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Temperature Characteristics of Power Ternary Polymer Li-ion Batteries
Fang Haifeng,Cai Lihua,Lu Huaimin,Wei Benjian,Zhu Hongping 보안공학연구지원센터 2015 International Journal of Hybrid Information Techno Vol.8 No.11
The characteristics of power ternary polymer Li-ion batteries are closely connected to ambient temperature. The capacity characteristic, resistance and state of charge-open circuit voltage (SOC-OCV) curve are important parameters to represent the performance of power batteries and to determine battery management system (BMS) design. The experiments at different ambient temperatures are carried out and the laws between temperature and capacity, resistance and OCV are studied. The capacity drops sharply under low temperature, and increases with a relatively slower rate than under low temperature when the temperature goes up. Polarization and ohmic resistances during charge and discharge process decrease when the temperature rises, and the change rate of ohmic resistance is higher than that of the polarization resistance. Moreover, the change of ohmic resistance under low temperature is more significant than under high temperature. With the decrease of temperature, the SOC-OCV curve moves down, but generally, the curve is affected only slightly by the temperature.
HCBP6 upregulates human SREBP1c expression by binding to C/EBPβ-binding site in the SREBP1c promoter
( Xueliang Yang ),( Ming Han ),( Shunai Liu ),( Xiaoxue Yuan ),( Xiaojing Liu ),( Shenghu Feng ),( Li Zhou ),( Yaru Li ),( Hongping Lu ),( Jun Cheng ),( Shumei Lin ) 생화학분자생물학회(구 한국생화학분자생물학회) 2018 BMB Reports Vol.51 No.1
Sterol regulatory element-binding protein-1c (SREBP1c) plays an important role in triglyceride (TG) homeostasis. Although our previous study showed that hepatitis C virus core-binding protein 6 (HCBP6) regulates SREBP1c expression to maintain intracellular TG homeostasis, the mechanism underlying this regulation is unclear. In the present study, we found that HCBP6 increased intracellular TG levels by upregulating SREBP1c expression. HCBP6 increased SREBP1c transcription by directly binding to the SREBP1c promoter (at the -139- to +359-bp region). Moreover, we observed that HCBP6 interacted with C/EBPβ-binding site in the SREBP1c promoter both in vitro and in vivo. These results indicate that HCBP6 upregulates human SREBP1c expression by binding to the C/EBPβ-binding site in the SREBP1c promoter. [BMB Reports 2018; 51(1): 33-38]