ライフサイエンスコーパス: fructose-1,6-bisphosphatase

1 n of the interface residues in porcine liver fructose-1,6-bisphosphatase.

2 etween the wild-type and the mutant forms of fructose-1,6-bisphosphatase.

3 ights into the conformational equilibrium of fructose-1,6-bisphosphatase.

4 in all known primary sequences of mammalian fructose-1,6-bisphosphatase.

5 rically modulating the activity of cytosolic fructose-1,6-bisphosphatase.

6 ate and fructose 6-phosphate, thus bypassing fructose-1,6-bisphosphatase.

7 Gid complex, and triggers ubiquitination of fructose-1,6-bisphosphatase.

8 of 6-phosphofructo-1-kinase and inhibitor of fructose-1,6-bisphosphatase.

9 t of these, hcef1, was mapped to chloroplast fructose-1,6-bisphosphatase.

10 ssigned the protein's function as a class IV fructose-1,6-bisphosphatase.

11 s, including the fbp1(+) gene, which encodes fructose-1,6-bisphosphatase.

12 a(54) to leucine destabilizes the T-state of fructose-1,6-bisphosphatase.

13 that arises from within a single subunit of fructose-1,6-bisphosphatase.

14 lmost abolished light-dependent reduction of fructose-1,6-bisphosphatase.

15 eric binding site located near the center of fructose-1,6-bisphosphatase.

16 bstrate inhibition dominates the kinetics of fructose-1,6-bisphosphatase.

17 d more mRNA for the tetraspanin CD53 and for fructose-1,6-bisphosphatase.

18 1 gene that encodes the gluconeogenic enzyme fructose-1,6-bisphosphatase.

19 the details suggest a closer relationship to fructose 1,6-bisphosphatases.

20 te-specific loss of the gluconeogenic enzyme fructose 1,6-bisphosphatase 1 (FBP1) disrupts liver meta

21 y discovered that liver-specific deletion of fructose-1, 6-bisphosphatase 1 (FBP1), a gluconeogenic e

22 moylphosphate synthase, fumarylacetoacetase, fructose-1,6-bisphosphatase 1 (FBP1) across cohorts achi

23 Here we identified the gluconeogenic enzyme fructose-1,6-bisphosphatase 1 (FBP1) as a p53 target tha

24 and determined that the gluconeogenic enzyme fructose-1,6-bisphosphatase 1 (FBP1) is uniformly deplet

25 in normal hepatocytes induces PERK-mediated fructose-1,6-bisphosphatase 1 (FBP1) S170 phosphorylatio

26 wnregulated that of a key glycolytic enzyme, fructose-1,6-bisphosphatase 1 (FBP1).

27 atocytes and hepatic metabolomics identified fructose-1,6-bisphosphatase 1 and glycolysis as PTPRK ta

28 luconeogenesis genes, such as FBP1 (encoding fructose-1,6-bisphosphatase 1) and ICL1 (encoding isocit

29 xylate) transporters, glucose-6-phosphatase, fructose-1,6-bisphosphatase, 12-lipoxygenase, and cycloo

30 and an inhibitor of the gluconeogenic enzyme fructose-1,6-bisphosphatase, 6-phosphofructo-2-kinase/fr

31 e-stimulated phosphorylation and turnover of fructose-1,6-bisphosphatase, a substrate of the cAMP-dep

32 activation of key enzymes of these pathways, fructose-1,6-bisphosphatase and ADP-glucose pyrophosphor

33 nt than wild-type Trx f in the activation of fructose-1,6-bisphosphatase and are altered in both S0.5

34 ent peaks in the temporal pattern of urinary fructose-1,6-bisphosphatase and glutathione-S-transferas

35 inary excretion of the renal tubular enzymes fructose-1,6-bisphosphatase and glutathione-S-transferas

36 enes, which encode the gluconeogenic enzymes fructose-1,6-bisphosphatase and phosphoenolpyruvate carb

37 Determinations of chloroplast fructose-1,6-bisphosphatase and sedoheptulose-1,7-bispho

38 ure between the canonical R- and T-states of fructose-1,6-bisphosphatase, and yet a dynamic loop esse

