ライフサイエンスコーパス: prostaglandin H(2)

1 catalyze formation of an identical product, prostaglandin H2.

2 he rate of conversion of arachidonic acid to prostaglandin H2.

3 oxidase reaction reduces prostaglandin G2 to prostaglandin H2.

4 rostaglandin biosynthesis, the generation of prostaglandin H(2).

5 rome P450 that catalyzes an isomerization of prostaglandin H(2), an endoperoxide, to prostacyclin.

6 shifts the dose response curve for U46619, a prostaglandin H2 analogue, to the right.

7 9) inhibited platelet aggregation induced by prostaglandin H2 and the conversion of prostaglandin H2

8 ne synthase using the cyclooxygenase product prostaglandin H(2) as the substrate.

9 of the cyclooxygenase-derived endoperoxide, prostaglandin H2, avidly binds to proteins.

10 nd platelet aggregation, is synthesized from prostaglandin H(2) by thromboxane synthase (TXAS).

11 Synthesis of prostaglandin H2 by prostaglandin H synthase (PHS) resul

12 The cyclooxygenase-derived endoperoxide, prostaglandin H2, can undergo rearrangement to highly re

13 In addition, synthetic levuglandin E(2) and prostaglandin H(2)-derived levuglandins produced pyrrole

14 cts formed by synthetic levuglandin E(2) and prostaglandin H(2)-derived levuglandins with lysine.

15 the ability of COX-2 to efficiently generate prostaglandin H(2) ethanolamide.

16 e (AEA) and 2-arachidonylglycerol (2-AG), to prostaglandin-H2-ethanolamide (PGH2-EA) and -glycerol es

17 e cyclooxygenases (COX-1 and COX-2) generate prostaglandin H(2) from arachidonic acid (AA).

18 ted heme-containing homodimers that generate prostaglandin H(2) from arachidonic acid (AA).

19 d 2-AG oxygenation provides the novel lipid, prostaglandin H(2) glycerol ester (PGH(2)-G), in vitro a

20 the ability of COX-2 to efficiently generate prostaglandin H(2) glycerol ester, explaining, in part,

21 Prostaglandin H(2) has been demonstrated to rearrange to

22 ucible nitric oxide synthase), production of prostaglandin H(2) (i.e., cyclooxygenase 2), and regulat

23 (PGHSs) 1 and 2 convert arachidonic acid to prostaglandin H2 in the committed step of prostanoid bio

24 rate of conversion from arachidonic acid to prostaglandin H2 in the PR pathway.

25 her enhancing or suppressing the activity of prostaglandin H(2) isoforms (PGHS-1 and PGHS-2).

26 sed to determine the docking of a substrate (prostaglandin H2) mimic (U46619) to the engineered prost

27 a good electrochemical sensing platform for prostaglandin H(2) (PGH(2)) as the basis for quantitatio

28 Prostaglandin H(2) (PGH(2)) formed from arachidonic acid

29 Prostaglandin H(2) (PGH(2)) formed from arachidonic acid

30 oxygenases, convert arachidonic acid (AA) to prostaglandin H(2) (PGH(2)) in the committed step of pro

31 The product of COX-2, prostaglandin H(2) (PGH(2)), can undergo spontaneous rea

32 (PGHS-1 and -2) convert arachidonic acid to prostaglandin H(2) (PGH(2)), the committed step in prost

33 ), respectively, convert the same substrate, prostaglandin H(2) (PGH(2)), to thromboxane A(2) and pro

34 cid by the prostaglandin H synthases (PGHS), prostaglandin H(2) (PGH(2)), undergoes rearrangement to

35 the conversion of arachidonic acid (AA) into prostaglandin H(2) (PGH(2)).

36 The first COX product, prostaglandin H2 (PGH2) is also a command substrate for

37 everal prostaglandin E synthases involved in prostaglandin H2 (PGH2) metabolism.

38 the dioxygenase and peroxidase activities of prostaglandin H2 (PGH2) synthase I and II were monitored

39 for a reductase or molecular oxygen, it uses prostaglandin H2 (PGH2) to catalyze either an isomerizat

40 he formation of prostaglandin E2 (PGE2) from prostaglandin H2 (PGH2).

41 the conversion of arachidonic acid (AA) into prostaglandin H2 (PGH2).

42 However, neither a thromboxane A2/prostaglandin H2 receptor antagonist SQ29548 and a throm

43 Furthermore, SQ29548, a thromboxane A2/prostaglandin H2 receptor antagonist, significantly redu

44 -dependent PGIS nitration and thromboxane A2/prostaglandin H2 receptor stimulation.

45 OX-2) (indomethacin or celecoxib) or of TXA2/prostaglandin H2 receptors (SQ-29548).

46 ly, as the conversion of arachidonic acid to prostaglandin H(2) requires two oxygenation and two cycl

47 y prostaglandin synthases of the accumulated prostaglandin H(2) substrate.

48 It has been shown to target prostaglandin H(2) synthase (COX)-1 and COX-2, which cat

49 block prostanoid biosynthesis by inhibiting prostaglandin H(2) synthase (EC 1.14.99.1).

50 have been shown to both activate and inhibit prostaglandin H(2) synthase 1 (PGHS-1).

51 We present here crystal structures of prostaglandin H(2) synthase-1 in complex with the inhibi

52 The response of the inducible isoform of the prostaglandin H2 synthase (COX-2) and the c-Jun N-termin

53 Prostaglandin H2 synthase (EC 1.14.99.1) is an integral

54 looxygenase activity of the membrane protein prostaglandin H2 synthase isoform 1 (PGHS-1) is the targ

55 resolution X-ray crystal structure of ovine prostaglandin H2 synthase-1 in complex with alpha-methyl

56 Prostaglandin H(2) synthesis by prostaglandin endoperoxi

57 talyze the conversion of arachidonic acid to prostaglandin H(2), the committed step in prostanoid syn

58 Cox-1) and Cox-2 convert arachidonic acid to prostaglandin H(2), the precursor of other prostaglandin

59 Free arachidonate is converted to prostaglandin H2, the common precursor to all prostanoid

60 The conversion of exogenous prostaglandin H2 to prostaglandin E2 was only modestly i

61 these cells efficiently converted exogenous prostaglandin H2 to prostaglandin E2.

62 ed by prostaglandin H2 and the conversion of prostaglandin H2 to thromboxane A2 in intact platelets.

63 e enzyme that catalyzes the isomerization of prostaglandin H2 to thromboxane A2.

64 ificantly alter beta 2-AR and thromboxane A2/prostaglandin H2 (TP) receptor affinity.

65 c (S > > R) and antagonism at thromboxane A2/prostaglandin H2 (TP; R > > S) receptors.

66 can also activate cyclooxygenases to produce prostaglandin H(2), which can form two specific isomers

67 enase-2, both metabolize arachidonic acid to prostaglandin H2, which is subsequently processed by dow