ライフサイエンスコーパス: OAA

1 OAA altered levels, distributions or post-translational

2 OAA increased Akt, mammalian target of rapamycin and P70

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

34 (9 fold enrichments) for N-octylacetamide (N-OAA).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

49 erates photorespiratory CO2 as oxaloacetate (OAA).

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

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

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

53 binary complex with substrate, oxaloacetate (OAA).

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

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

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

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

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

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

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

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

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

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

64 change conformation and/or interactions when OAA binds.

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