His primary areas of investigation include Biochemistry, Cyclooxygenase, Enzyme, Isozyme and Prostaglandin. His Molecular biology research extends to the thematically linked field of Biochemistry. His Cyclooxygenase research incorporates themes from Asparagine and Prostanoid.
His primary area of study in Enzyme is in the field of ATP synthase. The various areas that William L. Smith examines in his Isozyme study include Aspirin, Pharmacology, Nephrotoxicity and Cell biology. His study in Prostaglandin is interdisciplinary in nature, drawing from both Thromboxane, Regulation of gene expression and Arachidonic acid.
His main research concerns Biochemistry, Enzyme, Cyclooxygenase, Prostaglandin and ATP synthase. His Biochemistry research includes themes of Molecular biology and Stereochemistry. The concepts of his Enzyme study are interwoven with issues in Tyrosine and Mutant.
His studies deal with areas such as Microsome, Lipoxygenase and Epoxygenase as well as Cyclooxygenase. In his research, Biosynthesis is intimately related to Thromboxane, which falls under the overarching field of Prostaglandin. His work in ATP synthase tackles topics such as Heme binding which are related to areas like Amino acid.
His scientific interests lie mostly in Stereochemistry, Arachidonic acid, Biochemistry, Enzyme and ATP synthase. William L. Smith has included themes like Oxidoreductase, Ligand and Active site in his Stereochemistry study. The various areas that he examines in his Arachidonic acid study include Cyclooxygenase and Polyunsaturated fatty acid, Linoleic acid, Fatty acid.
His Biochemistry study frequently draws connections between adjacent fields such as Biophysics. His study in the field of Isozyme is also linked to topics like Monomer. His ATP synthase research integrates issues from Radical and Hydrogen peroxide.
William L. Smith focuses on Enzyme, Stereochemistry, Arachidonic acid, Cyclooxygenase and Active site. Enzyme is the subject of his research, which falls under Biochemistry. His Arachidonic acid study combines topics in areas such as Peroxidase and Hydrogen atom abstraction.
The study incorporates disciplines such as Inflammation, Regulation of gene expression, Aspirin and Isozyme in addition to Cyclooxygenase. William L. Smith works mostly in the field of Active site, limiting it down to topics relating to Binding site and, in certain cases, Prostaglandin H2, Protein subunit, Dimer and Isothermal titration calorimetry. His Prostaglandin research is multidisciplinary, relying on both Oxidoreductase, Fatty acid, Molecule, Oxygen and Pharmacology.
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Cyclooxygenases: Structural, cellular, and molecular biology
W. L. Smith;D. L. DeWitt;R. M. Garavito.
Annual Review of Biochemistry (2000)
Prostaglandin Endoperoxide H Synthases (Cyclooxygenases)-1 and −2
Smith Wl;Garavito Rm;DeWitt Dl.
Journal of Biological Chemistry (1996)
Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs.
Elizabeth A. Meade;William L. Smith;David L. DeWitt.
Journal of Biological Chemistry (1993)
Prostaglandin endoperoxide H synthases-1 and -2.
William L. Smith;David L. Dewitt.
Advances in Immunology (1996)
Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence.
David L. Dewitt;William L. Smith.
Proceedings of the National Academy of Sciences of the United States of America (1988)
Prostaglandin endoperoxide synthase : structure and catalysis
William L. Smith;Lawrence J. Marnett.
Biochimica et Biophysica Acta (1991)
Why there are two cyclooxygenase isozymes.
William L. Smith;Robert Langenbach.
Journal of Clinical Investigation (2001)
Different Intracellular Locations for Prostaglandin Endoperoxide H Synthase-1 and −2
Ikuo Morita;Melvin Schindler;Martha K. Regier;James C. Otto.
Journal of Biological Chemistry (1995)
Prostanoid biosynthesis and mechanisms of action
William L. Smith.
American Journal of Physiology-renal Physiology (1992)
Photolabeling of prostaglandin endoperoxide H synthase-1 with 3-trifluoro-3-(m-[125I]iodophenyl)diazirine as a probe of membrane association and the cyclooxygenase active site.
James C. Otto;William L. Smith.
Journal of Biological Chemistry (1996)
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