M.A.; Brooks, H.; Graham, L.J.; Flanagan, J.U.; Denny, W.A.
Targeting the Warburg Effect in cancer; relationships for 2-arylpyridazinones as inhibitors of the key glycolytic enzyme 6-phosphofructo-2-kinase/2,6-bisphosphatase 3 (PFKFB3)
Bioorg. Med. Chem.
22
1029-1039
2014
Homo sapiens (Q16875)
brenda
Novellasdemunt, L.; Tato, I.; Navarro-Sabate, A.; Ruiz-Meana, M.; Mendez-Lucas, A.; Perales, J.C.; Garcia-Dorado, D.; Ventura, F.; Bartrons, R.; Rosa, J.L.
Akt-dependent activation of the heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) isoenzyme by amino acids
J. Biol. Chem.
288
10640-10651
2013
Homo sapiens (O60825), Homo sapiens, Rattus norvegicus (Q9JJH5), Rattus norvegicus Sprague-Dawley (Q9JJH5)
brenda
Chesney, J.; Clark, J.; Klarer, A.C.; Imbert-Fernandez, Y.; Lane, A.N.; Telang, S.
Fructose-2,6-bisphosphate synthesis by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (PFKFB4) is required for the glycolytic response to hypoxia and tumor growth
Oncotarget
5
6670-6686
2014
Homo sapiens (Q16877)
brenda
Ros, S.; Schulze, A.
Balancing glycolytic flux: the role of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatases in cancer metabolism
Cancer Metab.
1
8
2013
Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877)
brenda
Klarer, A.C.; ONeal, J.; Imbert-Fernandez, Y.; Clem, A.; Ellis, S.R.; Clark, J.; Clem, B.; Chesney, J.; Telang, S.
Inhibition of 6-phosphofructo-2-kinase (PFKFB3) induces autophagy as a survival mechanism
Cancer Metab.
2
2
2014
Homo sapiens (Q16875), Homo sapiens
brenda
Yalcin, A.; Clem, B.F.; Imbert-Fernandez, Y.; Ozcan, S.C.; Peker, S.; ONeal, J.; Klarer, A.C.; Clem, A.L.; Telang, S.; Chesney, J.
6-Phosphofructo-2-kinase (PFKFB3) promotes cell cycle progression and suppresses apoptosis via Cdk1-mediated phosphorylation of p27
Cell Death Dis.
5
e1337
2014
Homo sapiens (Q16875), Homo sapiens
brenda
Clem, B.F.; ONeal, J.; Tapolsky, G.; Clem, A.L.; Imbert-Fernandez, Y.; Kerr, D.A.; Klarer, A.C.; Redman, R.; Miller, D.M.; Trent, J.O.; Telang, S.; Chesney, J.
Targeting 6-phosphofructo-2-kinase (PFKFB3) as a therapeutic strategy against cancer
Mol. Cancer Ther.
12
1461-1470
2013
Homo sapiens (Q16875), Homo sapiens
brenda
Strohecker, A.M.; Joshi, S.; Possemato, R.; Abraham, R.T.; Sabatini, D.M.; White, E.
Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel autophagy regulator by high content shRNA screening
Oncogene
34
5662-5676
2015
Homo sapiens (Q16877)
brenda
Minchenko, D.; Lypova, N.; Harmash, Y.; Kulinich, A.; Marunych, R.; Karbovskyi, L.; Minchenko, O.
Expression of genes encoded 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase and 6-phosphofructo-1-kinase in U87 glioma cells with ERN1 loss of function: hypoxic regulation
Res. J. Pharm. Biol. Chem. Sci.
4
28-42
2013
Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877)
-
brenda
Lea, M.A.; Guzman, Y.; Desbordes, C.
Inhibition of growth by combined treatment with inhibitors of lactate dehydrogenase and either phenformin or inhibitors of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Anticancer Res.
