ライフサイエンスコーパス: FRP

1 FRP denotes 4 quadrants of root planing performed within

2 FRP, which uses FMN as a cofactor to mediate the reducti

3 FRPs have been shown to interact with Wnt proteins and a

4 FRPs measured 24 to 72 hr after coronary ligation were 2

5 FRPs measured during acute ischemia shortened an average

6 f FMNH2 cofactor from FRP to luciferase in a FRP:luciferase noncovalent complex were retained by FRP-

7 An FRP derivative containing 2-thioFMN as the cofactor was

8 e structural similarities between FRG(F) and FRP(H) and between L(F) and L(H), direct flavin product

9 isms were determined for the FRG(F)-L(F) and FRP(H)-L(F) coupled reactions.

10 or transfer was detected for FRG(F)-L(F) and FRP(H)-L(F).

11 one treatment center indicated that FDIS and FRP attained greater therapeutic improvements than PDIS

12 gnificantly lesser cytotoxicity than LRP and FRP; further, the replacement of leucines with valines a

13 harveyi cellular contents of luciferase and FRP were estimated to be 172 and 3 microM, respectively.

14 .8077-0.9617) have been observed for TAC and FRP with antiradical activity and total phenolics conten

15 d 15-30 degrees C, the binding of FMN by apo-FRP was found to be noncooperative, exothermic, and prim

16 properties of binding of reduced FMN by apo-FRP were found to closely resemble those of FMN binding

17 he regulation of functional coupling between FRP(Vh) and luciferase, this study was carried out to ch

18 Both FRP and luciferase within FRP-alphabeta were catalytical

19 icated that similar results were attained by FRP with and without adjunctive chemotherapy.

20 F-alpha, and IL-6 in macrophages followed by FRP, VRP, and ARP.

21 d flavin mononucleotide (FMNH2) generated by FRP must be supplied, through either free diffusion or d

22 regulated at the post-translational level by FRP and/or oligomerization.

23 each was critical in the binding of NADPH by FRP.

24 dicated that the bioluminescence produced by FRP-alphabeta without added flavin was derived from dire

25 ast, other OCP families are not regulated by FRP.

26 iferase noncovalent complex were retained by FRP-alphabeta.

27 sponse bias as well as a smaller and delayed FRP (indicative of disrupted reward learning) and reduce

28 Wnt family members in early Xenopus embryos, FRP antagonized Wnt-dependent duplication of the embryon

29 Overexpression of a cDNA encoding FRP-50 in an FA(C) cell line resulted in partial correct

30 ted and characterized a novel fusion enzyme, FRP-alphabeta, in which FRP was fused to the luciferase

31 alysis has only been clearly established for FRP(Vh).

32 estigation of the mechanisms responsible for FRP inhibition revealed that FRP forms complexes with WN

33 V. harveyi luciferase but as a substrate for FRP(Vh) in the luciferase-coupled bioluminescent reactio

34 of a direct transfer of FMNH2 cofactor from FRP to luciferase in a FRP:luciferase noncovalent comple

35 Importantly, FRP-alphabeta gave a higher total quantum output without

36 Significant conformational changes in FRP upon binding of FMN were indicated.

37 ate fluorescence anisotropy of eosin-labeled FRP, it was shown that luciferase formed a complex at 1:

38 The labeled FRP in either the holo- or apoenzyme form was similar to

39 r the holo- nor the apoenzyme of the labeled FRP in the dimeric form was effective in complexing with

40 nes with the IVS4 + 4 A to T mutation lacked FRP-50.

41 At submicromolar levels, FRP-alphabeta was significantly more active than an equa

42 ty of FRP would be trapped in the luciferase/FRP complex.

43 on analysis, activity assays of FRP mutants, FRP:OCP docking simulations, and coimmunoprecipitation e

44 or apoenzyme form was similar to the native FRP in undergoing a monomer-dimer equilibrium.

45 higher than the 0.4 muM K(d) for the native FRP, whereas the k(cat) of these two variants were simil

46 Observed FRPs were used to infer action potential duration and T

47 d ESVs before and during coronary occlusion, FRP was -1.1+/-1.1 (+/-SD) mm Hg before versus 0.2+/-1.2

48 id conservation analysis, activity assays of FRP mutants, FRP:OCP docking simulations, and coimmunopr

49 a scheme that the reduced flavin cofactor of FRP is preferentially utilized by luciferase for light e

50 ffects of replacement of the FMN cofactor of FRP(H) and FRG(F) by 2-thioFMN were also characterized.

