PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
20656052-6	2010	I(0.5) for calcium ion (91 microM) is 100 times higher than the corresponding value of mammalian muscle FBPase.	Calcium	11-18	fructose-bisphosphatase 2	Homo sapiens	97-110
20656052-9	2010	AMP and fructose-2,6-bisphosphate (Fru-2,6P(2)) are potent inhibitors of frog muscle FBPase with I(0.5) of 0.2 microM and K(i) of 114 nM, respectively.	Adenosine Monophosphate	0-3	fructose-bisphosphatase 2	Homo sapiens	78-91
20656052-9	2010	AMP and fructose-2,6-bisphosphate (Fru-2,6P(2)) are potent inhibitors of frog muscle FBPase with I(0.5) of 0.2 microM and K(i) of 114 nM, respectively.	fructose 2,6-diphosphate	8-33	fructose-bisphosphatase 2	Homo sapiens	78-91
20656052-9	2010	AMP and fructose-2,6-bisphosphate (Fru-2,6P(2)) are potent inhibitors of frog muscle FBPase with I(0.5) of 0.2 microM and K(i) of 114 nM, respectively.	fru-2,6p	35-43	fructose-bisphosphatase 2	Homo sapiens	78-91
20656052-12	2010	I(0.5) for AMP for P. esculentus muscle FBPase is 55 times lower than the corresponding value for P. esculentus liver isozyme.	Adenosine Monophosphate	11-14	fructose-bisphosphatase 2	Homo sapiens	33-46
20702580-3	2010	Therefore, the goal of this study was the analysis of GK-PFK-2/FBPase-2 complex formation and its effect on metabolic stimulus-secretion coupling in beta-cells in dependence upon glucose.	Glucose	179-186	fructose-bisphosphatase 2	Homo sapiens	63-71
20702580-11	2010	Thus, this study clearly showed that binding and activation of GK by PFK-2/FBPase-2 in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion.	Glucose	113-120	fructose-bisphosphatase 2	Homo sapiens	75-83
20702580-11	2010	Thus, this study clearly showed that binding and activation of GK by PFK-2/FBPase-2 in beta-cells is promoted by glucose, resulting in an enhancement of insulin secretion at stimulatory glucose concentrations, without affecting basal insulin secretion.	Glucose	186-193	fructose-bisphosphatase 2	Homo sapiens	75-83
18214967-2	2008	In this article, we present evidence that the conservation is responsible for the unique properties of the muscle FBPase isozyme: high sensitivity to AMP and Ca(2+) inhibition and the high affinity to muscle aldolase, which is a factor desensitizing muscle FBPase toward AMP and Ca(2+).	Adenosine Monophosphate	150-153	fructose-bisphosphatase 2	Homo sapiens	107-120
19626708-3	2009	To test this, HL-1 cardiomyocytes were transfected with FITC-labeled muscle FBPase constructs, bearing mutations within the putative nuclear localization signal (NLS).	Fluorescein-5-isothiocyanate	56-60	fructose-bisphosphatase 2	Homo sapiens	69-82
18214967-2	2008	In this article, we present evidence that the conservation is responsible for the unique properties of the muscle FBPase isozyme: high sensitivity to AMP and Ca(2+) inhibition and the high affinity to muscle aldolase, which is a factor desensitizing muscle FBPase toward AMP and Ca(2+).	Adenosine Monophosphate	150-153	fructose-bisphosphatase 2	Homo sapiens	250-263
18214967-2	2008	In this article, we present evidence that the conservation is responsible for the unique properties of the muscle FBPase isozyme: high sensitivity to AMP and Ca(2+) inhibition and the high affinity to muscle aldolase, which is a factor desensitizing muscle FBPase toward AMP and Ca(2+).	Adenosine Monophosphate	271-274	fructose-bisphosphatase 2	Homo sapiens	107-120
18214967-2	2008	In this article, we present evidence that the conservation is responsible for the unique properties of the muscle FBPase isozyme: high sensitivity to AMP and Ca(2+) inhibition and the high affinity to muscle aldolase, which is a factor desensitizing muscle FBPase toward AMP and Ca(2+).	Adenosine Monophosphate	271-274	fructose-bisphosphatase 2	Homo sapiens	250-263
