Results 221 to 230 of about 23,800,079 (261)
A novel deep learning radiopathomics model for predicting carcinogenesis promotor cyclooxygenase-2 expression in common bile duct in children with pancreaticobiliary maljunction: a multicenter study. [PDF]
Insights ImagingMao HM, Zhang JJ, Zhu B, Guo WL.
europepmc +1 more source
Can Bisphenols Alter the Inflammation Process? [PDF]
Life (Basel)Bazany D +6 more
europepmc +1 more source
Expression of Cyclooxygenase-1 and Cyclooxygenase-2 in the human prostate [PDF]
Urology, 2000 To determine the cell-specific expression of the two major isoforms of cyclooxygenase (COX-1 and COX-2) in human noncancerous and cancerous prostatic tissues.Thirty-one specimens of prostate carcinoma (CaP) and 10 specimens of benign prostatic hyperplasia (BPH) were stained with mouse antihuman COX-1 and COX-2 monoclonal antibodies.
Pamela D. Unger +6 more
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Annual Review of Pharmacology and Toxicology, 1998
▪ Abstract Cyclooxygenase (COX), first purified in 1976 and cloned in 1988, is the key enzyme in the synthesis of prostaglandins (PGs) from arachidonic acid. In 1991, several laboratories identified a product from a second gene with COX activity and called it COX-2.
Y. S. Bakhle +2 more
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▪ Abstract Cyclooxygenase (COX), first purified in 1976 and cloned in 1988, is the key enzyme in the synthesis of prostaglandins (PGs) from arachidonic acid. In 1991, several laboratories identified a product from a second gene with COX activity and called it COX-2.
Y. S. Bakhle +2 more
openaire +3 more sources
European Journal of Pharmacology, 1998
The anti-inflammatory activity of drugs more selective for cyclooxgenase isoform inhibition (cyclooxygenase 1, cyclooxygenase 2), were compared in rat carrageenin-induced pleurisy. Suppression of inflammation by cyclooxygenase 2-selective inhibitors, NS-398 (N-[-2-cyclohexyloxy]-4-nitrophenyl methanesulphonamide) and nimesulide (4-nitro-2-phenoxy ...
Annette Tomlinson +2 more
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The anti-inflammatory activity of drugs more selective for cyclooxgenase isoform inhibition (cyclooxygenase 1, cyclooxygenase 2), were compared in rat carrageenin-induced pleurisy. Suppression of inflammation by cyclooxygenase 2-selective inhibitors, NS-398 (N-[-2-cyclohexyloxy]-4-nitrophenyl methanesulphonamide) and nimesulide (4-nitro-2-phenoxy ...
Annette Tomlinson +2 more
openaire +3 more sources
Cyclooxygenase-1 and -2 isoenzymes
The International Journal of Biochemistry & Cell Biology, 1999The cyclooxygenase isoenzymes (COX-1 and -2) catalyze the rate-limiting steps in prostanoid biosynthesis. COX-1 and -2 genes encode two isoenzymes with overlapping yet distinct expression patterns and functions. Physiologically, various extracellular stimuli such as growth factors, cytokines and tumor promoters regulate the expression of COX-1 and -2 ...
David Bishop-Bailey +4 more
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Cyclooxygenase‐1 and Cyclooxygenase‐2 Inhibition of Novel 1,2‐Disubstituted Imidazoles.
ChemInform, 2005AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Norbert Handler +3 more
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Journal of Medicinal Chemistry, 2013
3-(5-Chlorofuran-2-yl)-5-methyl-4-phenylisoxazole (P6), a known selective cyclooxygenase-1 (COX-1) inhibitor, was used to design a new series of 3,4-diarylisoxazoles in order to improve its biochemical COX-1 selectivity and antiplatelet efficacy ...
P. Vitale +10 more
semanticscholar +1 more source
3-(5-Chlorofuran-2-yl)-5-methyl-4-phenylisoxazole (P6), a known selective cyclooxygenase-1 (COX-1) inhibitor, was used to design a new series of 3,4-diarylisoxazoles in order to improve its biochemical COX-1 selectivity and antiplatelet efficacy ...
P. Vitale +10 more
semanticscholar +1 more source
Cloning and Expression of Cyclooxygenase-1 and Cyclooxygenase-2
2010Cyclooxygenase (COX) enzymes play important roles in normal physiology and during inflammation of various cells and tissues. In order to help understand the functions of these enzymes, their genes can be cloned to facilitate the production of the proteins in recombinant form.
Beverly A. Reitz, Nicholas R. Staten
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