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In-HwanOh,Seong-AhnHong,Sang-YeoulAhn,Yong-CheolLee,Tae-WonLim,HeungYongHa,Seok-JaeShin,Jang-HoJo 한국에너지학회 2002 에너지공학 Vol.11 No.3
?The fabrication method for the main components of the polymer electrolyte membrane fuel cell stack such as electrodes, membrane-electrode assemblies, and bipolar plates was established for the effective electrode area of 240 cm2. A counter-flow type 100-cell stack was fabricated by using the above components and then a maximum power of 7.44 kW for H2/O2 and 5.56 kW for H2/air could be obtained at 70oC and 1 atm. It was seen that the distribution of the OCV for unit cells in the stack was uniform but the voltage deviation increased as the load increased due to the IR drop and the electrode polarization. The stack was applied to the power source of the fuel cell/battery hybrid electric golf car. It produced about 1 kW at a room temperature operation during the test run, which occupied about 43% of the total power required by the 2.3 kW motor.1. Introduction
Activation of calcium signaling by hepatitis B virus-X protein in liver cells
JaneC.Oh,Deuk-LimJeong,In-KyungKim,Sang-HwanOh 생화학분자생물학회 2003 Experimental and molecular medicine Vol.35 No.4
Hepatitis B virus x gene product (HBx) is known to be a transactivator of transcriptional elements associated with the growth, diferentiation, survival and the apoptosis of cels. However, the exact mechanism of the activation and inhibition of cellular events by HBx remains uncertain. The present study was designed to measure the effect of HBx, on the signal transduction pathways as-sociated with intracellular Ca2+ mobilization follow-ing HBx transfection in the stable Chang liver cels (CHL-X). Enhanced cell proliferation by HBx in CHL-X was confirmed by MTT asay and by the imunodetection of PCNA. The transactivation of AP-1 by HBx induced in CHL-X was inhibited by cyclosporin A (CsA), a mitochondrial Ca2+ channel blocker and by BAPTA-AM, a cytosolic Ca2+ bloc-ker. Activation of the SAPK/JNK signaling path-way by HBx was evidenced by the increased phos-phorylations of c-Jun (Ser63) and of JNK (Thr183/ Tyr185). Increased phospho-Erk/Erk and phospho- Raf1/Raf in HBx-induced CHL-X indicated that HBx might stimulate the MAPK pathway. PI3K activity and cytosolic free Ca2+levels were elevated in HBx-induced CHL-X. These results imply that HBx duction pathways in association with the mobili-zation of cytosolic Ca2+.