51 The bound FMN functions as a cofactor of FRP(Vh) in transferring reducing equivalents from NADPH

52 ther the apoenzyme or the holoenzyme form of FRP with K(d) values of 7 and 11 microM, respectively.

53 form, a tetramer, may be an inactive form of FRP.

54 lso discussed in relation to the function of FRP as a reduced flavin donor in the FRP-luciferase coup

55 There were no differences in serum levels of FRP and Dkk-1 between case subjects with incidence or pr

56 Baseline serum levels of FRP and Dkk-1 were measured by capture enzyme-linked imm

57 a trend for higher baseline serum levels of FRP to be associated with a reduced risk of incident RHO

58 There was no association of serum levels of FRP with progression of RHOA.

59 The vast majority of FRP would be trapped in the luciferase/FRP complex.

60 e kinetically deduced ping-pong mechanism of FRP is now supported by direct measurements of binding a

61 However, the kinetic mechanism of FRP was changed to a sequential pattern with a Km,FMN of

62 y more active than an equal molar mixture of FRP and luciferase in coupled bioluminescence without FM

63 in whereas bioluminescence from a mixture of FRP and luciferase with or without exogenously added fla

64 bound FMN in the reductive half-reaction of FRP(Vh).

65 Therefore, the overall catalytic reaction of FRP-alphabeta without any FMN addition closely mimics th

66 Hence, the reduction of FRP(Vh)-bound FMN is not the committed step in coupling

67 some other properties of a R203A variant of FRP(Vh) and an NADH/NADPH-utilizing flavin reductase fro

68 Our study suggests that aftereffects on FRP may be an emergent property of the system that canno

69 Here we report the expression of one FRP gene, Mfrzb1, in the rostral mesenchyme of the mandi

70 of administering full-mouth therapy (FDIS or FRP) is to eliminate or reduce bacterial reservoirs with

71 h a functional role may also exist for other FRP homologous proteins.

72 The Vibrio harveyi NADPH-FMN oxidoreductase (FRP) and the luciferase pair were chosen as a model for

73 Vibrio harveyi NADPH-FMN oxidoreductase (FRP) catalyzes flavin reduction by NADPH.

74 of Vibrio harveyi NADPH:FMN oxidoreductase (FRP) to luciferase for the coupled bioluminescence react

75 Vibrio harveyi NADPH:FMN oxidoreductase P (FRP(Vh)) is a homodimeric enzyme having a bound FMN per

76 harveyi NADPH-preferring flavin reductase P (FRP(H)) to the luciferase (L(H)) from the same bacterium

77 ), previously known as familial rectal pain (FRP, OMIM 167400), is an inherited disease causing inten

78 s to measure behavioral free-running period (FRP), and then PER2::LUC bioluminescence from SCN, splee

79 , ventricular functional refractory periods (FRPs) were measured at five to eight epicardial, intramu

80 peptides with leucine (LRP), phenylalanine (FRP), valine (VRP), and alanine (ARP) residues at these

81 isinfection (FDIS), full-mouth root planing (FRP), and partial-mouth disinfection (PDIS) to improve p

82 mutation expressed a 50-kD FAC polypeptides, FRP-50 (FAC-related protein), shown to be an amino termi

83 The feedback-related positivity (FRP) in response to reward feedback was used as a neural

84 nt capacity (TAC) and ferric reducing power (FRP) based on reactions with electrogenerated bromine an

85 A negative fully relaxed pressure (FRP) indicates the presence of restoring forces.

86 blished a functional recombinant production (FRP) system to produce pure and functional HIV-1 intersu

87 Prolonging FRPs in the same area caused T-wave inversion in lead X

88 The fluorescence recovery protein (FRP) detaches OCP1 from the PBS core, accelerating its b

89 protein, the fluorescence recovery protein (FRP), dislodges the active OCP(r) from the PBSs and acce

90 involves the fluorescence recovery protein (FRP).

91 he regulatory fluorescence recovery protein (FRP).

