William L. Smith

ORCID: 0000-0001-8946-9400
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Research Areas
  • Inflammatory mediators and NSAID effects
  • Estrogen and related hormone effects
  • Eicosanoids and Hypertension Pharmacology
  • Pharmacogenetics and Drug Metabolism
  • Steroid Chemistry and Biochemistry
  • Integrated Circuits and Semiconductor Failure Analysis
  • Thermography and Photoacoustic Techniques
  • Silicon and Solar Cell Technologies
  • Fatty Acid Research and Health
  • Receptor Mechanisms and Signaling
  • Nitric Oxide and Endothelin Effects
  • Radioactive element chemistry and processing
  • X-ray Diffraction in Crystallography
  • Semiconductor materials and devices
  • Force Microscopy Techniques and Applications
  • Peroxisome Proliferator-Activated Receptors
  • Additive Manufacturing Materials and Processes
  • Spacecraft and Cryogenic Technologies
  • Semiconductor materials and interfaces
  • Cancer, Lipids, and Metabolism
  • Glass properties and applications
  • Additive Manufacturing and 3D Printing Technologies
  • Neuroscience and Neuropharmacology Research
  • Spacecraft Design and Technology
  • Ion Transport and Channel Regulation

Lawrence Livermore National Laboratory
1982-2023

Tulane University
2022

University of Michigan
2012-2021

University of California, Davis
2021

Lawrence Livermore National Security
2016-2021

Society for Neuroscience
2020

Allen Institute for Brain Science
2020

Medical Diagnostic Laboratories (United States)
2014-2016

Wayne State University
2016

Western Washington University
2016

Murine prostaglandin endoperoxide (PGH) synthase-1 and PGH synthase-2 expressed in cos-1 cells were found to be differentially sensitive inhibition by common nonsteroidal anti-inflammatory drugs (NSAIDs). Aspirin completely inhibited bis-oxygenation of arachidonate synthase-1; contrast, aspirin-treated metabolized primarily 15-hydroxyeicosatetraenoic acid (15-HETE) instead PGH2. ID50 values determined for a panel NSAIDs measuring instantaneous cyclooxygenase activity using an oxygen...

10.1016/s0021-9258(18)53294-4 article EN cc-by Journal of Biological Chemistry 1993-03-01

Prostaglandin G/H synthase (8,11,14-icosatrienoate, hydrogen-donor:oxygen oxidoreductase, EC 1.14.99.1) catalyzes the first step in formation of prostaglandins and thromboxanes, conversion arachidonic acid to prostaglandin endoperoxides G H. This enzyme is site action nonsteroidal anti-inflammatory drugs. We have isolated a 2.7-kilobase complementary DNA (cDNA) encompassing entire coding region from sheep vesicular glands. cDNA, cloned lambda gt 10 library prepared poly(A)+ RNA glands,...

10.1073/pnas.85.5.1412 article EN Proceedings of the National Academy of Sciences 1988-03-01

The subcellular locations of prostaglandin endoperoxide synthase-1 and −2 (PGHS-1 −2) were determined by quantitative confocal fluorescence imaging microscopy in murine 3T3 cells human bovine endothelial using immunocytofluorescence with isozyme-specific antibodies. In all the cell types examined, PGHS-1 immunoreactivity was found equally distributed endoplasmic reticulum (ER) nuclear envelope (NE). PGHS-2 also present ER NE. However, staining twice as concentrated NE ER. A histofluorescence...

10.1074/jbc.270.18.10902 article EN cc-by Journal of Biological Chemistry 1995-05-01

We developed an in vitro expression system for accurate kinetic analyses of the inhibition human prostaglandin H synthase isozymes (hPGHS-1 and -2) by nonsteroidal anti-inflammatory drugs (NSAIDs). Assays instantaneous which enzyme, 10 microM arachidonate, NSAID were mixed simultaneously used to determine apparent affinities 14 common NSAIDs hPGHS-1 hPGHS-2. All except salicylate had appreciable (IC50 < or = 100 microM) hPGHS-1. Most also exhibited toward hPGHS-2, but three prominent...

