D
David S. Smith
Researcher at University of Limoges
Publications - 218
Citations - 11741
David S. Smith is an academic researcher from University of Limoges. The author has contributed to research in topics: Thermal conductivity & Ceramic. The author has an hindex of 47, co-authored 205 publications receiving 10875 citations. Previous affiliations of David S. Smith include Lucideon & University of Toronto.
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Pharmacological sensitivity of the articular capsule of the primary spines of Eucidaris tribuloides.
TL;DR: While ACh induced only a slight desensitization, CCh caused a long-lasting blockade of the stiffening effects of the cholinergic agonists, showing that the receptors for ACh have a site or sites that recognize the ester moieties of these molecules.
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Neck formation and role of particle-particle contact area in the thermal conductivity of green and partially sintered alumina ceramics
David S. Smith,Jorge Martinez Dosal,Siham Oummadi,Delphine Nouguier,Diana Vitiello,Arnaud Alzina,Benoît Nait-Ali +6 more
TL;DR: In this paper, a simplified model was developed to describe the effects of pore fraction, average grain size and the contact area between particles due to neck formation on the thermal conductivity of the green or partially sintered ceramic.
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Mechanism of the excitation-contraction uncoupling of frog skeletal muscle by formamide
TL;DR: It is concluded that the resulting alterations in the triad structure and function are re sponsible for the irreversibility of the FMD uncoupling action in these muscles.
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Evolution of Thermophysical Characteristics in Tin Oxide: From Pressed Powder Compact to Fired Porous Body
TL;DR: The thermal response of a ceramic body during firing will be controlled by its thermophysical characteristics, such as grain boundary formation and neck growth, which increase the contact area between particles as mentioned in this paper.
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Actin-myosin interaction: the role of myosin in determining the actin pattern in self-assembled hybrid contractile units
TL;DR: Self-assembly of actin-myosin filamentous complexes was assayed by polymerizing rabbit G-ADP actin on formed filaments of lobster myosin and the results show that the pattern and mode ofActin complexing is determined by the specific myosIn and the arrangement of the cross-bridges on the organized filament.