• Animal cells and systems
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• v.10 no.1
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• pp.1-6
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• 2006

Previous studies showed that Cdc7 kinase of Schizosaccharomyces pombe phosphorylated the minichromosome maintenance (Mcm) complex efficiently in the presence of spMcm10 protein. The biochemical properties of the phosphorylated Mcm complexes were examined to understand the activation mechanism of the Mcm complex by Cdc7 kinase. The phosphorylation of Mcm complex in the presence of spMcm10 by Cdc7 kinase did not affect the stability of the Mcm complex containing all six subunits, and the changes in the sedimentation properties were not observed after the phosphorylation. The reconstitution of the Mcm complex using the purified proteins showed that the phosphorylation of Mcm2 proteins did not affect the interactions between Mcm proteins. The phosphorylation of the Mcm2-7 complex at the same condition also did not activate the other biochemical activities such as DNA helicase and single stranded (ss) DNA binding activities. On the other hand, spMcm10 protein that was used for the stimulation of Mcm phosphorylation showed single stranded DNA binding activity, and inhibited the DNA helicase activity of the Mcm4/6/7 complex. These inhibitory effects were reduced by the addition of Cdc7 kinase, suggesting that the phosphorylation by Cdc7 kinase decreased the interactions between spMcm10 and the Mcm complex. Taken together, these results suggested that the phosphorylation by Cdc7 kinase alone is not sufficient for the remodeling and the activation of the Mcm complex, and the additional factors or the phosphorylations might be required for the activation of the Mcm complex.

• BMB Reports
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• v.40 no.5
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• pp.805-813
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• 2007

Although MCM2 is obviously important for the initiation of eukaryotic DNA replication, its role in $O_2$ dependent regulation of replicon initiation is poorly understood. In this report, I analysed the changes of MCM2 during the transition from hypoxically suppressed replicon initiation to the burst of initiation triggered by reoxygenation in T24 cells. A high level of chromatin bound and nucleosolic MCM2 was found under the hypoxic replicon arrest. In contrast low cytosolic MCM2 was noticed. Recovery of $O_2$ induced phosphorylation and diminution of chromatin bound MCM2, whereas cytosolic MCM2 increased. The level of chromatin bound Cdc7 did not change significantly upon reoxygenation. However, after reoxygenation, significant phosphorylation of Cdc7 and an increase of coimmunoprecipitation with its substrate (MCM2) were observed. This provides a hint that reoxygenation may promote the kinase activity of Cdc7. These changes might be the critical factors in $O_2$ dependent regulation of replicon initiation. Moreover, phosphorylation of Cdc7 by Cdk2 can be observed in vitro, but seems to fail to regulate the level of chromatin bound Cdc7 as well as the changes of MCM2 in response to reoxygenation of hypoxically suppressed cells.

• Journal of Environmental Science International
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• v.20 no.7
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• pp.873-879
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• 2011

Adsorption experiment of carbon dioxide was performed on MCM41 silica impregnated with two kinds of EDA(ethylenediamine) and MEA(monoethanolamine). The prepared adsorbents were characterized by BET surface area, X-ray diffraction and FT-IR. The $CO_2$ capture study was investigated in a U type packed column with GC/TCD. The results of XRD for MCM-41 and amine-impregnated MCM41 showed typical the hexagonal pore system. BET results showed the MCM 41 impregnated amine to have a surface area of 141 $m^2/g$ to 595 $m^2/g$ and FT-IR revealed a N-H functional group at about 1400$cm^{-1}$ to 1600$cm^{-1}$. The $CO_2$ adsorption capacity on EDA and MEA was as follow: MCM41-EDA30 > MCM41 -EDA40 >MCM41-EDA20 >MCM-EDA10 and MCM41-MEA40 >MCM41-MEA30 > MCM41-MEA20> MCM41-MEA10. The MCM41-EDA30 showed the highest adsorption capacity due to physical adsorption and chemical adsorption by amino-group content. The results suggest that mesoporous media with EDA is effective adsorbent for $CO_2$ capture from flue gases.

• Membrane and Water Treatment
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• v.7 no.6
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• pp.495-505
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• 2016

Mesoporous MCM-41 was deposited on an inexpensive disk shaped ceramic support through hydrothermal technique for ultrafiltration of $Fe^{3+}$ from aqueous solution. The ceramic support was fabricated using uni-axial compaction technique followed by sintering at $950^{\circ}C$. The characteristics of MCM-41 powder as well as the composite membrane were examined by X-ray diffraction (XRD), thermogravimetric analysis (TGA), field emission scanning electron microscope (FESEM), porosity and pure water permeation test. The XRD result revealed the good crystallinity and well-resolved hexagonally arranged pore geometry of MCM-41. TGA profile of synthesized MCM-41 zeolite displayed the three different stepwise mechanisms for the removal of organic template. The formation of MCM-41 on the porous support was verified by FESEM analysis. The characterization results clearly indicated that the accumulation of MCM-41 by repeated coating on the ceramic disk directs to reduce the porosity and pore size from 47% to 23% and 1.0 to $0.173{\mu}m$, respectively. Moreover, the potential of the fabricated MCM-41 membrane was investigated by ultrafiltration of $Fe^{3+}$ from aqueous stream at various influencing parameters such as applied pressure, initial feed concentration and pH of solution. The maximum rejection 85% was obtained at applied pressure of 276 kPa and the initial feed concentration of 250 ppm at pH 2.