36
1479-1488
2016
Homo sapiens (Q16875)
brenda
Yalcin, A.; Solakoglu, T.H.; Ozcan, S.C.; Guzel, S.; Peker, S.; Celikler, S.; Balaban, B.D.; Sevinc, E.; Gurpinar, Y.; Chesney, J.A.
6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase-3 is required for transforming growth factor beta1-enhanced invasion of Panc1 cells invitro
Biochem. Biophys. Res. Commun.
484
687-693
2017
Homo sapiens (Q16875)
brenda
Ros, S.; Floeter, J.; Kaymak, I.; Da Costa, C.; Houddane, A.; Dubuis, S.; Griffiths, B.; Mitter, R.; Walz, S.; Blake, S.; Behrens, A.; Brindle, K.M.; Zamboni, N.; Rider, M.H.; Schulze, A.
6-Phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 is essential for p53-null cancer cells
Oncogene
36
3287-3299
2017
Homo sapiens (Q16877)
brenda
Du, J.Y.; Wang, L.F.; Wang, Q.; Yu, L.D.
miR-26b inhibits proliferation, migration, invasion and apoptosis induction via the downregulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 driven glycolysis in osteosarcoma cells
Oncol. Rep.
33
1890-1898
2015
Homo sapiens (Q16875)
brenda
Yan, S.; Wei, X.; Xu, S.; Sun, H.; Wang, W.; Liu, L.; Jiang, X.; Zhang, Y.; Che, Y.
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoform 3 spatially mediates autophagy through the AMPK signaling pathway
Oncotarget
8
80909-80922
2017
Homo sapiens (Q16875)
brenda
Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding
Proteins
85
117-124
2017
Homo sapiens (O60825), Bos taurus (P26285)
brenda
Langer, S.; Hofmeister-Brix, A.; Waterstradt, R.; Baltrusch, S.
6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase and small chemical activators affect enzyme activity of activating glucokinase mutants by distinct mechanisms
Biochem. Pharmacol.
168
149-161
2019
Homo sapiens (O60825)
brenda
Yang, H.; Shu, Z.; Jiang, Y.; Mao, W.; Pang, L.; Redwood, A.; Jeter-Jones, S.L.; Jennings, N.B.; Ornelas, A.; Zhou, J.; Rodriguez-Aguayo, C.; Bartholomeusz, G.; Iles, L.R.; Zacharias, N.M.; Millward, S.W.; Lopez-Berestein, G.; Le, X.F.; Ahmed, A.A.; Piwnica-Worms, H.; Sood, A.K.; Bast, R.C.; Lu, Z.
6-Phosphofructo-2-kinase/fructose-2,6-biphosphatase-2 regulates TP53-dependent paclitaxel sensitivity in ovarian and breast cancers
Clin. Cancer Res.
25
5702-5716
2019
Homo sapiens (O60825)
brenda
Emini Veseli, B.; Perrotta, P.; Van Wielendaele, P.; Lambeir, A.M.; Abdali, A.; Bellosta, S.; Monaco, G.; Bultynck, G.; Martinet, W.; De Meyer, G.R.Y.
Small molecule 3PO inhibits glycolysis but does not bind to 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3)
FEBS Lett.
594
3067-3075
2020
Homo sapiens (Q16875)
brenda
Lypova, N.; Telang, S.; Chesney, J.; Imbert-Fernandez, Y.
Increased 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 activity in response to EGFR signaling contributes to non-small cell lung cancer cell survival
J. Biol. Chem.
294
10530-10543
2019
Homo sapiens (Q16875)
brenda
Bao, J.; Wu, Y.; Wang, L.; Zhu, Y.
The role of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 in esophageal squamous cell carcinoma
Medicine (Baltimore)
99
e19626
2020
Homo sapiens (Q16875)
brenda
Yi, M.; Ban, Y.; Tan, Y.; Xiong, W.; Li, G.; Xiang, B.
6-Phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 and 4 A pair of valves for fine-tuning of glucose metabolism in human cancer
Mol. Metab.
20
1-13
2019
Homo sapiens (Q16875), Homo sapiens (Q16877)
brenda