346 resultados para Èze


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[Moses Schulbaum ; J. L. Bensew]

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von Moses Schulbaum

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vel verbis J. L. Bensew ; bearb. von Moses Schulbaum

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ze has-sēfer hoṭ meḥabbēr gwezn ... Mōše Kahanā ...

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hak-kōl ḥûbbār mē'ētî haṣ-ṣāʿîr Dôv Ber Ze'ēv Wôlf Lîvšîṣ

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Este artículo analiza la relación entre la eficiencia productiva y las Redes Sociales Virtuales (RSV) en las empresas de telecomunicaciones en España. En una primera etapa, se aplica el análisis envolvente de datos (DEA) incorporando varios indicadores de actividad ?Social Media?. En una segunda etapa, se utiliza una regresión logística para caracterizar las empresas eficientes. Los resultados muestran que la capacidad de absorción y utilización de las RSV es un factor determinante en la mejora de la eficiencia productiva. La utilización combinada y las distintas capacidades de gestión de las RSV permiten identificarlas como un recurso heterogéneo. Este trabajo presenta un modelo para la evaluación del desempeño estratégico al abordar su presencia y actividad en RSV. ABSTRACT. This paper analyzes the relationship between the productive efficiency and the Online Social Networks - OSN in the Spanish telecommunications firms. First, a data envelopment analysis (DEA) is used and several indicators of business "Social Media" activities are incorporated. In a second stage, a logistic regression model regression is applied to characteri ze the efficient enterprises. Results show that the company's ability to absorb and utilize this OSN is a key factor in improving the productive efficiency. These results on the combined use and different management capabilities of OSN point to a definitio n of OSN as a heterogeneous resource. This paper presents a model for assessing the strategic performance to address their presence and activity in OSN.

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During the last years many researchers have been working on the active matching or on non-Foster matching networks for one- and two-port electrically small antennas (ESAs). A new parameter on the sensitivity of the two-port electrically small antenna when loaded with a non-F oster network is presented. This sensitivity analysis will allow us to choose what kind of antennas can be properly matched with non-Foster networks and their position in order to optimi ze the performance of the design. Then, a typical high Q two-port antenna will be harder to match over a broad bandwidth, since |S21| is very small and only agrees with |S11| over very small frequency bands, yielding very large sensitivity values. However, for these two-port antennas, if high levels of coupling can be engineered for a high Q multiple-port antenna, the return and insertion losses can be similar over larger bandwidths and, hence, the sensitivity can be kept low over larger bandwidths, enabling broader impedance matched bandwidths to be achieved, even for highly resonant antennas.

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It has been suggested that the tethering caused by binding of the N-terminal region of smooth muscle caldesmon (CaD) to myosin and its C-terminal region to actin contributes to the inhibition of actin-filament movement over myosin heads in an in vitro motility assay. However, direct evidence for this assumption has been lacking. In this study, analysis of baculovirus-generated N-terminal and C-terminal deletion mutants of chicken-gizzard CaD revealed that the major myosin-binding site on the CaD molecule resides in a 30-amino acid stretch between residues 24 and 53, based on the very low level of binding of CaDΔ24–53 lacking the residues 24–53 to myosin compared with the level of binding of CaDΔ54–85 missing the adjacent residues 54–85 or of the full-length CaD. As expected, deletion of the region between residues 24 and 53 or between residues 54 and 85 had no effect on either actin-binding or inhibition of actomyosin ATPase activity. Deletion of residues 24–53 nearly abolished the ability of CaD to inhibit actin filament velocity in the in vitro motility experiments, whereas CaDΔ54–85 strongly inhibited actin filament velocity in a manner similar to that of full-length CaD. Moreover, CaD1–597, which lacks the major actin-binding site(s), did not inhibit actin-filament velocity despite the presence of the major myosin-binding site. These data provide direct evidence for the inhibition of actin filament velocity in the in vitro motility assay caused by the tethering of myosin to actin through binding of both the CaD N-terminal region to myosin and the C-terminal region to actin.