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1                                              PGH(2) fits well into the IMN binding site by placing th
2                                              PGH(2)-G produced by macrophages is a substrate for cell
3                                              PGH2-like endoperoxides are intermediates in this pathwa
4 to prostaglandin (PG) G2 (catalytic step 1), PGH2 (catalytic step 2), and PGI2 (catalytic step 3).
5 cal sensing platform for prostaglandin H(2) (PGH(2)) as the basis for quantitation of pain.
6                          Prostaglandin H(2) (PGH(2)) formed from arachidonic acid is an unstable inte
7                          Prostaglandin H(2) (PGH(2)) formed from arachidonic acid is an unstable inte
8 arachidonic acid (AA) to prostaglandin H(2) (PGH(2)) in the committed step of prostaglandin biosynthe
9    The product of COX-2, prostaglandin H(2) (PGH(2)), can undergo spontaneous rearrangement and nonen
10                     Prostaglandin (PG) H(2) (PGH(2)), formed from arachidonic acid, is an unstable in
11 vert arachidonic acid to prostaglandin H(2) (PGH(2)), the committed step in prostaglandin and thrombo
12 vert the same substrate, prostaglandin H(2) (PGH(2)), to thromboxane A(2) and prostaglandin I(2), whi
13 ndin H synthases (PGHS), prostaglandin H(2) (PGH(2)), undergoes rearrangement to the highly reactive
14 lectrons to prostaglandin endoperoxide H(2) (PGH(2)).
15 achidonic acid (AA) into prostaglandin H(2) (PGH(2)).
16 ic TXA(2), TXA(2) mimetic (U-46619), TXB(2), PGH(2) mimetic (U-51605), PGD(2,) PGJ(2), and PGF(2alpha
17 f the crystal structure and mutation data, a PGH(2)-bound model structure was built.
18 landin (PG) I(2) (PGI(2), prostacyclin) is a PGH(2) metabolite with anti-inflammatory, antiproliferat
19 sozymes and terminal enzymes by developing a PGH2-divided model.
20                                    U46619, a PGH2/TxA2 mimetic, induced specific phosphorylation of b
21 ce between the heme and the protein, where a PGH2 might be able to bind.
22 reflect, in part, rediversion of accumulated PGH(2) to augment formation of PGI(2).
23 s, reflecting rediversion of the accumulated PGH(2) substrate in the double knockouts.
24 recursors, arachidonic acid (AA), PGG(2) and PGH(2).
25 uctures of PGFS containing PGF(2)(alpha) and PGH(2) were built.
26  or SQ 29,548 (10(-4) M), cyclooxygenase and PGH(2)/TXA(2) receptor antagonists, partially restored a
27 the intermediate endoperoxides, PGH(2)-G and PGH(2)-EA, to the corresponding prostacyclin derivatives
28 abinoid-derived COX-2 products, PGH(2)-G and PGH(2)-EA.
29 nhibits both the PGD(2) 11-ketoreductase and PGH(2) 9,11-endoperoxide reductase activities of PGFS.
30 ediate PGH2 by cyclooxygenase-2 (COX-2), and PGH2 undergoes an isomerization reaction to generate PGE
31            Further metabolism of PGH2-EA and PGH2-G by prostaglandin synthases produces a variety of
32 c parameters of TXAS-catalyzed reaction are: PGH2 bound TXAS at a rate of 1.2-2.0 x 10(7) M(-1) s(-1)
33       Using N(alpha)-acetylarginine and both PGH(2) and synthetic LGE(2), we discovered a novel serie
34 ngs question mechanisms of catalysis in both PGH2 synthases.
35 ynthase was far more efficient at catalyzing PGH(2) isomerization than at catalyzing the isomerizatio
36                      Given that the cellular PGH2 concentration is quite low, we concluded that under
37 rize the contribution of mPGES-1 to cellular PGH2 metabolism in murine macrophages by studying the sy
38 te kinetic study revealed that TXAS consumed PGH2 at a rate of 3,800 min(-1) and that the k(cat)/K(m)
39 ating the levels of a synthase that converts PGH(2) to PGD(2), the intracellular signaling proteins t
40 (mPGES1), which converts COX-1/COX-2-derived PGH(2) to PGE(2).
