• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.14 no.5
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• pp.362-369
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• 2001

The electrical properties of varistors consisting of Zn-Pr-Co-Cr-Er oxides were investigated in the Er$_2$O$_3$content range of 0.0 to 2.0 mol%. the varistors without Er$_2$O$_3$ exhibited a relatively low nonlinearity, which was 14.24 in the nonlinear exponent and 21.47 $\mu$A in the leakage current. However, the varistors with Er$_2$O$_3$ sintered at 1335$^{\circ}C$ for 1h exhibited very high nonlinear exponent of 70, in particular, reaching a maximum value of 78.05 in 2.0 mol% Er$_2$O$_3$, and those sintered at 1335$^{\circ}C$ for 2h exhibited the nonlinear exponent close to 50, in particular, reaching a maximum value of52.76 in 0.5 mol% Er$_2$O$_3$. The others except for 0.5 mol% Er$_2$O$_3$-added varistors exhibited very high instability resulting in a thermal runaway within a short time, even a weak DC stress. Increasing soaking time decreased the nonlinearity, but increased the stability. The varistors containing 0.5mol% Er$_2$O$_3$ sintered for 2h exhibited excellent stability, in which the variation rate of the varistor voltage and nonlinear exponent was -1.70% and -7.15%, respectively, under more severe DC stress such as (0.80 V$_{1mA}$/9$0^{\circ}C$/12h)+(0.85 V$_{1mA}$/115$^{\circ}C$/12h)+(0.90 V$_{1mA}$/12$0^{\circ}C$/12h)+(0.95 V$_{1mA}$/1$25^{\circ}C$/12h)+(0.95 V$_{1mA}$/15$0^{\circ}C$/12h).TEX>/12h).

• BMB Reports
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• v.42 no.3
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• pp.154-159
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• 2009

JARID1B (jumonji AT rich interactive domain 1B) is a large nuclear protein that is highly expressed in breast cancers and is proposed to function as a repressor of gene expression. In this paper, a phage display screen using the N-terminus of JARID1B as bait identified one of the JARID1B interacting proteins, namely PcG protein (Polycomb group) hPc2. We demonstrated that the C-terminal region, including the COOH box, was required for the interaction with the N-terminus of JARID1B. In a reporter assay system, co-expression of JARID1B with hPc2 significantly enhanced the transcriptional repression. These results support a role for hPc2 acting as a transcriptional co-repressor.

• BMB Reports
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• v.54 no.6
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• pp.329-334
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• 2021

Collagen type I is the most abundant form of collagen in human tissues, and is composed of two identical α-1 type I chains and an α-2 type I chain organized in a triple helical structure. A previous study has shown that human collagen α-2 type I (hCOL1A2) promotes collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs). However, the biological effects of human collagen α-1 type I (hCOL1A1) on various skin properties have not been investigated. Here, we isolate and identify the hCOL1A1-collagen effective domain (CED) which promotes collagen type I synthesis. Recombinant hCOL1A1-CED effectively induces cell proliferation and collagen biosynthesis in HDFs, as well as increased cell migration and elastin production. Based on these results, hCOL1A1-CED may be explored further for its potential use as a preventative agent against skin aging.

• Bulletin of the Korean Chemical Society
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• v.31 no.7
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• pp.1869-1874
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• 2010

