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1 ucible nitric oxide synthase), production of prostaglandin H(2) (i.e., cyclooxygenase 2), and regulat
2 a good electrochemical sensing platform for prostaglandin H(2) (PGH(2)) as the basis for quantitatio
5 oxygenases, convert arachidonic acid (AA) to prostaglandin H(2) (PGH(2)) in the committed step of pro
7 (PGHS-1 and -2) convert arachidonic acid to prostaglandin H(2) (PGH(2)), the committed step in prost
8 ), respectively, convert the same substrate, prostaglandin H(2) (PGH(2)), to thromboxane A(2) and pro
9 cid by the prostaglandin H synthases (PGHS), prostaglandin H(2) (PGH(2)), undergoes rearrangement to
16 d 2-AG oxygenation provides the novel lipid, prostaglandin H(2) glycerol ester (PGH(2)-G), in vitro a
17 the ability of COX-2 to efficiently generate prostaglandin H(2) glycerol ester, explaining, in part,
20 ly, as the conversion of arachidonic acid to prostaglandin H(2) requires two oxygenation and two cycl
27 rome P450 that catalyzes an isomerization of prostaglandin H(2), an endoperoxide, to prostacyclin.
28 talyze the conversion of arachidonic acid to prostaglandin H(2), the committed step in prostanoid syn
29 Cox-1) and Cox-2 convert arachidonic acid to prostaglandin H(2), the precursor of other prostaglandin
30 can also activate cyclooxygenases to produce prostaglandin H(2), which can form two specific isomers
31 In addition, synthetic levuglandin E(2) and prostaglandin H(2)-derived levuglandins produced pyrrole
32 cts formed by synthetic levuglandin E(2) and prostaglandin H(2)-derived levuglandins with lysine.
34 sing specific antibodies for human 15-Lox-1, prostaglandin H synthase (also called cyclooxygenase, Co
38 mmalian tissues is regulated at the level of prostaglandin H synthase (PGHS) cyclooxygenase catalysis
39 nt techniques to examine the distribution of prostaglandin H synthase (PGHS) in ovine astrocyte-enric
44 Peroxide-generated tyrosyl radicals in both prostaglandin H synthase (PGHS) isozymes have been demon
45 in hours after infection, and is mediated by prostaglandin H synthase (PGHS) products in animal model
50 dal antiinflammatory drugs and inhibitors of prostaglandin H synthase (PGHS)-2 by exhibiting little e
56 with both native and indomethacin-pretreated prostaglandin H synthase 1 (PGHS-1) were examined by low
57 e monotopic lumenal enzyme cyclooxygenase 1 (prostaglandin H synthase 1) that share this mechanism of
58 ucible cyclooxygenase (Cox-2), also known as prostaglandin H synthase 2 (PGH-2) is a key enzyme in th
59 d the hypothesis that abnormal expression of prostaglandin H synthase 2 (PHS-2), which can be induced
60 that C. parvum infection directly activates prostaglandin H synthase 2 expression and prostaglandin
69 nce electron reactions in enzymes, including prostaglandin H synthase, galactose oxidase, ribonucleot
70 ooxygenase (COX)-2, the inducible isoform of prostaglandin H synthase, has been implicated in the gro
71 -oxygenase 2 (COX2), an inducible isoform of prostaglandin H synthase, which mediates prostaglandin s
72 peroxidase and cyclooxygenase activities of prostaglandin H synthase-1 (PGHS-1) both become irrevers
73 radical generated in the peroxidase cycle of prostaglandin H synthase-1 (PGHS-1) can serve as the ini
74 cosubstrates for the peroxidase activity of prostaglandin H synthase-1 (PGHS-1) have been reported t
77 l middle dot)NO is catalytically consumed by prostaglandin H synthase-1 (PGHS-1) through acting as a
79 The method was successfully used to detect prostaglandin H synthase-1 and -2 (PGHS-1 and -2) in nor
82 Peroxides also induce radical formation in prostaglandin H synthase-2 (PGHS-2) and in PGHS-1 recons
83 t redox characteristics on the modulation of prostaglandin H synthase-2 (PGHS-2) in primary mouse cor
85 lted in a significant inhibition of monocyte prostaglandin H synthase-2 (PGHS-2), a pivotal enzyme in
87 e drugs block the cyclooxygenase activity of prostaglandin H synthase-2 (PGHS2), but do not affect th
89 gonucleotide or when the early response gene prostaglandin H synthase-2 mRNA was measured over the ti
90 radicals detected in the photosystem II and prostaglandin H synthase-2 systems strongly suggest a me
95 ct of oxygenation of arachidonic acid by the prostaglandin H synthases (PGHS), prostaglandin H(2) (PG
97 prostanoids is regulated by cyclooxygenases (prostaglandin H synthases), which catalyze the conversio
98 the covalent binding of reactive products of prostaglandin H-synthases (PGHSs) to the enzyme and to o
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