18214967-4	2008	On the other hand, the first residue significantly influencing the kinetics of muscle FBPase is proline 5.	Proline	96-103	fructose-bisphosphatase 2	Homo sapiens	79-92
18214967-6	2008	Deletion of the first 10 amino acids of muscle FBPase abolishes cooperativity of Mg(2+) activation and results in biphasic inhibition of the enzyme by AMP.	magnesium ion	81-87	fructose-bisphosphatase 2	Homo sapiens	40-53
18214967-6	2008	Deletion of the first 10 amino acids of muscle FBPase abolishes cooperativity of Mg(2+) activation and results in biphasic inhibition of the enzyme by AMP.	Adenosine Monophosphate	151-154	fructose-bisphosphatase 2	Homo sapiens	40-53
17805487-1	2008	The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) controls the glycolytic flux via the allosteric activator fructose 2,6-bisphosphate.	Fructose	49-57	fructose-bisphosphatase 2	Homo sapiens	84-92
17374851-1	2007	Glucokinase (GK) and 6-phosphofructo-2-kinase (PFK-2)/fructose-2,6-bisphosphatase (FBP-2) are each powerful regulators of hepatic carbohydrate metabolism that have been reported to influence each other"s expression, activities, and cellular location.	Carbohydrates	130-142	fructose-bisphosphatase 2	Homo sapiens	83-88
17805487-1	2008	The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) controls the glycolytic flux via the allosteric activator fructose 2,6-bisphosphate.	2,6-bisphosphate	161-177	fructose-bisphosphatase 2	Homo sapiens	84-92
17374851-7	2007	This means that the GK-bound PFK-2/FBP-2 produces more of the biofactor fructose-2,6-bisphosphate, a potent activator of 6-phosphofructo-1-kinase, the committing step to glycolysis.	fructose 2,6-diphosphate	72-97	fructose-bisphosphatase 2	Homo sapiens	35-40
17374851-8	2007	Therefore, we conclude that the binding of GK to PFK-2/FBP-2 promotes a coordinated up-regulation of glucose phosphorylation and glycolysis in the liver, i.e. hepatic glucose disposal.	Glucose	101-108	fructose-bisphosphatase 2	Homo sapiens	55-60
17374851-8	2007	Therefore, we conclude that the binding of GK to PFK-2/FBP-2 promotes a coordinated up-regulation of glucose phosphorylation and glycolysis in the liver, i.e. hepatic glucose disposal.	Glucose	167-174	fructose-bisphosphatase 2	Homo sapiens	55-60
17374851-9	2007	The GK:PFK-2/FBP-2 interaction may also serve as a metabolic signal transduction pathway for the glucose sensor, GK, in the liver.	Glucose	97-104	fructose-bisphosphatase 2	Homo sapiens	13-18
16860376-2	2006	A truly bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PFK2/FBP2), with two active sites synthesizes F26P2 from fructose-6-phosphate (F6P) and ATP or degrades F26P2 to F6P and Pi.	fructose-6-phosphate	141-161	fructose-bisphosphatase 2	Homo sapiens	89-93
16766380-3	2006	Results from a bioinformatics analysis of genome databases suggest that very early in evolution, in a common ancestor of all extant eukaryotes, distinct genes encoding PFK-2 and FBPase-2, or related enzymes with broader substrate specificity, fused resulting in a bifunctional enzyme both domains of which had, or later acquired, specificity for fructose 2,6-bisphosphate.	fructose 2,6-diphosphate	346-371	fructose-bisphosphatase 2	Homo sapiens	178-186
16860376-2	2006	A truly bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PFK2/FBP2), with two active sites synthesizes F26P2 from fructose-6-phosphate (F6P) and ATP or degrades F26P2 to F6P and Pi.	Adenosine Triphosphate	172-175	fructose-bisphosphatase 2	Homo sapiens	89-93