41 onic acid-derived prostaglandin endoperoxide PGH(2).
42 donic acid to the prostaglandin endoperoxide PGH2, from which all other prostaglandins are formed.
43 w a cell processes the unstable endoperoxide PGH2 during the inactivation of a major metabolic outlet
44 enase metabolite prostaglandin endoperoxide (PGH(2)).
45 he conversion of prostaglandin endoperoxide (PGH2) into thromboxane A2 (TxA2) which plays a crucial r
46 erization of the intermediate endoperoxides, PGH(2)-G and PGH(2)-EA, to the corresponding prostacycli
47 el lipid, prostaglandin H(2) glycerol ester (PGH(2)-G), in vitro and in cultured macrophages.
48 -ethanolamide (PGH2-EA) and -glycerol ester (PGH2-G), respectively.
49 ol (2-AG), to prostaglandin-H2-ethanolamide (PGH2-EA) and -glycerol ester (PGH2-G), respectively.
50 ES-2h has significant catalytic activity for PGH2 degradation.
51 f 3,800 min(-1) and that the k(cat)/K(m) for PGH2 consumption was 3 x 10(6) M(-1) s(-1).
52  the 15-hydroperoxyl group of PGG(2) to form PGH(2) catalyzed by the peroxidase activity.
53 (S)-1 catalyzes the formation of PGE(2) from PGH(2), a cyclooxygenase product that is derived from ar
54  activities: formation of PGF(2)(alpha) from PGH(2) by the PGH(2) 9,11-endoperoxide reductase activit
55 ta-PGF(2) from PGD(2) and PGF(2)(alpha) from PGH(2) in the presence of NADPH.
56              Formation of PGF(2)(alpha) from PGH(2) most likely involves a direct hydride transfer fr
57       Prostaglandin (PG) E(2) is formed from PGH(2) by a series of PGE synthase (PGES) enzymes.
58 ly all of the LG predicted to be formed from PGH2 can be accounted for as adducts of the PGH-synthase
59 tadecatrienoic acid and malondialdehyde from PGH2, but not formation of PGE2.
60     The first COX product, prostaglandin H2 (PGH2) is also a command substrate for other prostanoid e
61 in E synthases involved in prostaglandin H2 (PGH2) metabolism.
62 d peroxidase activities of prostaglandin H2 (PGH2) synthase I and II were monitored by stopped-flow s
63  molecular oxygen, it uses prostaglandin H2 (PGH2) to catalyze either an isomerization reaction to fo
64 ostaglandin E2 (PGE2) from prostaglandin H2 (PGH2).
65 arachidonic acid (AA) into prostaglandin H2 (PGH2).
66 und I and compound II observed with EtOOH in PGH2 synthase II suggest that peroxidative cleavage is n
67 bit the enzyme, and that diclofenac inhibits PGH(2) but not 15-hydroperoxyeicosatraenoic acid formati
68 ently converted to the unstable intermediate PGH2 by cyclooxygenase-2 (COX-2), and PGH2 undergoes an
69 e nonacetylated partner monomer forms mainly PGH(2) but only at 15 to 20% of the rate of native huPGH
70 n the presence of an enzyme that metabolizes PGH(2).
71 athways leading to LTB(4) and LTC(4) but not PGH(2) biosynthesis.
72 trated their formation after coincubation of PGH(2) with synthetic peptides and proteins.
73 and specifically catalyzes the conversion of PGH(2) to PGE(2).
74  from the bound NADPH to the endoperoxide of PGH(2) without the participation of specific amino acid
75 , respectively, of the rates of formation of PGH(2) by native PGHS-2.
