• Carbon letters
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• v.10 no.3
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• pp.217-220
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• 2009

In this study, porous electrospun carbon fibers were prepared by electrospinning with PAN and $MgCl_2$, as a MgO precursor. MgO was selected as a substrate because of its chemical and thermal stability, no reaction with carbon, and ease of removal after carbonization by dissolving out in acidic solutions. $MgCl_2$ was mixed with polyacrylonitrile (PAN) solution as a precursor of MgO with various weight ratios of $MgCl_2$/PAN. The average diameter of porous electrospun carbon fibers increased from 1.3 to 3 ${\mu}m$, as the $MgCl_2$ to PAN weight ratio increased. During the stabilization step, $MgCl_2$ was hydrolyzed to MgOHCl by heat treatment. At elevated temperature of 823 K for carbonization step, MgOHCl was decomposed to MgO. Specific surface area and pore structure of prepared electrospun carbon fibers were decided by weight ratio of $MgCl_2$/PAN. The amount of hydrogen storage increased with increase of specific surface area and micropore volume of prepared electrospun carbon fibers.

• Molecules and Cells
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• v.27 no.3
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• pp.359-363
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• 2009

Chfr, a checkpoint with FHA and RING finger domains, plays an important role in cell cycle progression and tumor suppression. Chfr possesses the E3 ubiquitin ligase activity and stimulates the formation of polyubiquitin chains by Ub-conjugating enzymes, and induces the proteasome-dependent degradation of a number of cellular proteins, including Plk1 and Aurora A. While Chfr is a nuclear protein that functions within the cell nucleus, how Chfr is localized in the nucleus has not been clearly demonstrated. Here, we show that nuclear localization of Chfr is mediated by nuclear localization signal (NLS) sequences. To reveal the signal sequences responsible for nuclear localization, a short lysine-rich stretch (KKK) at amino acid residues 257-259 was replaced with alanine, which completely abolished nuclear localization. Moreover, we show that nuclear localization of Chfr is essential for its checkpoint function but not for its stability. Thus, our results suggest that NLS-mediated nuclear localization of Chfr leads to its accumulation within the nucleus, which may be important in the regulation of Chfr activation and Chfr-mediated cellular processes, including cell cycle progression and tumor suppression.

• Journal of Microbiology and Biotechnology
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• v.22 no.5
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• pp.592-599
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• 2012

Bacillus licheniformis ${\alpha}$-amylase (BLA), a thermophilic counterpart of Bacillus amyloliquefaciens ${\alpha}$-amylase (BAA), is an appropriate model for the design of stabilizing mutations in BAA. BLA has 10 more histidines than BAA. Considering this prominent difference, in the present study, three out of these positions (I34, Q67, and P407; located in the thermostability determinant 1 region and Ca-III binding site of BAA) were replaced with histidine in BAA, using the site-directed mutagenesis technique. The results showed that the thermostability of P407H and Q67H mutants had increased, but no significant changes were observed in their kinetic parameters compared to that of the wild type. I34H replacement resulted in complete loss of enzyme activity. Moreover, fluorescence and circular dichroism data indicated a more rigid structure for the P407H variant compared with that of the wild-type BAA. However, the flexibility of Q67H and I34H mutants increased in comparison with that of wild-type enzyme.

• Molecules and Cells
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• v.21 no.2
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• pp.218-223
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• 2006

The effect of poly(ADP-ribosyl)ation on the stability of p53 in SK-HEP1 cells treated with UV light was examined. Intracellular levels of p53 increased in cells treated with a low dose of UV light ($20J/m^2$), whereas they increased but then declined after a higher dose of UV ($100J/m^2$). Intracellular levels of p53 in the UV treated SK-HEP1 cells were dependent on the UV dose. Use of proteasome inhibitors revealed that p53 is degraded by proteasomal proteolysis after high doses of UV light. We present evidence that, at low doses, poly(ADP-ribose)polymerase (PARP) poly(ADP-ribosyl) ates p53 and protects it from proteasomal degradation before caspase-3 is activated, whereas at high doses the cells undergo UV induced apoptosis and PARP is cleaved by caspase-3 before it can protect p53 from degradation. Destabilization of p53 by cleavage of PARP may be important in cell fate decision favoring apoptosis.

• Journal of Microbiology and Biotechnology
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• v.16 no.4
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• pp.562-568
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• 2006

GABA $(\gamma-aminobutyric\;acid)$ is the principal inhibitory neurotransmitter in the brain. For the efficient production of GAB A, a semi continuous cell entrapment system using Lactobacillus brevis GABA 057 was optimized, including the substrate concentration, bead-stabilizing additives, and reaction conditions. The converted monosodium glutamate (MSG), which was added as a substrate for glutamic acid decarboxylase (GAD), increased from 2% (w/v) to 12% (w/v). The addition of isomaltooligosaccharide to the alginate beads also increased the stability of the entrapped L. brevis and GABA productivity. Consequently, when optimal conditions were applied, up to 223 mM GABA could be produced from 534 mM MSG after 48 h of reaction by using alginate-beadencapsulated L. brevis GABA 057.