39 egulatory enzymes of gluconeogenesis such as fructose-1,6-bisphosphatase are degraded via the ubiquit

40 ly, two pathways of allosteric inhibition of fructose-1,6-bisphosphatase are possible, only one of wh

41 r could mimic an unknown natural effector of fructose-1,6-bisphosphatase, as it interacts strongly wi

42 drogenase and oxidized spinach chloroplastic fructose-1,6-bisphosphatase by wild-type Trx f, wild-typ

43 f residues in the C1-C4 (C2-C3) interface of fructose-1,6-bisphosphatase can significantly affect the

44 ductase), followed by cbbRII, cbbF (encoding fructose 1,6-bisphosphatase), cbbP (encoding phosphoribu

45 Three different hybrid tetramers of fructose-1,6-bisphosphatase, composed of one wild-type s

46 en showed consistently low levels of urinary fructose-1,6-bisphosphatase excretion over comparable pe

47 linoquinazolines as allosteric inhibitors of fructose-1,6-bisphosphatase (F16Bpase) are reported.

48 The enzyme fructose-1,6-bisphosphatase (FBP) is key regulatory poin

49 Silencing expression of fructose-1,6-bisphosphatases (FBP) in brain metastatic c

50 ation at phosphofructokinase-1 (PFK1) and/or fructose 1,6-bisphosphatase (FBP1) in association with a

51 Down-regulation of fructose-1,6-bisphosphatase (FBP1) in gluconeogenesis in

52 Fructose-1,6-bisphosphatase (FBP1) is a rate-limiting en

53 ssion of the metabolic tumor suppressor gene fructose-1,6-bisphosphatase (FBP1), epigenetically repre

54 gase mediates glucose-induced degradation of fructose-1,6-bisphosphatase (Fbp1), malate dehydrogenase

55 nd reexpression of a gluconeogenesis enzyme, fructose-1,6-bisphosphatase (FBP1), was found to inhibit

56 te carboxykinase (PCK1) and between MDH2 and fructose-1,6-bisphosphatase (FBP1).

57 tal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition

58 ctive thiazole phosphonic acid inhibitors of fructose 1,6-bisphosphatase (FBPase) exhibited low oral

59 report the structure-guided design of potent fructose 1,6-bisphosphatase (FBPase) inhibitors that int

60 ies of nucleoside monophosphate analogues as fructose 1,6-bisphosphatase (FBPase) inhibitors.

61 ibitors, we targeted the AMP binding site of fructose 1,6-bisphosphatase (FBPase).

62 68, Lys71, Lys72, and Asp74 of porcine liver fructose-1, 6-bisphosphatase (FBPase) are conserved resi

63 atory enzyme in the gluconeogenesis pathway, fructose-1, 6-bisphosphatase (FBPase), is induced when S

64 to yeast cells that are starved for 3 days, fructose-1,6-bisphosphatase (FBPase) and malate dehydrog

65 hat co-localized with IVC markers, including fructose-1,6-bisphosphatase (FBPase) and the vacuole imp

66 tial amounts of the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) are in the extracel

67 Residues 1--10 of porcine fructose-1,6-bisphosphatase (FBPase) are poorly ordered

68 enteric bacterium Escherichia coli requires fructose-1,6-bisphosphatase (FBPase) for growth on gluco

69 Allosteric activation of fructose-1,6-bisphosphatase (FBPase) from Escherichia co

70 Fructose-1,6-bisphosphatase (FBPase) governs a key step

71 72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated

72 Wild-type porcine fructose-1,6-bisphosphatase (FBPase) has no tryptophan r

73 tory potency of the initial purine series of fructose-1,6-bisphosphatase (FBPase) inhibitors led to t

74 Liver fructose-1,6-bisphosphatase (FBPase) is a regulatory enz

75 The gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is degraded in the

76 s between AMP domains in recombinant porcine fructose-1,6-bisphosphatase (FBPase) is explored by site

77 fresh glucose, the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is imported into Vi

78 The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is induced when Sac

79 The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is subjected to cat

80 Fructose-1,6-bisphosphatase (FBPase) is synthesized in y

81 Fructose-1,6-bisphosphatase (FBPase) is targeted to the

82 The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is targeted to Vid

83 Fructose-1,6-bisphosphatase (FBPase) operates at a contr

84 ed targeting of the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) to the vacuole for