76                                 Formation of PGH(2) involves an initial oxygenation of arachidonate t
77  PGI synthases catalyze the isomerization of PGH(2)-G at rates approaching those observed with PGH(2)
78 tion than at catalyzing the isomerization of PGH(2)-G.
79 tion data, a putative catalytic mechanism of PGH(2) 9,11-endoperoxide reductase of PGFS is proposed.
80        To examine the catalytic mechanism of PGH(2) 9,11-endoperoxide reductase, a crystal structure
81 y that these functions include metabolism of PGH(2) to PGE(2).
82  this study, we assessed whether reaction of PGH(2) with arginine yielded covalent adducts.
83 quivalent to the enzymatic transformation of PGH(2) to PGD(2).
84 hat specifically catalyzes the conversion of PGH2 to PGE2.
85 ) s(-1); the rate of catalytic conversion of PGH2 to TXA2 or MDA was at least 15,000 s(-1) and the lo
86 ting the prostaglandin pathway downstream of PGH2 synthesis and avoiding suppression of antithromboti
87           An important structural feature of PGH2 formed by COX is the trans-configuration of side ch
88  PGE synthases catalyze the isomerization of PGH2 into PGE2.
89 nthase (PGES) catalyzes the isomerization of PGH2 to PGE2.
90 tic function of PGIS in the isomerization of PGH2 to prostacyclin.
91                        Further metabolism of PGH2-EA and PGH2-G by prostaglandin synthases produces a
92                          During reactions of PGH2 synthase I with arachidonic acid (AA) and ethyl hyd
93                 However, during reactions of PGH2 synthase II with EtOOH, compound I and compound II
94 ter reaction of levuglandin E(2) (LGE(2)) or PGH(2) with lysine.
95  that recombinant Lac1 does not modify AA or PGH(2), but does have a marked activity toward PGG(2) co
96 gation response stimulated by thromboxane or PGH2 analogs.
97  of arachidonic acid to the PGI(2) precursor PGH(2) or other eicosanoids likely results in TP recepto
98  isomerization of the cyclooxygenase product PGH(2) into PGE(2).
99  the endocannabinoid-derived COX-2 products, PGH(2)-G and PGH(2)-EA.
100 ynthase catalyzes an isomerization reaction, PGH(2) to PGE(2).
101 ironment, was used to interact with a stable PGH(2) analog,.
102 impact to facilitate their common substrate, PGH(2), across the membrane into their active sites from
103 ure of the unstable TXAS and PGIS substrate, PGH(2).
104 ormation of PGF(2)(alpha) from PGH(2) by the PGH(2) 9,11-endoperoxide reductase activity and 9alpha,1
105 Data Bank suggests that IMN can fit into the PGH(2) binding site in various proteins.
106 ses (COXs), convert arachidonic acid (AA) to PGH2.
107 nase-2 (COX-2), converts arachidonic acid to PGH2 PGHS-2 is a conformational heterodimer composed of
108 talyze the conversion of arachidonic acid to PGH2.
109 ey step in the conversion of arachidonate to PGH2, the immediate substrate for a series of cell speci
110 HS peroxidase (POX) activity reduces PGG2 to PGH2.
111 en and a peroxidase that reduces the PGG2 to PGH2.
112                              Aspirin-treated PGH2 synthase II was found to produce 15-HETE, and the a
113                However, when aspirin-treated PGH2 synthase II was reacted with AA, a unique spectral
114                         When aspirin-treated PGH2 synthase II was reacted with EtOOH, a normal peroxi
115 btained for the bicycloendoperoxides U44069, PGH2, and U46619 (Ki = 29-39 nM).
116 )-G at rates approaching those observed with PGH(2).
117  with heme ligands in binding study and with PGH2 in enzymatic study.
118        Incubations of cells carried out with PGH2 demonstrated that PGE2 synthase activity was increa
119                        During reactions with PGH2 synthase II with AA, compound I and compound II wer
120 nal absorbance changes upon mixing TXAS with PGH2, indicating minimal accumulation of any heme-derive

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