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- W2010394216 abstract "There are two isoenzymes of prostaglandin endoperoxide (PGH) synthase (cyclooxygenase) called PGH synthase-1 and -2 or COX I and II. Both isoenzymes catalyze the conversion of arachidonate to PGH2, the committed step in the formation of prostaglandins and thromboxane. PGH synthase-1 is expressed constitutively in most tissues whereas PGH synthase-2 expression is induced in a variety of cell types by treatment with growth factors, tumour promoters and/or cytokines. Although PGH-synthase-1 has long been thought to be the site of action of non-steroidal anti-inflammatory drugs (NSAIDs), recent evidence suggests that PGH synthase-2 is the actual target of NSAIDs acting in their anti-inflammatory capacity. PGH synthase isoenzymes differ in gene and protein structures and regulation of expression; the isoenzymes utilize similar amino acids in catalysis. Subtle differences in active site structure are apparent from sequence comparisons and measurements of interactions with common NSAIDs including aspirin. The tw..." @default.
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- W2010394216 title "Section Review: Pulmonary-Allergy, Dermatological, Gastrointestinal & Arthritis: Differential interactions of prostaglandin endoperoxide synthases with nonsteroidal anti-inflammatory drugs" @default.
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- W2010394216 doi "https://doi.org/10.1517/13543784.3.1.1" @default.
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