85 2-MC isomer produced by GltA (2-MC(GltA)) is fructose-1,6-bisphosphatase (FBPase), a key enzyme in gl

86 um patens was found to be similar to that of fructose-1,6-bisphosphatase (FBPase), an enzyme involved

87 sphoenolpyruvate carboxylase kinase (PEPCK), fructose-1,6-bisphosphatase (FBPase), and glucose-6-phos

88 the enzyme together with the better studied fructose-1,6-bisphosphatase (FBPase), in both cases from

89 degradation of the key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), in Saccharomyces c

90 The key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), is induced when Sa

91 with glucose, the key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), is selectively tar

92 eriod of time, gluconeogenic enzymes such as fructose-1,6-bisphosphatase (FBPase), malate dehydrogena

93 Fructose-1,6-bisphosphatase (FBPase), the key enzyme in

94 fects of monovalent cations on porcine liver fructose-1,6-bisphosphatase (FBPase).

95 entify potential inhibitor lead compounds of fructose-1,6-bisphosphatase (FBPase).

96 limiting enzymes within this pathway such as fructose-1,6-bisphosphatase (FBPase).

97 f, spinach phosphoribulokinase (PRK) and the fructose-1,6-bisphosphatases (FBPase) from pea and spina

98 AMP transforms fructose-1,6-bisphosphatase from its active R-state to i

99 The role of the 190's loop of fructose-1,6-bisphosphatase (Fru-1, 6-P2ase) in the allo

100 fructose-2, 6-bisphosphate concentrations on fructose-1,6-bisphosphatase gene expression were stimula

101 However, we observed that a mutant devoid of fructose-1,6-bisphosphatases grew normally on erythritol

102 Crystals of fructose-1,6-bisphosphatase grow from an equilibrium mix

103 The gluconeogenic enzyme fructose-1,6-bisphosphatase has been proposed as a poten

104 es for mutants R15A, E19Q, R22K, and T27A of fructose-1,6-bisphosphatase; however, a 2-fold increase

105 e three of five possible hybrid tetramers of fructose-1,6-bisphosphatase in high purity.

106 mental changes in the catalytic mechanism of fructose-1,6-bisphosphatase in response to pH and differ

107 te carboxykinase, glucose-6-phosphatase, and fructose 1,6-bisphosphatase, in RLIP76(-/-).

108 ibits gluconeogenesis by directly inhibiting fructose 1,6-bisphosphatase is based entirely on in vitr

109 Fructose-1,6-bisphosphatase is a square planar tetramer

110 Here, the interaction of Tl+ with fructose-1,6-bisphosphatase is explored under conditions

111 three crystal structures of Leishmania major fructose-1,6-bisphosphatase (LmFBPase) along with enzyme

112 Loop 52-72 of porcine fructose-1,6-bisphosphatase may play a central role in t

113 uctures of the wild-type and mutant forms of fructose-1, 6-bisphosphatase on the basis of CD data.

114 ose 2,6-bisphosphate (Fru-2,6-P2) on porcine fructose-1,6-bisphosphatase (pFBPase) and Escherichia co

115 Fructose-1,6-bisphosphatase requires a divalent metal ca

116 Fructose-1,6-bisphosphatase requires divalent cations (M

117 in f and the regulatory sulfhydryl groups of fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosph

118 tator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the pr

119 nk specific interactions between subunits in fructose-1,6-bisphosphatase to observed properties of co

120 he sole C source should require aldolase and fructose-1,6-bisphosphatase to produce essential hexose-

121 The structural transformation of fructose-1,6-bisphosphatase upon binding of the alloster

122 ymes, phosphoenolpyruvate carboxykinase, and fructose-1,6-bisphosphatase was also down-regulated.

123 Glu-19, Arg-22, and Thr-27 of porcine liver fructose-1,6-bisphosphatase was carried out by site-dire

124 9 and Lys50 in the function of porcine liver fructose-1,6-bisphosphatase was explored by site-directe

125 higher activity of the gluconeogenic enzyme fructose-1,6-bisphosphatase when grown on glucose, glyce