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RISS 인기검색어
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- 저자 : Luis I. Silva (검색결과 4 건)
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Multi-Domain Model for Electric Traction Drives Using Bond Graphs
Silva, Luis I.,De La Barrera, Pablo M.,De Angelo, Cristian H.,Aguilera, Facundo,Garcia, Guillermo O. The Korean Institute of Power Electronics 2011 JOURNAL OF POWER ELECTRONICS Vol.11 No.4
In this work the Multi-Domain model of an electric vehicle is developed. The electric domain model consists on the traction drive and allows including faults associated with stator winding. The thermal model is based on a spatial discretization. It receives the power dissipated in the electric domain, it interacts with the environment and provides the temperature distribution in the induction motor. The mechanical model is a half vehicle model. Given that all models are obtained using the same approach (Bond Graph) their integration becomes straightforward. This complete model allows simulating the whole system dynamics and the analysis of electrical/mechanical/thermal interaction. First, experimental results are aimed to validate the proposed model. Then, simulation results illustrate the interaction between the different domains and highlight the capability of including faults.
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Multi-Domain Model for Electric Traction Drives Using Bond Graphs
Luis I. Silva,Pablo M. de la Barrera,Cristian H. De Angelo,Facundo Aguilera,Guillermo O. Garcia 전력전자학회 2011 JOURNAL OF POWER ELECTRONICS Vol.11 No.4
In this work the Multi-Domain model of an electric vehicle is developed. The electric domain model consists on the traction drive and allows including faults associated with stator winding. The thermal model is based on a spatial discretization. It receives the power dissipated in the electric domain, it interacts with the environment and provides the temperature distribution in the induction motor. The mechanical model is a half vehicle model. Given that all models are obtained using the same approach (Bond Graph) their integration becomes straightforward. This complete model allows simulating the whole system dynamics and the analysis of electrical/mechanical/thermal interaction. First, experimental results are aimed to validate the proposed model. Then, simulation results illustrate the interaction between the different domains and highlight the capability of including faults.
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Serum Albumin Modulates the Bioactivity of Rosmarinic Acid
Elsa Brito,Andre Silva,Pedro Luis Vieira Fale,Rita Pacheco,Antonio Serralheiro,Parvez I. Haris,Lia Ascensao,Maria Luısa Serralheiro 한국식품영양과학회 2018 Journal of medicinal food Vol.21 No.8
Rosmarinic acid (RA) is a phenolic compound with biological activity. The objective of the present study was to investigate whether this compound kept its biological activity in the presence of proteins. For this purpose, bovine serum albumin (BSA) was used as a model protein, and the capacity of the RA to inhibit acetylcholinesterase (AChE) and affect antioxidant activity was evaluated in the absence and presence of BSA. A mixture of phenolic compounds containing RA, obtained from a medicinal plant was added to this study. The AChE inhibitory activity of RA was reduced by ∼57% in the presence of BSA, while the antioxidant activity increased. These results lead to the investigation of the effect of RA on the BSA structure using Fourier transform infrared spectroscopy (FTIR). At 37°C and higher temperatures, RA caused a decrease in the temperature modifications on the protein structure. Furthermore, FTIR and native-gel analysis revealed that protein aggregation/precipitation, induced by temperature, was reduced in the presence of RA. The novelty of the present work resides in the study of the enzyme inhibitory activity and antioxidant capacity of polyphenols, such as RA, in the presence of a protein. The findings highlight the need to consider the presence of proteins when assessing biological activities of polyphenols in vitro and that enzyme inhibitory activity may be decreased, while the antioxidant capacity remains or even increases.
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( Pablo D. Cabral ),( Guillermo B. Silva ),( Sandra T. Baigorria ),( Luis I. Juncos ),( Ebenezer I. O. Ajayi ),( Néstor H. García ) 대한신장학회 2022 Kidney Research and Clinical Practice Vol.41 No.6
Background: Sodium chloride (NaCl) reabsorption in the cortical thick ascending limb (cTAL) is regulated by opposing effects. Nitric oxide (NO) inhibits NaCl reabsorption while 8-iso-prostaglandin-F2α (8-iso-PGF2α) stimulates it. Their interaction has not been evalu ated in the cTAL. Because 8-iso-PGF2α has considerable stability while NO is a free radical with a short half-life, we hypothesized that, in the cTAL, the inhibition of NaCl absorption will be reversed by 8-iso-PGF2α. Methods: Chloride absorption (J<sub>Cl</sub>) was measured in isolated perfused cTALs and whether the activation of protein kinase A (PKA) is required for this interaction. Since cyclic adenosine monophosphate (cAMP) is a major messenger for the 8-iso-PGF2α signaling cas cade, and NO inhibits J<sub>Cl</sub> by decreasing cAMP bioavailability, we measured 8-iso-PGF2α-stimulated cAMP in the presence of sodium nitroprusside (SNP). Results: The NO donor, SNP (10<sup>-6</sup> M), decreased J<sub>Cl</sub> by 41%, while luminal 8-iso-PGF2α (100 μM) increased J<sub>Cl</sub> to 315 ± 46 pmol/ min/mm (p < 0.003), reversing the effects of the NO donor. SNP inhibited J<sub>Cl</sub>, 8-iso-PGF2α failed to increase J<sub>Cl</sub> in the presence of H89. Basal cAMP was 56 ± 13 fmol/min/mm, in the presence of SNP 57 ± 6 fmol/min/mm, and 8-iso-PGF2α increased it to 92 ± 2 fmol/min/mm (p < 0.04). Conclusion: We concluded that 1) NO-induced inhibition of J<sub>Cl</sub> in the cTAL can be reversed by 8-iso-PGF2α, 2) 8-iso-PGF2α and NO in teraction requires PKA to control J<sub>Cl</sub>, and 3) in the presence of NO, 8-iso-PGF2α continues to stimulate J<sub>Cl</sub> because NO cannot reverse 8-iso-PGF2α-stimulated cAMP level.
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