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Choi, Suck-Chei,Choi, Eun-Ju,Oh, Hyun-Mee,Lee, SungGa,Lee, Jeong-Kun,Lee, Meung-Su,Shin, Yong-Il,Choi, Suck-Jun,Chae, Jeong-Ryong,Lee, Kang-Min,Lee, Won-Jung,Park, Jae-Sik,Shin, Chang-Yell,Oh, Tae-You WJG Press 2006 WORLD JOURNAL OF GASTROENTEROLOGY Vol.12 No.30
<P>To investigate whether, or how, DA-9601, which is a new gastroprotective agent, inhibits TNF-alpha-induced inflammatory signals in gastric epithelial AGS cells.</P>
효율적(效率的) 의사결정(意思決定)을 위한 초등학교(初等學校) 계획(計劃)에서의 사용자(使用者)와 전문가(專門家)의 인식(認識) 차이(差異) 분석(分析)
오일룡(Oh, Il-Ryong),최재영(Choi, Jae-Young),이동주(Lee, Dong-Joo),고은형(Ko, Eun-Hyung),최무혁(Choi, Moo-Hyuck) 한국교육시설학회 2005 敎育施設 Vol.12 No.6
The purpose of this study is to investigate cognitive gap between users and architectural experts for architectural planning of elementary schools to support effective decision-makings. For this study, each architectural factor was selected from the journals published by Korean Institute of Education Facilities( KIEF ) from 2000 to 2004. Among these factors, the priority planning factors were decided through Analytic Hierarchy Process(AHP). The results of this study showed users' emphasis on the amenities of physical environment such as orientation, ventilation, noise, view, but experts' preference on spatial composition of space and function such as orientation, circulation, zoning, parking lot, courtyard. This difference shows clear cognitive gaps between two groups and also suggests factors required to be considered to develop effective decision-making in elementary school planning.
Chemical Modification of Porcine Brain myo-Inositol Monophosphate Phosphatase by N-bromosuccinimide
Choi,Soo Young,Kwon,Hyeok Yil,Yoon,Byung Hak,Ahn,Yoon Kyung,Lee,Byung Ryong,Jeon,Seong Gyu,Bahn,Jae Hoon,Kwon,Oh-Shin The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.3
Myo-inositol monophosphate phosphatase is a key enzyme in the phophoinositide cell-signaling system. Incubation of myo-inositol monophosphate phosphatase from porcine brain with N-bromosuccinimide (NBS) resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo-first-order kinetics with the second-order rate constant of 3.8×10³M -¹ min-¹. The time course of the reaction was significantly affected by the substrate myo-inositol-1-phosphate, which afforded complete protection against the loss of catalytic activity. Spectrophotometric studies indicated that about one oxindole group per molecule of enzyme was formed following complete loss of enzymatic activity. It is suggested that the catalytic function of myo-inositol monophosphate phosphatase is modulated by the binding of NBS to a specific tryptophan residue at or near the substrate binding site of the enzyme.
Fusion of multispectral and panchromatic Satellite images using the curvelet transform
Choi, Myungjin,Kim, Rae Young,Nam, Myeong-Ryong,Kim, Hong Oh IEEE 2005 IEEE geoscience and remote sensing letters Vol.2 No.2
A useful technique in various applications of remote sensing involves the fusion of different types of satellite images, namely multispectral (MS) satellite images with a high spectral and low spatial resolution and panchromatic (Pan) satellite image with a low spectral and high spatial resolution. Recent studies show that wavelet-based image fusion provides high-quality spectral content in fused images. However, the results of most wavelet-based methods of image fusion have a spatial resolution that is less than that obtained via the Brovey, intensity-hue-saturation, and principal components analysis methods of image fusion. We introduce an improved method of image fusion which is based on the amelioration de la resolution spatiale par injection de structures (ARSIS) concept using the curvelet transform, because the curvelet transform represents edges better than wavelets. Because edges are fundamental in image representation, enhancing the edges is an effective means of enhancing spatial resolution. Curvelet-based image fusion has been used to merge a Landsat Enhanced Thematic Mapper Plus Pan and MS image. The proposed method simultaneously provides richer information in the spatial and spectral domains.
Choi, Kiheon,Lim, Hyun Kyung,Oh, Sung Ryong,Chung, Woo-Hyun,Jung, Joohee Hindawi Publishing Corporation 2017 Evidence-based Complementary and Alternative Medic Vol.2017 No.-
<P>Interest in marine bioresources is increasing in the drug development sector. In particular, marine sponges produce a wide range of unique metabolites that enable them to survive in challenging environments, which makes them attractive sources of candidate pharmaceuticals. In previous study, we investigated over 40 marine specimens collected in Micronesia and provided by the Korean Institute of Ocean Science and Technology, for their antiproliferative effects on various cancer cell lines, and<I> Lipastrotethya</I> sp. extract (LSSE) was found to have a marked antiproliferative effect. In the present study, we investigated the mechanism responsible for its anticancer effect on wild-type p53 (WT) or p53 knockout (KO) HCT116 cells. LSSE inhibited cell viability and induced apoptotic cell death more so in HCT116 p53 KO cells than the WT. HCT116 WT cells treated with LSSE underwent apoptosis associated with the induction of p53 and its target genes. On the other hand, in HCT116 p53 KO cells, LSSE reduced mTOR and Bcl-2 and increased Beclin-1 and LC3-II protein levels, suggesting autophagy induction. These results indicate that the mechanisms responsible for the anticancer effect of LSSE depend on p53 status.</P>
Choi, Soo Young,Bahn, Jae Hoon,Park, Jinseu,Jin, Li Hua,Lee, Byung Ryong,Kim, Chung Kwon,Cho, Sung-Woo,Jeon, Seong Gyu,Cho, Yong Joon,Jang, Joong Sik,Kwon, Oh-Shin The Korea Science and Technology Center 2000 BMB Reports Vol.33 No.4
The succinic semialdehyde dehydrogenase from bovine brain was inactivated by treatment with phenylglyoxal, a reagent that specifically modifies arginine residues. The inhibition at various phenylglyoxal ocncentrations shows pseudo-first-order kinetics with an apparent second-order rate constant of 30 M-¹min-¹ for inactivation. Partial pretection against inactivation was provided by the coenzyme NAD+, but not by the substrate succinic semialdehyde. Spectrophotoetric studies indicated that complete inactivation of the enzyme resulted from the binding of 2 mol phenylglyoxal per mol of enzyme. These results suggest that essential arginine residues, located at or near the coenzyme-bindig site, are connected with the catalytic activity of brain succinic semialdehyde dehydrogenase.