11522786-11	2001	The interaction between glucokinase and PFK-2/FBPase-2 may provide the rationale for recent observations of a fructose-2,6-bisphosphate level-dependent partial channeling of glycolytic intermediates between glucokinase and glycolytic enzymes.	fructose 2,6-diphosphate	110-135	fructose-bisphosphatase 2	Homo sapiens	46-54
15554702-2	2004	It has been proposed that association of aldolase with FBPase not only desensitizes muscle FBPase toward AMP inhibition but it also might enable the channeling of intermediates between the enzymes [Rakus et al.	Adenosine Monophosphate	105-108	fructose-bisphosphatase 2	Homo sapiens	84-97
15554702-10	2004	A physiological concentration of Mg(2+) increased the affinity of muscle FBPase to muscle aldolase, whereas higher concentrations of the cation decreased the concentration of the complex.	magnesium ion	33-39	fructose-bisphosphatase 2	Homo sapiens	66-79
12939425-4	2003	In CSF, the overall folate binding capacity by the two soluble folate-binding proteins FBP1 and FBP2 (sFBP) was measured using a radioligand binding method for H3-labeled folate.	Folic Acid	20-26	fructose-bisphosphatase 2	Homo sapiens	96-100
12939425-4	2003	In CSF, the overall folate binding capacity by the two soluble folate-binding proteins FBP1 and FBP2 (sFBP) was measured using a radioligand binding method for H3-labeled folate.	Folic Acid	63-69	fructose-bisphosphatase 2	Homo sapiens	96-100
12939425-4	2003	In CSF, the overall folate binding capacity by the two soluble folate-binding proteins FBP1 and FBP2 (sFBP) was measured using a radioligand binding method for H3-labeled folate.	HS 3	160-162	fructose-bisphosphatase 2	Homo sapiens	96-100
12939425-4	2003	In CSF, the overall folate binding capacity by the two soluble folate-binding proteins FBP1 and FBP2 (sFBP) was measured using a radioligand binding method for H3-labeled folate.	Folic Acid	63-69	fructose-bisphosphatase 2	Homo sapiens	96-100
11522786-13	2001	Changes in fructose-2,6-bisphosphate levels and modulation of PFK-2/FBPase-2 activities may participate in the physiological regulation of glucokinase-mediated glucose-induced insulin secretion.	Glucose	160-167	fructose-bisphosphatase 2	Homo sapiens	68-76
9119406-1	1997	6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) catalyzes the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis.	fructose 2,6-diphosphate	113-138	fructose-bisphosphatase 2	Homo sapiens	60-68
11165514-0	2001	PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate.	fructose 2,6-diphosphate	61-86	fructose-bisphosphatase 2	Homo sapiens	6-14
10964712-0	2000	Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition.	Adenosine Monophosphate	59-62	fructose-bisphosphatase 2	Homo sapiens	26-39
10964712-1	2000	Muscle aldolase bound to muscle FBPase (K(d) = 8.7 microM) decreases the latter"s sensitivity towards AMP inhibition.	Adenosine Monophosphate	102-105	fructose-bisphosphatase 2	Homo sapiens	25-38
9652401-1	1998	6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme that catalyzes the synthesis and degradation of Fru-2,6-P2, a key regulator of glycolysis.	fru-2,6-p2	143-153	fructose-bisphosphatase 2	Homo sapiens	60-68
10095107-1	1999	6-Phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK-2/FBPase-2) is a bifunctional enzyme responsible for the synthesis and breakdown of Fru-2,6-P2, a key metabolite in the regulation of glycolysis.	fru-2,6-p2	142-152	fructose-bisphosphatase 2	Homo sapiens	60-68
9095468-2	1996	Fru-2,6-P2 content is tightly regulated and appears to be under the control of different hormones and growth factors, acting either through covalent modification of isoenzymatic forms of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase (PFK-2/FBPase-2), the bifunctional enzyme responsible for the synthesis and the degradation of the compound, or through changes in transcription rate and/or in the expression of different isoforms of the enzyme.	fru-2,6-p2	0-10	fructose-bisphosphatase 2	Homo sapiens	247-255
