• Molecules and Cells
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• v.39 no.9
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• pp.654-662
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• 2016

Almost all eukaryotic proteins are subject to post-translational modifications during mitosis and cell cycle, and in particular, reversible phosphorylation being a key event. The recent use of high-throughput experimental analyses has revealed that more than 70% of all eukaryotic proteins are regulated by phosphorylation; however, the mechanism of dephosphorylation, counteracting phosphorylation, is relatively unknown. Recent discoveries have shown that many of the protein phosphatases are involved in the temporal and spatial control of mitotic events, such as mitotic entry, mitotic spindle assembly, chromosome architecture changes and cohesion, and mitotic exit. This implies that certain phosphatases are tightly regulated for timely dephosphorylation of key mitotic phosphoproteins and are essential for control of various mitotic processes. This review describes the physiological and pathological roles of mitotic phosphatases, as well as the versatile role of various protein phosphatases in several mitotic events.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.02a
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• pp.301-301
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• 2011

We present theoretical investigations of the self-assembled growth of one-dimensional (1D) molecular lines directed across the dimer rows on the H-terminated Si(001) surface [1]. Based on density-functional theory calculations, a new growth mechanism of the 1D acetylacetone line is proposed [2], which involves the radical chain reaction initiated at two dangling-bond sites on one side of two adjacent Si dimers. It is also enabled that, if an H-free Si dimer were employed as the initial reaction site, a 1D acetylacetone line can grow along the dimer row. Our findings represent the first insight into the growth of 1D molecular lines not only across but also along the dimer rows on the H-terminated Si(001) surface.

• Bulletin of the Korean Chemical Society
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• v.25 no.11
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• pp.1711-1713
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• 2004

• Bulletin of the Korean Chemical Society
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• v.23 no.9
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• pp.1347-1350
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• 2002

• Bulletin of the Korean Chemical Society
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• v.26 no.1
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• pp.184-186
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• 2005

• Bulletin of the Korean Chemical Society
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• v.27 no.12
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• pp.2055-2057
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• 2006

• Proceeding of EDISON Challenge
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• 2013.04a
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• pp.221-223
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• 2013

Self-assembly of the molecular system of perylene-3,4,9,10-tetracarboxylic-3,4,9,10-dianhydride (PTCDA) and the amide analogue (PTCDI) is of potential importance for organic semiconductor devices. Therefore we studied the density of states (DOS), the charge densities, and intermolacular bond lengths for PTCDA and PTCDI using the density functional theory calculations.

• The Journal of Korea Institute of Information, Electronics, and Communication Technology
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• v.8 no.1
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• pp.37-44
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• 2015

In this paper, we have investigated a selective assembly method of single-walled carbon nanotubes (SWCNTs) on a silicon substrate using only photolithographic process and then proposed a fabrication method of field effect transistors (FETs) using SWCNT-based patterns. The aminopropylethoxysilane (APTES) patterns, which are formed for positively charged surface molecular patterns, are utilized to assemble and align millions of SWCNTs and we can more effectively assemble on a silicon (Si) surface using this method than assembly processes using only the 1-octadecyltrichlorosilane (OTS). We investigated a selective assembly method of SWCNTs on a Si surface using surface-programmed APTES and OTS patterns and then a fabrication method of FETs. photoresist(PR) patterns were made using photolithographic process on the silicon dioxide (SiO2) grown Si substrate and the substrate was placed in the OTS solution (1:500 v/v in anhydrous hexane) to cover the bare SiO2 regions. After removing the PR, the substrate was placed in APTES solution to backfill the remaining SiO2 area. This surface-programmed substrate was placed into a SWCNT solution dispersed in dichlorobenzene. SWCNTs were attracted toward the positively charged molecular regions, and aligned along the APTES patterns. On the contrary, SWCNT were not assembled on the OTS patterns. In this process, positively charged surface molecular patterns are utilized to direct the assembly of negatively charged SWCNT on SiO2. As a result, the selectively assembled SWCNT channels can be obtained between two electrodes(source and drain electrodes). Finally, we can successfully fabricate SWCNT-based multi-channel FETs by using our self-assembled monolayer method.

• BMB Reports
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• v.49 no.8
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• pp.449-454
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• 2016

Stress Granules (SGs) are microscopically visible, phase dense aggregates of translationally stalled messenger ribonucleoprotein (mRNP) complexes formed in response to distinct stress conditions. It is generally considered that SG formation is induced to protect cells from conditions of stress. The precise constituents of SGs and the mechanism through which SGs are dynamically regulated in response to stress are not completely understood. Hence, it is important to identify proteins which regulate SG assembly and disassembly. In the present study, we report Neuregulin-2 (NRG2) as a novel component of SGs; furthermore, depletion of NRG2 potently inhibits SG formation. We also demonstrate that NRG2 specifically localizes to SGs under various stress conditions. Knockdown of NRG2 has no effect on stress-induced polysome disassembly, suggesting that the component does not influence early step of SG formation. It was also observed that reduced expression of NRG2 led to marginal increase in cell survival under arsenite-induced stress.

• BMB Reports
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• v.29 no.5
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• pp.411-416
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• 1996

In order to study the role of the protein shell in both iron uptake and iron core formation of ferritin, we constructed a deletion mutant of the ferritin gene and expressed the mutant gene in Escherichia coli, This mutant was obtained by introducing an amber mutation at position Pro-157 and a deletion of the 19 amino acid residues at the carboxy-terminus of the recombinant tadpole H-chain ferritin. The deleted amino acids correspond to E-helix forming the hydrophobic channel in the protein. E. coli harboring the plasmid pTHP157, which contains the deleted gene, was grown at $23^{\circ}C$ in the presence of 0.1 mM IPTG, and the induced protein appeared to be partly soluble. Nondenaturing polyacrylamide gel electrophoresis showed that the expressed mutant H-chains coassemble into holoprotein, suggesting that E-helix is not necessary for assembly of the subunits as reported for human H-chain ferritin. Its ability in iron core formation was proven in an Fe staining gel, the result disagreeing with the observation that the hydrophobic channel is necessary for iron core formation in human H-chain ferritin.