• Journal of Life Science
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• v.14 no.5
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• pp.732-740
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• 2004

MCM proteins are essential for eukaryotic DNA replication, playing roles in the initiation and elongation of DNA replication. MCM proteins expression is much higher in malignant tissues than normal tissues. Several reports have indicated the usefulness of MCM proteins as markers of cancer cells in histopathological diagnosis. However, the cause of enhanced expression of MCM proteins in cancer cells remain to be clarified. The purpose of this study is to examine the relative transcriptional activities of human mcm gene promoters in cancer and normal cells. The minimal promoter region required for transcription of a luciferase reporter gene was contained an E-box and one E2F site. In addition, luciferase activities from mcm7 and mcm2 promoter/luciferase gene reporter constructs were significantly increased in cancer cells at 8 times compared with normal cells. E-box and E2F binding site in the promoter of mcm genes are responsible for different mechanism of transcription regulation on the cellular environment.

• Journal of the Korean Chemical Society
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• v.55 no.4
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• pp.691-696
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• 2011

CTAB or CTAB-Nafion catalyst were successfully supported on siliceous hollow tubular MCM-41 which synthesized by hydrothermal method using CTAB as a single template or CTAB and Nafion-Na as mixed templates. The properties of two kinds of catalysts were characterized with XRD, SEM and adsorption and desorption isotherms of nitrogen and pore diameter distribution, respectively. Then they were applied to catalyze brominating reaction of 1,7-heptanediol, moreover the rate of brominating reaction with different catalysts was compared. The results showed that catalytic activities of CTAB/MCM-41 and CTAB-Nafion/MCM-41 are better than CTAB, and that of CTAB-Nafion/MCM-41 is the best because of its phase-transfer and strong acidity function. The two kinds of catalysts can be separated from the reactive products and recycled.

• Bulletin of the Korean Chemical Society
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• v.35 no.7
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• pp.1951-1955
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• 2014

Catalytic pyrolysis of Geodae-Uksae 1, a kind of miscanthus found in Korea, was carried out over mesoporous MCM-48 catalysts. For rapid product analysis and catalyst evaluation, pyrolysis-gas chromatography/mass spectrometry was used. X-ray diffraction, nitrogen sorption, pyridine adsorbed Fourier transform infrared, and NH3 temperature programmed desorption were utilized to analyze the properties of the catalysts. Compared to non-catalytic reaction, catalytic upgrading over mesoporous Al-MCM-48 catalysts produced a higher-quality bio-oil with a high stability and low oxygen content. Al-MCM-48 exhibited higher deoxygenation ability than Si-MCM-48 due to its higher acidity.

• BMB Reports
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• v.41 no.8
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• pp.581-586
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• 2008

The pre-replication complex (pre-RC), including the core hexameric MCM2-7 complex, ensures that the eukaryotic genome is replicated only once per cell division cycle. In this study, we identified a rice $\underline{m}ini\underline{c}hromosome$ $\underline{m}aintenance$ (MCM) homologue (OsMCM2) that functionally complemented fission yeast MCM2 (CDC19) mutants. We found OsMCM2 transcript expression in roots, leaves, and seeds, although expression levels differed slightly among the organs. Likewise, the OsMCM2 protein was ubiquitously expressed, but it was downregulated when nutritients were limiting, indicating that MCM2 expression (and therefore cell cycle progression) requires adequate nutrition. Yeast two-hybrid and GST pull-down assays demonstrated that OsMCM2 interacted with the COP9 signalosome 5 (CSN5). Taken as a whole, our results indicated that OsMCM2 functions as a subunit of the rice MCM complex and interacts with CSN5 during developmental regulation.

• Applied Chemistry for Engineering
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• v.10 no.7
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• pp.1096-1098
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• 1999

MCM-41 type spherical mesoporous silica material was synthesized, under basic conditions, in the presence of cationic surfactant as templating species. The cationic surfactants used in this experiment were octyltrimethylammonium bromide, dodecyltrimetylammonium bromide, cetyltrimethylammonium bromide, octadecyltrimethyammonium bromide and cetylpyridium bromide. Specific surface area of spherical MCM-41 was as high as $1500m^2/g$ and the pore size decreased with increasing alkyl chain length of surfactant.

• Applied Chemistry for Engineering
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• v.10 no.7
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• pp.1020-1027
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• 1999

Heteropoly acid(HPW) catalysts supported on three different carriers, an amorphous silica, MCM-41 and MCM-48, with different loadings and calcination temperatures have been prepared and characterized by X-ray diffraction, nitrogen physorption, infrared spectroscopy, and $^{31}P$ magic angle spinning NMR. From the result of IR and NMR, it was shown that HPW retains the Keggin structure on the supported catalysts. No HPW crystal phase was developed even at HPW loadings as high as 35 wt % on the MCM-41 and 65 wt % MCM-48. Thus, HPW appeared to form finely dispersed species. In the hydrolysis reaction of di, bis, tri-pentaerythritol, HPW/MCM-41, 48 exhibited higher catalytic activity than $HPW/SiO_2$ or HPW.