10.1016/s0022-3565(25)23861-7 article EN Journal of Pharmacology and Experimental Therapeutics 1994-11-01

Acetylation of Ser-530 sheep prostaglandin endoperoxide (PGG/H) synthase by aspirin causes irreversible inactivation the cyclooxygenase activity enzyme. To determine catalytic function hydroxyl group Ser-530, we used site-directed mutagenesis to replace with an alanine. Cos-1 cells transfected expression vectors containing native (Ser-530) or mutant (Ala-530) cDNAs for PGG/H expressed comparable and hydroperoxidase activities. Km values arachidonate (8 microM) ID50 reversible inhibition...

10.1016/s0021-9258(19)34105-5 article EN cc-by Journal of Biological Chemistry 1990-03-01

Dietary fish oil containing ω3 highly unsaturated fatty acids has cardioprotective and anti-inflammatory effects. Prostaglandins (PGs) thromboxanes are produced in vivo both from the ω6 acid arachidonic (AA) eicosapentaenoic (EPA). Certain beneficial effects of may result altered PG metabolism resulting increases EPA/AA ratios precursor phospholipids. Here we report vitro specificities prostanoid enzymes receptors toward EPA-derived, 3-series versus AA-derived, 2-series substrates products....

10.1074/jbc.m703169200 article EN cc-by Journal of Biological Chemistry 2007-05-23

We show that thermal wave detection and analysis can be performed, in a noncontact highly sensitive manner, through the dependence of sample optical reflectance on temperature. Applications to study microelectronic materials are illustrated by an example measuring thickness thin metal films.

10.1063/1.95794 article EN Applied Physics Letters 1985-06-01

Aspirin (acetylsalicylate) treatment of human (h) prostaglandin endoperoxide H synthase (PGHS)-1 expressed in cos-1 cells caused a time-dependent inactivation oxygenase activity. hPGHS-2 produced an enzyme which retained activity but formed exclusively 15-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE) instead PGH2. The 15-HETE was the 15R configuration. Km values for arachidonate native and aspirin-treated were about same suggesting that binds to both similar manner. If, as expected,...

10.1016/s0021-9258(17)36820-5 article EN cc-by Journal of Biological Chemistry 1994-05-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTOxygenation of polyunsaturated fatty acids during prostaglandin biosynthesis by sheep vesicular glandsWilliam L. Smith and William E. M. LandsCite this: Biochemistry 1972, 11, 17, 3276–3285Publication Date (Print):August 15, 1972Publication History Published online1 May 2002Published inissue 15 August 1972https://pubs.acs.org/doi/10.1021/bi00767a024https://doi.org/10.1021/bi00767a024research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00767a024 article EN Biochemistry 1972-08-15

An enzymic system of sheep vesicular gland which forms prostaglandins showed a time-dependent, concentration-dependent activation by phenol before full dioxygenase activity could be manifested. The process reversibly inhibited o-phenanthroline. Aspirin and indomethacin did not instantly inhibit the dioxygenase, but acted in manner to block synthetic an irreversible manner. enzyme preparation was protected from inhibitory action these drugs presence

10.1016/s0021-9258(19)34171-7 article EN cc-by Journal of Biological Chemistry 1971-11-01

Typically, mechanical metamaterial properties are programmed and set when the architecture is designed constructed, do not change in response to shifting environmental conditions or application requirements. We present a new class of architected materials called field responsive metamaterials (FRMMs) that exhibit dynamic control on-the-fly tunability enabled by careful design selection both material composition architecture. To demonstrate FRMM concept, we print complex structures composed...

10.1126/sciadv.aau6419 article EN cc-by-nc Science Advances 2018-12-07

Drawbacks of current carbon dioxide capture methods include corrosivity, evaporative losses and fouling. Separating the solvent from infrastructure effluent gases via microencapsulation provides possible solutions to these issues. Here we report materials that may enable low-cost energy-efficient flue gas. Polymer microcapsules composed liquid carbonate cores highly permeable silicone shells are produced by microfluidic assembly. This motif couples capacity selectivity sorbents with high...

10.1038/ncomms7124 article EN cc-by-nc-nd Nature Communications 2015-02-05
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