ライフサイエンスコーパス: OAA

1 OAA accumulation was also associated with decreased conv

2 OAA altered levels, distributions or post-translational

3 OAA increased Akt, mammalian target of rapamycin and P70

4 OAA is observed to bind in a number of different orienta

5 OAA lowered nuclear factor kappaB nucleus-to-cytoplasm r

6 OAA sugar binding was tested against Man-9 and various d

7 ce and all of the quenching that accompanies OAA binding.

8 dria, even in the absence of ADP, accumulate OAA and manifest limited respiration, similar to muscle

9 found that ACMSD catalyzes oxaloacetic acid (OAA) tautomerization at a rate of 6.51 +/- 0.42 s(-1) bu

10 d in the PEPCK-Mn2+, -Mn2+-oxaloacetic acid (OAA), -Mn2+-OAA-Mn2+-guanosine-5'-diphosphate (GDP), and

11 ntal factors play a major role in activating OAA to react with the carbanion of acetyl-CoA.

12 tural results explain the antiviral activity OAA and add to the growing body of knowledge about antiv

13 In addition, OAA and glutarate also bind to free enzyme as does lysin

14 Oscillatoria agardhii agglutinin (OAA) is a recently discovered cyanobacterial lectin that

15 rystalline Oscillatoria agardhii agglutinin (OAA), we demonstrate that judiciously designed 2D and 3D

16 lation of enzyme activity by acetylation and OAA accumulation at the substrate level are two strategi

17 cetyl-CoA, is able to convert acetyl-CoA and OAA to (3S)-citryl-CoA in the ASH domain, and can load C

18 In summary, GOT2 and OAA mediate complex II respiration and mitochondrial ene

19 ystematic evaluation of a variety of PEP and OAA analogues as potential reversible inhibitors of the

20 ilizing modes of recognition of both PEP and OAA in order to achieve a micromolar inhibition constant

21 on of the major receptor on the HIV virus by OAA.

22 erved in the corresponding type I chicken CS.OAA.CMX complex.

23 We observed decreased OAA, increased NADH/NAD(+), and increased succinate-supp

24 de evidence for membrane potential-dependent OAA accumulation in mitochondria during complex II-energ

25 itochondria is tempered by complex I-derived OAA in a manner dependent on UCP1.

26 automerase (OAT) activity that converts enol-OAA to the physiological keto-OAA form, and determined t

27 As for OAA, tight and specific binding to alpha3,alpha6-mannope

28 icate that Arg51 and Arg239* are crucial for OAA tautomerization.

29 as expected, affected the kcats and Kms for OAA and acetyl-CoA to varying degrees.

30 omplex I electron flow and is needed to form OAA.

31 ein behind the active site wall ca. 9 A from OAA, is responsible for the majority of the protein's in

32 euron counts and neurite length increased in OAA-treated mice.

33 hypothesis that deleting GOT2 would increase OAA concentrations, decrease complex II-energized respir

34 te revealed that increments in ADP increased OAA and caused a preferential use of glutamate for energ

35 complex II energized respiration, increased OAA, and decreased consumption of glutamate relative to

36 eurogenesis, we administered intraperitoneal OAA, 1-2 g/kg once per day for 1-2 weeks, to C57Bl/6 mic

37 structures of the unliganded enzyme and its OAA binary complex, hybrid quantum mechanics-molecular d

38 converts enol-OAA to the physiological keto-OAA form, and determined that it belongs to the highly c

39 Herein we focus on the anti-HIV lectin OAA from Oscillatoria agardhii: We show that in the abse

40 (cMDH) catalyzed oxidation/reduction of MAL/OAA.

41 or in nonphotosynthetic tissues, the malate-OAA shuttle was proposed to be mediated by the constitut

42 xCO(2), NICO, sweat conductance measurement, OAA/S, and the Aldrete score.

43 Apart from data for the founding member OAA, neither three-dimensional structures, information a

44 fold, resembling the founding family member, OAA, with minor differences in loop conformations.

45 In mice, OAA promotes brain mitochondrial biogenesis, activates t

46 The Mn2+-OAA and Mn2+-OAA-Mn2+GDP structures illustrate inner-sphere coordinat

47 CK-Mn2+, -Mn2+-oxaloacetic acid (OAA), -Mn2+-OAA-Mn2+-guanosine-5'-diphosphate (GDP), and -Mn2+-Mn2+-

48 In the PEPCK-Mn2+-OAA complex, an alternate bound conformation of OAA is p

49 The Mn2+-OAA and Mn2+-OAA-Mn2+GDP structures illustrate inner-sph

50 Comparison of the Mn2+-OAA-Mn2+GDP and Mn2+-Mn2+GTP structures illustrates a ma

51 (9 fold enrichments) for N-octylacetamide (N-OAA).

