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1 lmost abolished light-dependent reduction of fructose-1,6-bisphosphatase.
2 rically modulating the activity of cytosolic fructose-1,6-bisphosphatase.
3 n of the interface residues in porcine liver fructose-1,6-bisphosphatase.
4 etween the wild-type and the mutant forms of fructose-1,6-bisphosphatase.
5 ights into the conformational equilibrium of fructose-1,6-bisphosphatase.
6 in all known primary sequences of mammalian fructose-1,6-bisphosphatase.
7 ate and fructose 6-phosphate, thus bypassing fructose-1,6-bisphosphatase.
8 Gid complex, and triggers ubiquitination of fructose-1,6-bisphosphatase.
9 of 6-phosphofructo-1-kinase and inhibitor of fructose-1,6-bisphosphatase.
10 t of these, hcef1, was mapped to chloroplast fructose-1,6-bisphosphatase.
11 ssigned the protein's function as a class IV fructose-1,6-bisphosphatase.
12 s, including the fbp1(+) gene, which encodes fructose-1,6-bisphosphatase.
13 a(54) to leucine destabilizes the T-state of fructose-1,6-bisphosphatase.
14 that arises from within a single subunit 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 and determined that the gluconeogenic enzyme fructose-1,6-bisphosphatase 1 (FBP1) is uniformly deplet
21 luconeogenesis genes, such as FBP1 (encoding fructose-1,6-bisphosphatase 1) and ICL1 (encoding isocit
22 xylate) transporters, glucose-6-phosphatase, fructose-1,6-bisphosphatase, 12-lipoxygenase, and cycloo
23 and an inhibitor of the gluconeogenic enzyme fructose-1,6-bisphosphatase, 6-phosphofructo-2-kinase/fr
24 e-stimulated phosphorylation and turnover of fructose-1,6-bisphosphatase, a substrate of the cAMP-dep
25 activation of key enzymes of these pathways, fructose-1,6-bisphosphatase and ADP-glucose pyrophosphor
26 nt than wild-type Trx f in the activation of fructose-1,6-bisphosphatase and are altered in both S0.5
27 ent peaks in the temporal pattern of urinary fructose-1,6-bisphosphatase and glutathione-S-transferas
28 inary excretion of the renal tubular enzymes fructose-1,6-bisphosphatase and glutathione-S-transferas
29 enes, which encode the gluconeogenic enzymes fructose-1,6-bisphosphatase and phosphoenolpyruvate carb
31 ure between the canonical R- and T-states of fructose-1,6-bisphosphatase, and yet a dynamic loop esse
32 egulatory enzymes of gluconeogenesis such as fructose-1,6-bisphosphatase are degraded via the ubiquit
33 ly, two pathways of allosteric inhibition of fructose-1,6-bisphosphatase are possible, only one of wh
34 r could mimic an unknown natural effector of fructose-1,6-bisphosphatase, as it interacts strongly wi
35 drogenase and oxidized spinach chloroplastic fructose-1,6-bisphosphatase by wild-type Trx f, wild-typ
36 f residues in the C1-C4 (C2-C3) interface of fructose-1,6-bisphosphatase can significantly affect the
37 ductase), followed by cbbRII, cbbF (encoding fructose 1,6-bisphosphatase), cbbP (encoding phosphoribu
39 en showed consistently low levels of urinary fructose-1,6-bisphosphatase excretion over comparable pe
40 linoquinazolines as allosteric inhibitors of fructose-1,6-bisphosphatase (F16Bpase) are reported.
46 tal structures of metal-product complexes of fructose 1, 6-bisphosphatase (FBPase) reveal competition
47 ctive thiazole phosphonic acid inhibitors of fructose 1,6-bisphosphatase (FBPase) exhibited low oral
48 report the structure-guided design of potent fructose 1,6-bisphosphatase (FBPase) inhibitors that int
51 68, Lys71, Lys72, and Asp74 of porcine liver fructose-1, 6-bisphosphatase (FBPase) are conserved resi
52 atory enzyme in the gluconeogenesis pathway, fructose-1, 6-bisphosphatase (FBPase), is induced when S
53 to yeast cells that are starved for 3 days, fructose-1,6-bisphosphatase (FBPase) and malate dehydrog
54 tial amounts of the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) are in the extracel
56 enteric bacterium Escherichia coli requires fructose-1,6-bisphosphatase (FBPase) for growth on gluco
59 72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated
61 tory potency of the initial purine series of fructose-1,6-bisphosphatase (FBPase) inhibitors led to t
64 s between AMP domains in recombinant porcine fructose-1,6-bisphosphatase (FBPase) is explored by site
65 fresh glucose, the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is imported into Vi
72 ed targeting of the key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) to the vacuole for
73 2-MC isomer produced by GltA (2-MC(GltA)) is fructose-1,6-bisphosphatase (FBPase), a key enzyme in gl
74 sphoenolpyruvate carboxylase kinase (PEPCK), fructose-1,6-bisphosphatase (FBPase), and glucose-6-phos
75 the enzyme together with the better studied fructose-1,6-bisphosphatase (FBPase), in both cases from
76 degradation of the key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), in Saccharomyces c
78 with glucose, the key gluconeogenic enzyme, fructose-1,6-bisphosphatase (FBPase), is selectively tar
79 eriod of time, gluconeogenic enzymes such as fructose-1,6-bisphosphatase (FBPase), malate dehydrogena
84 f, spinach phosphoribulokinase (PRK) and the fructose-1,6-bisphosphatases (FBPase) from pea and spina
87 fructose-2, 6-bisphosphate concentrations on fructose-1,6-bisphosphatase gene expression were stimula
88 However, we observed that a mutant devoid of fructose-1,6-bisphosphatases grew normally on erythritol
91 es for mutants R15A, E19Q, R22K, and T27A of fructose-1,6-bisphosphatase; however, a 2-fold increase
93 mental changes in the catalytic mechanism of fructose-1,6-bisphosphatase in response to pH and differ
95 ibits gluconeogenesis by directly inhibiting fructose 1,6-bisphosphatase is based entirely on in vitr
98 three crystal structures of Leishmania major fructose-1,6-bisphosphatase (LmFBPase) along with enzyme
100 uctures of the wild-type and mutant forms of fructose-1, 6-bisphosphatase on the basis of CD data.
101 ose 2,6-bisphosphate (Fru-2,6-P2) on porcine fructose-1,6-bisphosphatase (pFBPase) and Escherichia co
104 in f and the regulatory sulfhydryl groups of fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosph
105 tator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the pr
106 nk specific interactions between subunits in fructose-1,6-bisphosphatase to observed properties of co
107 he sole C source should require aldolase and fructose-1,6-bisphosphatase to produce essential hexose-
109 ymes, phosphoenolpyruvate carboxykinase, and fructose-1,6-bisphosphatase was also down-regulated.
110 Glu-19, Arg-22, and Thr-27 of porcine liver fructose-1,6-bisphosphatase was carried out by site-dire
111 9 and Lys50 in the function of porcine liver fructose-1,6-bisphosphatase was explored by site-directe
112 higher activity of the gluconeogenic enzyme fructose-1,6-bisphosphatase when grown on glucose, glyce
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