14812285-0	1950	[Specificity of alkaline phosphatase and of hexosediphosphatase (fructose-1,6-phosphatase) towards various glucidic esters].	glucidic esters	107-122	fructose-bisphosphatase 2	Homo sapiens	44-63
34234350-2	2021	One of the rate limiting enzymes of glycolysis is 6-phosphofructo-1-kinase, which is allosterically activated by fructose 2,6-bisphosphate which in turn is produced by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2 or PFKFB).	fructose 2,6-diphosphate	113-138	fructose-bisphosphatase 2	Homo sapiens	228-236
35626746-2	2022	Here, we present several lines of evidence that in HL-1 cardiomyocytes, a forced, chemically induced reduction in the FBP2 dimer-tetramer ratio that imitates AMP and NAD+ action and restricts FBP2-mitochondria interaction, results in an increase in Tau phosphorylation, augmentation of FBP2-Tau and FBP2-MAP1B interactions, disturbance of tubulin network, marked reduction in the speed of mitochondrial trafficking and increase in mitophagy.	Adenosine Monophosphate	158-161	fructose-bisphosphatase 2	Homo sapiens	118-122
8395137-4	1993	The results indicate that in established lines of hepatoma cells the biochemical properties of the bifunctional enzyme, PFK-2/FBPase-2, involved in the synthesis and degradation of fructose 2,6-bisphosphate, differ from those of the enzyme from normal liver.	fructose 2,6-diphosphate	181-206	fructose-bisphosphatase 2	Homo sapiens	126-134
35626746-2	2022	Here, we present several lines of evidence that in HL-1 cardiomyocytes, a forced, chemically induced reduction in the FBP2 dimer-tetramer ratio that imitates AMP and NAD+ action and restricts FBP2-mitochondria interaction, results in an increase in Tau phosphorylation, augmentation of FBP2-Tau and FBP2-MAP1B interactions, disturbance of tubulin network, marked reduction in the speed of mitochondrial trafficking and increase in mitophagy.	NAD	166-170	fructose-bisphosphatase 2	Homo sapiens	118-122
18934711-0	1948	Inhibition of hexosediphosphatase by sulphhydryl reagents and by ascorbic acid.	sulphhydryl reagents	37-57	fructose-bisphosphatase 2	Homo sapiens	14-33
18934711-0	1948	Inhibition of hexosediphosphatase by sulphhydryl reagents and by ascorbic acid.	Ascorbic Acid	65-78	fructose-bisphosphatase 2	Homo sapiens	14-33
33977939-4	2021	Our data showed that palmitate (PA) and oleic acid (OA) induced the expression of FBP2 in time- and dose-dependent manners, and accelerated the development of lipid droplets in LO2 human normal liver cells.	Palmitates	21-30	fructose-bisphosphatase 2	Homo sapiens	82-86
33977939-4	2021	Our data showed that palmitate (PA) and oleic acid (OA) induced the expression of FBP2 in time- and dose-dependent manners, and accelerated the development of lipid droplets in LO2 human normal liver cells.	Palmitates	32-34	fructose-bisphosphatase 2	Homo sapiens	82-86
33977939-4	2021	Our data showed that palmitate (PA) and oleic acid (OA) induced the expression of FBP2 in time- and dose-dependent manners, and accelerated the development of lipid droplets in LO2 human normal liver cells.	Oleic Acid	40-50	fructose-bisphosphatase 2	Homo sapiens	82-86
33977939-4	2021	Our data showed that palmitate (PA) and oleic acid (OA) induced the expression of FBP2 in time- and dose-dependent manners, and accelerated the development of lipid droplets in LO2 human normal liver cells.	Oleic Acid	52-54	fructose-bisphosphatase 2	Homo sapiens	82-86
