Stereospecificity of Hydrogen Abstraction in the Conversion of Arachidonic Acid to 15R-HETE by Aspirin-treated Cyclooxygenase-2
Open Access
- 1 February 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (7) , 4743-4746
- https://doi.org/10.1074/jbc.275.7.4743
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The Binding of Arachidonic Acid in the Cyclooxygenase Active Site of Mouse Prostaglandin Endoperoxide Synthase-2 (COX-2)Journal of Biological Chemistry, 1999
- The Role of Arginine 120 of Human Prostaglandin Endoperoxide H Synthase-2 in the Interaction with Fatty Acid Substrates and InhibitorsPublished by Elsevier ,1999
- A 12 R -lipoxygenase in human skin: Mechanistic evidence, molecular cloning, and expressionProceedings of the National Academy of Sciences, 1998
- Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agentsNature, 1996
- Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2Nature Structural & Molecular Biology, 1996
- The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthaseNature Structural & Molecular Biology, 1995
- Mutation of serine‐516 in human prostaglandin G/H synthase‐2 to methionine or aspirin acetylation of this residue stimulates 15‐R‐HETE synthesisFEBS Letters, 1994
- The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1Nature, 1994
- Selectivity of nonsteroidal antiinflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase.Proceedings of the National Academy of Sciences, 1993
- [63] Argentation—high-pressure liquid chromatography of prostaglandins and monohydroxyeicosenoic acidsPublished by Elsevier ,1982