52 The substrates PEP and GTP, but not OAA, GDP, or CO2, offered full protection from inactivat

53 The overall architecture of OAA comprises 10 beta-strands that fold into a single, c

54 etitive inhibitors that mimic the binding of OAA (oxalate and phosphonoformate) coordinate directly t

55 molecule displaced by the C1 carboxylate of OAA is displaced by one of the gamma-phosphate oxygens o

56 ompetent binding mode, the C1 carboxylate of OAA is sandwiched between R87 and R405 in an environment

57 ition corresponding to the C1 carboxylate of OAA, and the edge-on aromatic interaction between a carb

58 complex, an alternate bound conformation of OAA is present.

59 Furthermore, during the conversion of OAA to PEP, the destabilization of the lid-closed confor

60 ures illustrate inner-sphere coordination of OAA to the manganese ion through the displacement of two

61 tate (OAA), a metabolically inactive form of OAA that is a strong inhibitor of succinate dehydrogenas

62 n corresponding to the C2 methylene group of OAA to facilitate interactions with R405, a carboxylate

63 uctural basis for the antiviral mechanism of OAA, we determined the structure of this lectin by x-ray

64 gh succinate dehydrogenase via regulation of OAA and consequent inhibition of succinate dehydrogenase

65 e specific carbohydrate recognition sites of OAA by NMR spectroscopy.

66 the observed isomerase activity of ACMSD on OAA and its structural similarity to ACMS, we propose th

67 The isomerase activity of ACMSD on OAA warrants further investigation in future biological

68 Oxaloacetate (OAA) is a central liver metabolite fundamental to critic

69 Oxaloacetate (OAA) is converted to aspartate by mitochondrial glutamic

70 Oxaloacetate (OAA), pyruvate, and glutarate behave as dead-end analogu

71 phosphoenolpyruvate (PEP) and oxaloacetate (OAA) by cytosolic phosphoenolpyruvate carboxykinase (cPE

72 erates photorespiratory CO2 as oxaloacetate (OAA).

73 genase oxidizes malate to enol-oxaloacetate (OAA), a metabolically inactive form of OAA that is a str

74 The decline resulted from oxaloacetate (OAA) accumulation and inhibition of succinate dehydrogen

75 To test how one intermediate, oxaloacetate (OAA) affects brain bioenergetics, insulin signaling, inf

76 dox) homeostasis is the malate-oxaloacetate (OAA) shuttle.

77 by conversion of mitochondrial oxaloacetate (OAA) to phosphoenolpyruvate, regulates glucose carbon fl

78 alysis revealed high levels of oxaloacetate (OAA) in RABV-infected mouse brains.

79 binary complex with substrate, oxaloacetate (OAA).

80 ucture of AaCS, complexed with oxaloacetate (OAA) and the inhibitor carboxymethyldethia-coenzyme A (C

81 ondensation of acetyl-CoA with oxaloacetate (OAA) to form citryl-CoA and the subsequent, slower hydro

82 ategy employing arginine residues to promote OAA isomerization.

83 we describe a novel approach to quantifying OAA in liver mitochondria.

84 pendent malate dehydrogenase (MDH) to reduce OAA to malate, thus regenerating the electron acceptor N

85 Our study also indicates the role OAA could play in neuronal protection by suppressing exc

86 (1)H-MRS showed OAA increased brain lactate, GABA and glutathione thereb

87 y the kcat/Km for the individual substrates, OAA and acetyl-CoA.

88 Finally, we confirmed that OAA could reduce excessive neuroinflammation in CVS-infe

89 ular dynamics (QM-MM) calculations show that OAA itself is the most likely quencher with the OAA carb

90 ent RABV strain infections and suggests that OAA treatment is a strategy to prevent neural damage dur

91 banion of that intermediate then attacks the OAA carbonyl to furnish citryl-CoA, the initial product.

92 .2% in the CAZ-AVI + ATM group vs 44% in the OAA group (P = .007).

93 Specifically, the OAA level in CVS-infected mouse brains was higher than t

94 tive electrostatic potential surrounding the OAA carbonyl within the enzymes' active site is essentia

95 itself is the most likely quencher with the OAA carbonyl as the electron acceptor.

96 However, understanding OAA metabolism in the liver has been limited because the

97 leading to cytosolic glucose carbon flow via OAA-malate-pyruvate and acetyl-CoA-fatty acid pathways i

98 change conformation and/or interactions when OAA binds.

99 lex II-energized respiration consistent with OAA inhibition of succinate dehydrogenase.

100 , and its active site residues interact with OAA and CMX in the same manner observed in the correspon

101 cow heart mitochondria an enzyme (OAT1) with OAA tautomerase (OAT) activity that converts enol-OAA to