33977939-7	2021	Moreover, betaine, a methyl donor, attenuated the expression of the FBP2 gene, the accumulation of lipid droplets, and the expression of perilipin-2, a biomarker of lipid droplets, in LO2 cells.	Betaine	10-17	fructose-bisphosphatase 2	Homo sapiens	68-72
33946543-3	2021	NAD+ and AMP stabilize an inactive T-state of Fbp2 and thus, affect these interactions.	NAD	0-4	fructose-bisphosphatase 2	Homo sapiens	46-50
33946543-3	2021	NAD+ and AMP stabilize an inactive T-state of Fbp2 and thus, affect these interactions.	Adenosine Monophosphate	9-12	fructose-bisphosphatase 2	Homo sapiens	46-50
33946543-6	2021	We describe for the first time the kinetics of Fbp2 in the presence of Co2+, and we provide a line of evidence that Co2+ blocks the AMP-induced transition of Fbp2 to the canonical T-state triggering instead of a new, non-canonical T-state.	Adenosine Monophosphate	132-135	fructose-bisphosphatase 2	Homo sapiens	47-51
33946543-6	2021	We describe for the first time the kinetics of Fbp2 in the presence of Co2+, and we provide a line of evidence that Co2+ blocks the AMP-induced transition of Fbp2 to the canonical T-state triggering instead of a new, non-canonical T-state.	Adenosine Monophosphate	132-135	fructose-bisphosphatase 2	Homo sapiens	158-162
33671514-4	2021	However, the most potent regulator of PFK-1 is fructose-2,6-bisphosphate (F-2,6-BP), the level of which is strongly associated with 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase activity (PFK-2/FBPase-2, PFKFB).	fructose 2,6-diphosphate	47-72	fructose-bisphosphatase 2	Homo sapiens	201-209
32492972-6	2020	We therefore hypothesize that this NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation.	Lactic Acid	153-160	fructose-bisphosphatase 2	Homo sapiens	72-76
33671514-4	2021	However, the most potent regulator of PFK-1 is fructose-2,6-bisphosphate (F-2,6-BP), the level of which is strongly associated with 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase activity (PFK-2/FBPase-2, PFKFB).	fructose 2,6-diphosphate	74-82	fructose-bisphosphatase 2	Homo sapiens	201-209
33671514-5	2021	PFK-2/FBPase-2 is a bifunctional enzyme responsible for F-2,6-BP synthesis and degradation.	fructose 2,6-diphosphate	56-64	fructose-bisphosphatase 2	Homo sapiens	6-14
33502838-3	2021	It has been shown that residue E69 in this loop plays a key role in the sensitivity of muscle FBPase towards calcium ions.	E69	31-34	fructose-bisphosphatase 2	Homo sapiens	87-100
33502838-3	2021	It has been shown that residue E69 in this loop plays a key role in the sensitivity of muscle FBPase towards calcium ions.	Calcium	109-116	fructose-bisphosphatase 2	Homo sapiens	87-100
29435871-1	2018	Lymphocyte activation is associated with rapid increase of both the glycolytic activator fructose 2,6-bisphosphate (Fru-2,6-P2) and the enzyme responsible for its synthesis, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2).	fructose 2,6-diphosphate	89-114	fructose-bisphosphatase 2	Homo sapiens	234-242
32492972-4	2020	Silencing of Fbp2 expression or simultaneous inhibition and tetramerization of the enzyme with a synthetic effector mimicking the action of physiological inhibitors (NAD+ and AMP) abolishes Camk2 autoactivation and blocks formation of the early phase of LTP and expression of the late phase LTP markers.	NAD	166-170	fructose-bisphosphatase 2	Homo sapiens	13-17
32492972-4	2020	Silencing of Fbp2 expression or simultaneous inhibition and tetramerization of the enzyme with a synthetic effector mimicking the action of physiological inhibitors (NAD+ and AMP) abolishes Camk2 autoactivation and blocks formation of the early phase of LTP and expression of the late phase LTP markers.	Adenosine Monophosphate	175-178	fructose-bisphosphatase 2	Homo sapiens	13-17
