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MEMS-based thin-film solid-oxide fuel cells
An, Jihwan,Shim, Joon Hyung,Kim, Young-Beom,Park, Joong Sun,Lee, Wonyoung,Gü,r, Turgut M.,Prinz, Fritz B. Cambridge University Press (Materials Research Soc 2014 MRS bulletin Vol.39 No.9
<▼1><B>Abstract</B><P/></▼1><▼2><P>Thin-film solid-oxide fuel cells (TF-SOFCs) fabricated using microelectromechanical systems (MEMS) processing techniques not only help lower the cell operating temperature but also provide a convenient platform for studying cathodic losses. Utilizing these platforms, cathode kinetics can be enhanced dramatically by engineering the microstructure of the cathode/electrolyte interface by increasing the surface grain-boundary density. Nanoscale secondary ion mass spectrometry and high-resolution transmission electron microscopy studies have shown that oxygen exchange at electrolyte surface grain boundaries is facilitated by a high population of oxide-ion vacancies segregating preferentially to the grain boundaries. Furthermore, three-dimensional structuring of TF-SOFCs enabled by various lithography methods also helps increase the active surface area and enhance the surface exchange reaction. Although their practical prospects are yet to be verified, MEMS-based TF-SOFC platforms hold the potential to provide high-performance for low-temperature SOFC applications.</P></▼2>
Atomic layer deposition of thin-film ceramic electrolytes for high-performance fuel cells
Shim, Joon Hyung,Kang, Sangkyun,Cha, Suk-Won,Lee, Wonyoung,Kim, Young Beom,Park, Joong Sun,Gü,r, Turgut M.,Prinz, Fritz B.,Chao, Cheng-Chieh,An, Jihwan The Royal Society of Chemistry 2013 Journal of materials chemistry. A, Materials for e Vol.1 No.41
Kiho Bae,Dong Young Jang,Joong Sun Park,Ji-Won Son,Fritz B. Prinz,Joon Hyung Shim 한국정밀공학회 2020 International Journal of Precision Engineering and Vol.7 No.2
Diffusion of oxide ions along heterostructured yttria-stabilized zirconia (YSZ) epitaxially grown on single crystalline MgO (001) is investigated. Pulsed laser deposition is used for the epitaxial growth and focused ion beam was applied to open the lateral surface of the YSZ-MgO interface layers and to enable incorporation and diffusion of oxygen. The sample is annealed in 18O2 environment to trace oxide ion transport with Al2O3 layers atop to block diffusion perpendicular to surface of the YSZ plane. Time-of-flight secondary mass ion spectrometry (TOF–SIMS) analyze the planar diffusion profiles. Diffusivity and surface exchange rate are estimated by SIMS data fitting. As a result, it is identified that both oxide ion diffusion and surface incorporation rates are significantly enhanced on surface of the heterostructured YSZ on MgO (001) compared to bulk YSZ.
Kim, D.Y.,Kang, T.B.,Shim, D.W.,Sun, X.,Han, J.W.,Ji, Y.E.,Kim, T.J.,Koppula, S.,Lee, K.H. North-Holland ; Elsevier Science Ltd 2014 european journal of pharmacology Vol.723 No.-
Mast cells are known to play a pivotal role in allergic diseases. Cross-linking of the high-affinity IgE receptor (FcεRI) is known to be one of the major causes that lead to degranulation and allergic inflammation. An increase in intracellular calcium (Ca<SUP>2+</SUP>) concentration also triggers degranulation, bypassing receptor activation. Emodin (1,3,8-trihydroxy-6-methylanthraquinone) is known to exhibit a variety of pharmacological activities including anti-allergic effects. However, the detailed molecular mechanisms involved in exhibiting anti-allergic effects by emodin were remained to be clarified. In the present investigation we report the regulatory function of emodin on the allergic signal mediators through Ca<SUP>2+</SUP> ionophore activation in mast cells. Emodin significantly inhibited A23187-induced tumor necrosis factor-α production and degranulation through the attenuation of protein kinase C, IκB kinase 2, and soluble N-ethylmaleimide-sensitive fusion factor attachment protein receptor complex formation, bypassing FcεRI activation. Data from our study indicated that emodin acts by regulating multiple signaling pathways in inhibiting the allergic reactions in mast cells.
Yim, Su Y,Chae, Kab R,Shim, Sun B,Hong, Jin T,Park, Jung Y,Lee, Chung Y,Son, Hong J,Sheen, Yhun Y,Hwang, Dae Y D.A. Spandidos 2009 INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE Vol.24 No.1
<P>Selenium reportedly contribute to the modulation process of protein phosphorylation to regulate various cellular functions including growth, differentiation, proliferation and development. The aim of this study was to investigate whether selenium and Selenoprotein M (SelM) affects the mechanism of Alzheimer's disease. To achieve this, we determined the change of the MAPK pathway, secretase activity, and Tau phosphorylation in the transgenic rat overexpressing human selenoprotein M. Based on these results, we concluded that, i) CMV/GFP-hSelM Tg rats showed a high activity level of antioxidant enzyme in the brain tissues, ii) in response to selenium treatment, the ERK signaling pathway was significantly increased in Tg rats, but did not change in wild-type rats, iii) the activation of the ERK pathway by selenium treatment and SelM overexpression induced the inhibition of the alpha/gamma-secretase activity related to the protection of Abeta-42 production, iv) the activation of the ERK pathway by selenium treatment and SelM overexpression inhibited the phosphorylation in several sites of Tau protein. Therefore, these results provide strong evidence that selenium treatment and SelM activate the ERK pathway to attenuate alpha/gamma-secretase-mediated proteolysis and Tau phosphorylation to protect brain function.</P>