• Food Science of Animal Resources
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• v.42 no.2
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• pp.197-209
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• 2022

Extracellular vesicles (EVs) are nanosized vesicles secreted from cells into the extracellular environment and are composed of a lipid bilayer that contains cargos with biological activity, such as lipids, proteins, mRNAs, and noncoding microRNAs (miRNAs). Due to their biological activity and their role in cell-to-cell communication, interest in EVs is rapidly increasing. Bovine milk is a food consumed by people of all ages around the world that contains not only a significant amount of nutrients but also EVs. Milk-derived EVs also exhibit biological activity similar to other source-derived EVs, and studies on bovine milk EVs have been conducted in various research fields regarding sufficient milk production. In particular, not only are the effects of milk EVs themselves being studied, but the possibility of using them as drug carriers or biomarkers is also being studied. In this review, the characteristics and cargo of milk EVs are summarized, as well as their uptake and stability, efficacy and biological effects as carriers, and future research directions are presented.

• Korean Journal of Food Science and Technology
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• v.10 no.2
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• pp.250-257
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• 1978

Functional additives such as methyl silicone, TBHQ and BHA/BHT have been evaluated for their effects on storage and frying stabilities of the vegetable salad oil. All test results strongly suggest that methyl silicone improved the frying stability and TBHQ improved the storage stability. BHA/BHT improved neither storage stability, nor frying stability of the vegetable saladoil. Based on the test results, it is recommended that methyl silicone in the range of $1.0{\pm}0.5ppm$ and TBHQ in the range of 200ppm be added to the vegetable salad oil for the improvement of frying and storage stabilities.

• Asian Pacific Journal of Cancer Prevention
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• v.13 no.8
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• pp.3583-3587
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• 2012

SUMOylation has emerged as an important post-translational modification that modulates the localization, stability and activity of a broad spectrum of proteins. A dynamic process, it can be reversed by a family of SUMO-specific proteases (SENPs). However, the biological roles of SENPs in mammalian development and pathogenesis remain largely elusive. Here, we demonstrated that SENP2 plays a critical role in the control of hepatocellular carcinoma cell growth. SENP2 was found to be down-regulated in hepatocellular carcinoma (HCC) tissues and over-expression suppressed the growth and colony formation of HCC cells. In contrast, silencing of SENP2 by siRNAs promoted cancer cell growth. We further found that stability of ${\beta}$-catenin was markedly decreased when SENP2 was over-expressed. Interestingly, the decrease was dependent on the de-SUMOylation activity of SENP2, because over-expression of a SENP2 catalytic mutant form had no obviously effects on ${\beta}$-catenin. Our results suggest that SENP2 might play a role in hepatocellular carcinoma cell growth control by modulating the stability of ${\beta}$-catenin.

• Journal of Microbiology
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• v.34 no.3
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• pp.241-247
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• 1996

The stability of the genetically engineered microorganisms and their recombinant plasmids released in natural environments has been regarded as one of the molecular ecological topics. In this study, the recombinant plasmids pCU103 in which the pcbCD genes involved in biodegradation of biphenyl and 4-chlorobiphenyl were cloned in pBluescript SK(+) vector, were examined for their structural and functional stability in different waters at 15 $^{\circ}C$ by the methods of electrophoresis, Southern hybridization, quantification with fluorescent dye, and transformation. The recombinant plamids maintained their stabilities for about 30 days in sterilized distilled water (SDW), 15 days in autoclaved creek water (AW), 25 days in filtered and autoclaved non-sterile creek water (FAW), 4 days in Luria-Bertani (LB) broth, and less than one day in filtered non-sterile creek water (FW). The covalently closed circular (CCC) form of the plasmid was decreased and open circular (OC) form was increased as a function of incubation time, and then linear (L) form was produced to be ultimately degraded out. The degradation rates of the plasmid were proportionally correlated to trophic level of the water, and the biological factor such as DNases was found to be one of the most critical factors affecting structural and functional stability of the plasmid in non-sterile natural water.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2001.11b
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• pp.3-6
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• 2001

In common globular proteins, the native form is in its most stable state. However, the native form of inhibitory serpins (serine protease inhibitors) and some viral membrane fusion proteins is in a metastable state. Metastability in these proteins is critical to their biological functions. Our previous studies revealed that unusual interactions, such as side-chain overpacking, buried polar groups, surface hydrophobic pockets, and internal cavities are the structural basis of the native metastability. To understand the mechanism by which these structural defects regulate protein functions, cavity-filling mutations of a 1-antitrypsin, a prototype serpin, were characterized. Increasing conformational stability is correlated with decreasing inhibitory activity. Moreover, the activity loss appears to correlate with the decrease in the rate of the conformational switch during complex formation with a target protease. We also increased the stability of a 1-antitrypsin greatly via combining various stabilizing single amino acid substitutions that were distributed throughout the molecule. The results showed that a substantial increase of stability, over 13 kcal/mol, affected the inhibitory activity with a correlation of 11% activity loss per kcal/mol. The results strongly suggest that the native metastability of proteins is indeed a structural design that regulates protein functions and that the native strain of a 1-antitrypsin distributed throughout the molecule regulates the inhibitory function in a concerted manner.