32492972-5	2020	Astrocyte-derived lactate reduces NAD+/NADH ratio in neurons and thus diminishes the pool of tetrameric and increases the fraction of dimeric Fbp2.	Lactic Acid	18-25	fructose-bisphosphatase 2	Homo sapiens	142-146
32492972-6	2020	We therefore hypothesize that this NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation.	NAD	35-39	fructose-bisphosphatase 2	Homo sapiens	72-76
31947613-6	2020	Since Fbp2 oligomerization state and thus, its role is regulated by AMP and NAD+-crucial indicators of cellular metabolic conditions-we hypothesize that the Hif1alpha-dependent regulation of the metabolism in cancer is modulated through Fbp2, a sensor of the energy and redox state of a cell.	Adenosine Monophosphate	68-71	fructose-bisphosphatase 2	Homo sapiens	6-10
31947613-6	2020	Since Fbp2 oligomerization state and thus, its role is regulated by AMP and NAD+-crucial indicators of cellular metabolic conditions-we hypothesize that the Hif1alpha-dependent regulation of the metabolism in cancer is modulated through Fbp2, a sensor of the energy and redox state of a cell.	NAD	76-79	fructose-bisphosphatase 2	Homo sapiens	6-10
29435871-1	2018	Lymphocyte activation is associated with rapid increase of both the glycolytic activator fructose 2,6-bisphosphate (Fru-2,6-P2) and the enzyme responsible for its synthesis, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2).	fru-2,6-p2	116-126	fructose-bisphosphatase 2	Homo sapiens	234-242
27146014-3	2016	Glucokinase is inhibited in the postabsorptive state by sequestration in the nucleus bound to GKRP, and it is activated postprandially by portal hyperglycemia and fructose through dissociation from GKRP, translocation to the cytoplasm, and binding to PFK2/FBP2.	Fructose	163-171	fructose-bisphosphatase 2	Homo sapiens	256-260
29383170-1	2017	Muscle fructose 1,6-bisphosphatase (FBP2), besides being a regulatory enzyme of glyconeogenesis also protects mitochondria against calcium stress and plays a key role in regulation of the cell cycle, promoting cardiomyocytes survival.	Calcium	131-138	fructose-bisphosphatase 2	Homo sapiens	36-40
29383170-6	2017	The dimeric form is fully active and insensitive to AMP, the main allosteric inhibitor of FBP2.	Adenosine Monophosphate	52-55	fructose-bisphosphatase 2	Homo sapiens	90-94
29383170-8	2017	Only the tetrameric form of FBP2 is retained in cardiomyocyte cell nucleus whereas only the dimeric form associates with mitochondria and protects them against stress stimuli, such as elevated calcium and H2O2 level.	Calcium	193-200	fructose-bisphosphatase 2	Homo sapiens	28-32
29383170-8	2017	Only the tetrameric form of FBP2 is retained in cardiomyocyte cell nucleus whereas only the dimeric form associates with mitochondria and protects them against stress stimuli, such as elevated calcium and H2O2 level.	Hydrogen Peroxide	205-209	fructose-bisphosphatase 2	Homo sapiens	28-32
27050133-18	2016	In addition, the crystal structures of muscle FBPase in the T conformation with and without AMP strongly suggest that the T-to-R transition is a discrete jump rather than a shift of an equilibrium smooth transition through multiple intermediate states.	Adenosine Monophosphate	92-95	fructose-bisphosphatase 2	Homo sapiens	39-52
26810065-5	2016	At the cellular level, we found that FBP2 was correlated with cell cycle progression by accelerating G1/S transition, and knockdown of FBP2 could weaken cell proliferation, anchorage-independent cell growth, while enhancing the sensitivity of breast cancer cells to doxorubicin.	Doxorubicin	266-277	fructose-bisphosphatase 2	Homo sapiens	135-139