By reducing PVP with $H_2NOH$.HCl and NaOH 2:2:1 mass ratios in aqueous ethanol, poly-N-vinyl pyrrolidone oxime [PVPO] was prepared with 92% yield. Applying the sol-gel concept, orthosilicic acid [OSA] was made by hydrolyzing TEOS with ethanol in 1:0.5 molar ratios using 1 N KOH aqueous solution as a catalyst. The OSA + PVPO + $_L$-Valine ($\alpha$-amino acid) were mixed with pure ethanolic medium in 1:2:2 mass ratios and refluxed at $78^{\circ}C$ and 6 pH for 6.5 h. A white residue of poly-N-vinyl pyrrolidone oximo-L-valyl-siliconate [POVS] appeared after 5 h. The heating of reaction mixture was stopped and the contents were brought to NTP. The residue formation of POVS was intensified with lowering a temperature and completely solidified within 5 h, was filtered using a vacuum pump with Whatmann filter paper no. 42. The residue of POVS was washed several times with 20% aqueous cold ethanolic solution and dried in vacuum chamber at $25^{\circ}C$ for 24 h. The MP was noted above $350^{\circ}C$. Structural and internal morphology were analyzed with IR and $^1H$-NMR, and SEM respectively. A drug loading and transporting ability of the POVS in water and at pH = 5 and 8 was determined chromatographically.

• Journal of the Korean Chemical Society
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• v.51 no.4
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• pp.339-345
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• 2007

Urea reacts with PtCl2, H2[PtCl6]·6H2O, H2[IrCl6] and Ni(CH3CO2)2 in aqueous solution at high temperature (60-80 °C) yielding [PtCl2(Urea)]·2H2O (1), (NH4)2[PtCl6] (2), (NH4)2[IrCl6]·H2O (3) and [Ni2(OH)2(NCO)2(H2O)2] (4) complexes, respectively. In complex 1, urea coordinates to Pt(II) as a neutral bidentate ligand via amido nitrogen atoms. In complexes 2, 3 and 4 it seems that the coordinated urea molecules decompose during the reaction at high temperature and a variety of reaction products are obtained. All complexes were isolated in moderate yields as dark green (1), yellow (2), pale brown (3) and faint green (4) precipitates, respectively. The reaction products were characterized by their microanalysis, IR, 1H and 13C NMR spectra as well as thermal analysis. General mechanisms describing the formation of these complexes were suggested.

• Bulletin of the Korean Chemical Society
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• v.34 no.6
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• pp.1751-1754
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• 2013

3,4-Dihydropyrimidin-2(1H)-ones were efficiently converted into the corresponding pyrimidin-2(1H)-ones in high yields within a short period of time on treatment with aqueous acetonitrile using 1,4-bis(triphenylphosphonium)-2-butene peroxodisulfate. Chemoselective oxidation of 3,4-dihydropyrimidin in the presence of other oxidizable functional groups was also achieved by this reagent.

• Korean Journal of Veterinary Service
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• v.34 no.3
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• pp.195-200
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• 2011

Swine influenza is an acute respiratory disease prevalent in pig-growing areas all around the world and plays the roles of an intermediate host to be transmitted to mammals including human beings through a genetic recombination with the avian influenza virus. Recognizing that people could be contracted with swine influenza, this study set out to investigate the seroprevalence of individual and multiple infections with two subtypes (H1N1 and H3N2) of the swine influenza virus in pig farms in the Gyeongnam region according to age, area, and season, as well as to provide basic data for the prevention and control of swine influenza. Used in the study were total 904 swine sera that were not vaccinated against the influenza gathered from the pig farms in the Gyeongnam region from November, 2009 to October, 2010. HerdChek SIV (H1N1, H3N2) ELISA kit (IDEXX Laboratories, USA) was used for antibody testing against swine influenza. The test results show that 370 sera (40.9%) were infected with either H1N1 or H3N2 with 37.3% (337 sera) being contracted with H1N1, 13.1% (118 sera) with H3N2, and 9.4% (85) with both H1N1 and H3N2.

• Journal of Microbiology and Biotechnology
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• v.22 no.5
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• pp.699-707
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• 2012

Since the 2009 pandemic human H1N1 influenza A virus emerged in April 2009, novel reassortant strains have been identified throughout the world. This paper describes the detection and isolation of reassortant strains associated with human pandemic influenza H1N1 and swine influenza H1N2 (SIV) viruses in swine populations in South Korea. Two influenza H1N2 reassortants were detected, and subtyped by PCR. The strains were isolated using Madin-Darby canine kidney (MDCK) cells, and genetically characterized by phylogenetic analysis for genetic diversity. They consisted of human, avian, and swine virus genes that were originated from the 2009 pandemic H1N1 virus and a neuraminidase (NA) gene from H1N2 SIV previously isolated in North America. This identification of reassortment events in swine farms raises concern that reassortant strains may continuously circulate within swine populations, calling for the further study and surveillance of pandemic H1N1 among swine.