92 aling antagonists, Frizzled-related protein (FRP) and Dkk-1, are associated with the development and

93 two members of the Frizzled-related protein (FRP) gene family that are thought to encode antagonists

94 is protein, called Frizzled-related protein (FRP), was first identified as a heparin-binding polypept

95 Frizzled related proteins (FRPs) comprise a family of secreted molecules that conta

96 izzled receptors, Frizzled-related proteins (FRPs), which contain the cysteine-rich domain of Frizzle

97 kinases, including Tor1p, Tor2p, FRAP/RAFT, FRP/ATR, ATM, Mec1p, Rad3, and Tel1p, function in signal

98 brio harveyi luciferase and flavin reductase FRP are, together, a two-component monooxygenase couple.

99 brio harveyi NADPH-specific flavin reductase FRP follows a ping-pong mechanism but switches to a sequ

100 ted did not correlate with behavioral rhythm FRP.

101 Serum FRP levels were measured by enzyme-linked immunosorbent

102 the Arg200Trp minor allele had higher serum FRP levels than controls who were homozygous for the maj

103 women, whereas the highest quartile of serum FRP levels tended to be associated with a modest reducti

104 Shortening FRPs in the anterolateral wall of the ventricle increase

105 In biosynthetic studies, FRP was secreted but, like Wnts, tended to remain associ

106 similar to the dimeric form of Synechocystis FRP.

107 ally, we demonstrated by cotransfection that FRP forms complexes with a prototype frizzled.

108 We demonstrated that FRP antagonizes the Wnt-induced increase in uncomplexed

109 We showed further that FRP inhibits Wnt signaling in a paracrine mode using a T

110 These results indicate that FRP may function as an inhibitor of Wnt action during de

111 responsible for FRP inhibition revealed that FRP forms complexes with WNT-1 or WNT-2 through its CRD

112 FRPs containing different tags revealed that FRP itself forms complexes and that this ability is conf

113 The FRP acts to dissociate the OCP from the phycobilisomes b

114 The FRP of SCN samples was negatively correlated with the FR

115 The FRP of the four peripheral oscillators tested did not co

116 e binding of oxidized and reduced FMN by the FRP apoenzyme.

117 r back-conversion, lack of regulation by the FRP, a different oligomeric state (monomer compared to d

118 al recombination breakpoints from either the FRP system or dual infection cultures.

119 Moreover, for the FRP, FMN at concentrations over 2 microM significantly i

120 between C1 and gp41 regions either from the FRP system or from the dual infection culture, and very

121 er understanding the functions of FMN in the FRP holoenzyme, this study was undertaken to quantify an

122 tion of FRP as a reduced flavin donor in the FRP-luciferase couple.

123 e determined the 3D crystal structure of the FRP at 2.5 A resolution.

124 A 4.4-kb transcript of the FRP gene is present in many organs, both in the adult an

125 Remarkably, the FRP is found in two very different conformational and ol

126 Similar to the FRP(H)-L(H) couple, direct cofactor transfer was detecte

127 N samples was negatively correlated with the FRP of behavioral rhythms, replicating prior results in

128 gainst flavin substrate in reacting with the FRP reduced flavin cofactor.

129 Conceptually, full-mouth therapy (FRP or FDIS) could reduce the number of patient visits a

130 tion to NADPH binding, NADP(+) also bound to FRP(Vh) in either the oxidized (K(d) 180 microM) or redu

131 ant-by-quadrant root planing was compared to FRP or FDIS with regard to PD reduction, gains of clinic

132 if benefits induced beyond PDIS were due to FRP or administration of multifaceted intraoral chlorhex

133 d shown that those residues are essential to FRP activity.

134 CP1, including its regulation by Tolypothrix FRP, which we show is structurally similar to the dimeri

135 i are quite similar to that of the wild-type FRP(Vh), the reversal of the reduction of bound FMN was

136 cterize coupled luminescence reactions using FRP(H) and the Vibrio fischeri NAD(P)H-utilizing flavin

137 indings are consistent with a model by which FRP inhibits Wnt signaling through interactions with Wnt

138 novel fusion enzyme, FRP-alphabeta, in which FRP was fused to the luciferase alpha subunit.

139 The bound FMN co-isolated with FRP, while acting as a genuine cofactor in the single-en

140 nism, a complex formation of luciferase with FRP is essential, but until now, no evidence for such a

141 Transfection analysis with FRPs containing different tags revealed that FRP itself

142 Both FRP and luciferase within FRP-alphabeta were catalytically active.

143 In this work, FRP was labeled at 1:1 molar ratio with the fluorophore