27050133-19	2016	Finally, using snapshots from three crystal structures of human muscle FBPase, it is conclusively demonstrated that the AMP-binding event is correlated with a beta alpha transition at the N-terminus of the protein and with the formation of a new helical structure.	Adenosine Monophosphate	120-123	fructose-bisphosphatase 2	Homo sapiens	64-77
24412565-2	2014	Here, we show that the quaternary structure of FBP2 plays a crucial role in this interaction, and that the AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria.	Adenosine Monophosphate	107-110	fructose-bisphosphatase 2	Homo sapiens	47-51
24566088-5	2014	Glucagon caused dissociation of glucokinase from PFK2/FBPase2, concomitant with phosphorylation of PFK2/FBPase2 on Ser-32, uptake of glucokinase into the nucleus and increased interaction with GKRP.	Glucagon	0-8	fructose-bisphosphatase 2	Homo sapiens	54-61
24566088-5	2014	Glucagon caused dissociation of glucokinase from PFK2/FBPase2, concomitant with phosphorylation of PFK2/FBPase2 on Ser-32, uptake of glucokinase into the nucleus and increased interaction with GKRP.	Glucagon	0-8	fructose-bisphosphatase 2	Homo sapiens	104-111
24634222-10	2014	We suggest that bifunctionality of PFK-2/FBPase-2 complements the metabolic zonation of the liver by ensuring coherent switching in response to insulin and glucagon.	Glucagon	156-164	fructose-bisphosphatase 2	Homo sapiens	41-49
26901106-3	2016	Using perturbation approaches (kinase inhibitors, small interfering RNAs) and a novel system for rapalog-dependent activation of AKT isoforms, we demonstrate that activity of the phosphatidylinositol-4,5-biphosphate 3-kinase/AKT pathway is involved in the enrichment of nuclear FBP1 and FBP2 in liver cancer cells.	Phosphatidylinositol 4,5-Diphosphate	179-215	fructose-bisphosphatase 2	Homo sapiens	287-291
24412565-2	2014	Here, we show that the quaternary structure of FBP2 plays a crucial role in this interaction, and that the AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria.	Adenosine Monophosphate	107-110	fructose-bisphosphatase 2	Homo sapiens	136-140
24412565-4	2014	This strengthens the recently raised hypothesis that FBP2 evolved as a regulator not only for glycogen storage but also for mitochondrial function in contracting muscle.	Glycogen	94-102	fructose-bisphosphatase 2	Homo sapiens	53-57
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	fructose-1,6-diphosphate	126-151	fructose-bisphosphatase 2	Homo sapiens	44-73
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	fructose-1,6-diphosphate	126-151	fructose-bisphosphatase 2	Homo sapiens	75-79
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	fructose-6-phosphate	155-175	fructose-bisphosphatase 2	Homo sapiens	44-73
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	fructose-6-phosphate	155-175	fructose-bisphosphatase 2	Homo sapiens	75-79
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	Phosphates	142-151	fructose-bisphosphatase 2	Homo sapiens	44-73
24063558-2	2013	Here, we investigated the potential role of fructose-1,6-bisphosphatase-2 (FBP2), the enzyme that catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose-6-phosphate and inorganic phosphate in glucose metabolism, in gastric cancer (GC) development.	Phosphates	142-151	fructose-bisphosphatase 2	Homo sapiens	75-79
24063558-5	2013	Bisulphite genomic sequencing (BGS) in gastric cancer cell lines revealed that the FBP2 promoter region was densely methylated, and treatment of GC cells with the demethylation reagent, 5-aza-2-deoxycytidine (5-Aza), led to an increase in FBP2 expression.	hydrogen sulfite	0-10	fructose-bisphosphatase 2	Homo sapiens	83-87