• Korean Journal of Microbiology
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• v.52 no.4
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• pp.487-494
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• 2016

In Saccharomyces cerevisiae, Paf1 complex consists of five proteins, and they are structurally and functionally well conserved in yeast, fruit fly, plants, and human. With binding to RNA polymerase II from transcription start site to termination site, Paf1 complex functions as a platform for recruiting many types of transcription factors to RNA polymerase II. Paf1 complex contributes to H2B ubiquitination and indirectly influences on H3K4 di- and tri-methylation by histone crosstalk. But the individual effects of five components in Paf1 complex on these two histone modifications including H2B ubiquitination and H3K4 methylation largely remained to be identified. In this study, we constructed the single-gene knockout mutants of each Paf1 complex component and observed H3K4 mono-, di-, and trimethylation as well as H2B ubiquitination in these mutants. Interestingly, in each ${\Delta}paf1$, ${\Delta}rtf1$, and ${\Delta}ctr9$ strain, we observed the dramatic defect in H3K4 monomethylation, which is independent of H2B ubiquitination, as well as H3K4 di- and trimethylation. However, the protein level of Set1, which is methyltransferase for H3K4, was not changed in these mutants. This suggests that Paf1 complex may directly influence on H3K4 methylation by directly regulating the activity of Set1 or the stability of Set1 complex in an H2B ubiquitination independent manner.

• Bulletin of the Korean Chemical Society
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• v.15 no.11
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• pp.990-996
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• 1994

New ferrocene-based chelate amines, $Fe[C_5H_4CH(Me)NMe_2]_2\;(3), \;Fe[C_5H-3(CH(Me)NMe_2)(PPh_2)-1,2]_2\;(4),\;(C_5H_5)Fe(C_5H_3(CH_2NMe_2)(CH(CN)NMe_2-1,2)\;(6),\;and\;(C_5H_5)Fe(C_5H_3(CH_2NMe_2)(CH(Me)NMe_2-1,2)$ (7) have been prepared. The reaction and the coordination chemistry of 4 and other related compounds (S,R)-(1-N,N-dimethylaminoethyl)-2-dicyclohexylphosphino)ferrocene (CPFA) and 1,1'-bis-(diphenylphosphino)ferrocene (BPPF) with $Rh_2(OAc)_4(MeOH)_2$ were investigated. The reaction of the chiral ligand (S,R)-CPFA forms a complex of the type (${\eta}^1$-(S,R)-CPFA-P)$_2Rh_2(OAc)_4$ (8) in which the ligand is coordinated to both rhodium centers in a monodentate fashion through phosphorus. In contrast, the bisphosphine analogues such as BPPF and 4 afford chelate complexes of the type (${\eta}^2-PP)Rh_2(OAc)_4$ (9 & 10) where both ligands act as a chelate bidentate to a single rhodium atom. All these complexes were characterized by microanalytical and spectroscopic techniques. In one case, the structure of 8 was determined by X-ray crystallography. Crystals are monoclinic, space group C2 (No. 5), with a=26.389 (3), b=12.942 (1), c=11.825 (1) A, ${\beta}$=111.22(1)$^{\circ}$, V=3964.7 (8) $A^3$, Z=4, and $D_{calc}$=1.58 g $cm^{-3}$. Two Rh(II) centers are bridged by four $AcO^-$ groups in the ${\eta}^1$ : ${\eta}^1$ mode across a Rh-Rh single bond, and octahedral coordination at Rh(1) and Rh(1') is completed by axially coordinating (S,R)-CPFA and a briding $AcO^-$, respectively.