24063558-5	2013	Bisulphite genomic sequencing (BGS) in gastric cancer cell lines revealed that the FBP2 promoter region was densely methylated, and treatment of GC cells with the demethylation reagent, 5-aza-2-deoxycytidine (5-Aza), led to an increase in FBP2 expression.	Decitabine	186-207	fructose-bisphosphatase 2	Homo sapiens	83-87
24063558-5	2013	Bisulphite genomic sequencing (BGS) in gastric cancer cell lines revealed that the FBP2 promoter region was densely methylated, and treatment of GC cells with the demethylation reagent, 5-aza-2-deoxycytidine (5-Aza), led to an increase in FBP2 expression.	Decitabine	186-207	fructose-bisphosphatase 2	Homo sapiens	239-243
24063558-5	2013	Bisulphite genomic sequencing (BGS) in gastric cancer cell lines revealed that the FBP2 promoter region was densely methylated, and treatment of GC cells with the demethylation reagent, 5-aza-2-deoxycytidine (5-Aza), led to an increase in FBP2 expression.	Decitabine	209-214	fructose-bisphosphatase 2	Homo sapiens	83-87
23703029-6	2013	The PFK2 domain of PFK2/FBPase2 (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) regulates glycolysis to maintain the pyruvate pool for lactate synthesis.	Pyruvic Acid	124-132	fructose-bisphosphatase 2	Homo sapiens	24-31
23703029-6	2013	The PFK2 domain of PFK2/FBPase2 (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) regulates glycolysis to maintain the pyruvate pool for lactate synthesis.	Lactic Acid	142-149	fructose-bisphosphatase 2	Homo sapiens	24-31
22305745-9	2012	Because the glucokinase-PFK-2/FBPase-2 complex was conserved under LY2121260 treatment as shown by size exclusion chromatography a concerted action of both activators towards the closed active glucokinase conformation can be anticipated.	2-cyclohexyl-1-(4-methanesulfonylphenyl)cyclopropanecarboxylic acid thiazol-2-ylamide	67-76	fructose-bisphosphatase 2	Homo sapiens	30-38
22214556-7	2012	Glucose raises fructose 2,6-bisphosphate levels in hepatocytes by reversing the phosphorylation of PFK2/FBP2 at Ser32, but also independently of Ser32 dephosphorylation.	Glucose	0-7	fructose-bisphosphatase 2	Homo sapiens	104-108
23207906-6	2013	It was counteracted by selective depletion of fructose 2,6-bisphosphate with a bisphosphatase-active kinase-deficient variant of phosphofructokinase 2/fructosebisphosphatase 2, which prevented translocation of MondoA to the nucleus and recruitment to the PTG promoter.	fructose 2,6-diphosphate	46-71	fructose-bisphosphatase 2	Homo sapiens	151-175
22305745-5	2012	PFK-2/FBPase-2 but not LY2121260 antagonized glucokinase inhibition by the competitive glucokinase inhibitor mannoheptulose at increasing glucose concentrations.	Mannoheptulose	109-123	fructose-bisphosphatase 2	Homo sapiens	6-14
22305745-5	2012	PFK-2/FBPase-2 but not LY2121260 antagonized glucokinase inhibition by the competitive glucokinase inhibitor mannoheptulose at increasing glucose concentrations.	Glucose	138-145	fructose-bisphosphatase 2	Homo sapiens	6-14
22214556-4	2012	By using diverse substrates and inhibitors and a kinase-deficient bisphosphatase-active variant of the bifunctional enzyme PFK2/FBP2 (6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase), we demonstrate an essential role for fructose 2,6-bisphosphate in the induction of G6pc and other ChREBP target genes by glucose.	fructose 2,6-diphosphate	226-251	fructose-bisphosphatase 2	Homo sapiens	128-132
22214556-4	2012	By using diverse substrates and inhibitors and a kinase-deficient bisphosphatase-active variant of the bifunctional enzyme PFK2/FBP2 (6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase), we demonstrate an essential role for fructose 2,6-bisphosphate in the induction of G6pc and other ChREBP target genes by glucose.	Glucose	310-317	fructose-bisphosphatase 2	Homo sapiens	128-132