• Bulletin of the Korean Chemical Society
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• v.33 no.6
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• pp.2005-2011
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• 2012

Nopp140 is a highly phosphorylated protein that resides in the nucleolus of mammalian cell and is involved in the biogenesis of the nucleolus. It interacts with a variety of proteins related to the synthesis and assembly of the ribosome. It also can bind to a ubiquitous protein kinase CK2 that mediates cell growth and prevents apoptosis. We found that Nopp140 is an intrinsically unfolded protein (IUP) lacking stable secondary structures over its entire sequence of 709 residues. We discovered that mitoxantrone, an anticancer agent, was able to enhance the interaction between Nopp140 and CK2 and maintain suppressed activity of CK2. Surface plasma resonance studies on different domains of Nopp140 show that the C-terminal region of Nopp140 is responsible for binding with mitoxantrone. Our results present an interesting example where a small chemical compound binds to an intrinsically unfolded protein (IUP) and enhances protein-protein interactions.

• Journal of the Korean Magnetic Resonance Society
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• v.21 no.1
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• pp.26-30
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• 2017

Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as $T_1$, $T_2$, and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.

• Asian-Australasian Journal of Animal Sciences
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• v.4 no.4
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• pp.361-368
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• 1991

In two experiments 640 starcross replacement pullets between 25 and 154 days of age were fed ad libitum on either of 16 diets formed by the combination of $4CP{\times}4ME$ levels to study the interaction of CP and ME on growth performances. In both experiments, feed intake decreased, but protein intake, energy intake, live weight gain and feed conversion efficiency increased and sexual maturity hastened with the increase of dietary protein and/or energy level. The protein conversion efficiency decreased with the increase of dietary protein level. The energy conversion efficiency, however, did not show any relationship with dietary energy level. There was a greater improvement of growth performance due to simultaneous increase of dietary protein and energy level than that of increasing protein or energy alone.

• Journal of Nutrition and Health
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• v.30 no.3
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• pp.266-276
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• 1997

To investigate the effects of dietary protein and calcium levels on calcium and bone metabolism Sprague-Dawley male growing rats weighting approximately 91.4g were divided into four groups and fed one of the following four experimental diets-15% protein 0.2% calcium ; 15% protein 0.5% calcium ; 30% protein 0.2% calcium ; 30% protein 0.5% calcium-for five weeks. Calcium intake and excretion, apparent calcium absorption were measured and bone densities and mineral contents of femur and scapula were analyzed. Calcium excretion through feces and urine was significantly greater in animals receiving diets of higher calcium. Fecal calcium but not urinary calcium excretion was greater when the protein level was increased from 15% to 30%. Apparent calcium absorption rate was significantly higher with lower calcium intakes. Serum alkaline phosphatase activity was significantly higher in 0.2% calcium group than in 0.5% calcium group, while urinary hydroxyproline excretion was essentially same among all experimental groups. Weights and mineral contents or protein. Bone weights were greater, but calcium and ash contents of femur and scapula were lower in animals on the diet containing low calcium and high protein, which suggests that bone metabolism may be affected by the interaction between calcium and protein intake. These results indicate that during growth high protein intake might be beneficial to bone health if the diet is sufficient in calcium, however, if the diet fails to provide an optimum amount of calcium, such practice might be detrimental.

• Bulletin of the Korean Chemical Society
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• v.29 no.4
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• pp.736-740
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• 2008

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 ${^{\circ}C}$ in aqueous solution. The extended solvation model was used to reproduce the enthalpies of $Co^{2+}$-MBP interaction over the whole $Co^{2+}$ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for $Co^{2+}$ ions. The association equilibrium constant is 0.015 ${\mu}M^{-1}$. The molar enthalpy of binding is $\Delta$H = −14.60 kJ $mol^{-1}$.

• Korean Journal of Poultry Science
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• v.30 no.2
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• pp.113-118
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• 2003

In this study, broilers were raised up to 6 weeks of age in a single room to determine if different levels of dietary protein or addition of aluminum sulfate[alum, $Al_2$(SO$_4$)$_3$ㆍ14$H_2O$] to the litter affected growth performance, production of ammonia(NH$_3$) and soluble phosphorus(SP) content of the litter.The experimental treatments consisted of six treatments in a 2x3 factorial arrangements: T$_1$＝23% protein ＋ 0.2% alum to litter; T$_2$＝21% protein ＋ 0.2% alum to litter; T$_3$＝19% protein ＋ 0.2% alum to litter; T$_4$＝23% protein ＋ no alum; T$_{5}$＝21% protein ＋ no alum; T$_{6}$＝19% protein ＋ no alum. For broiler performance, there was no effect of alum addition to the litter, but the dietary protein levels significantly affected feed intake from days 22 to 42(P<0.05) and day 0 to 42(P< 0.05), weight gain during all periods(P<0.05 or 0.01), and feed:gain from day 0 to 21(P<0.05) and day 0 to 42(P<0.05). Alum addition to the litter did not affect body weight at 21 and 42 days, but dietary protein levels has a significant effect on it at both 21(P<0.0l) and 42 days(P<0.05). Alum addition only affected ammonia production at weeks 3(P

• BMB Reports
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• v.34 no.2
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• pp.102-108
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• 2001

A time-dependent folding process was used to determine whether or not protein disulfide isomerase (PDI) plays an important role in the maturation of nascent lactoferrin polypeptides. Interaction between lactoferrin and PDI was analyzed according to the co-immunoprecipitation of the two proteins. The results indicate that lactoferrin folding requires a significant interaction with PDI and its binding is relatively brief compared to other nascent polypeptides. The amount of lactoferrin interacting with PDI increases up to half a minute and sharply decreases beyond this time point. During the refolding process that follows reduction by DTT, lactoferrin polypeptides heavily interact with PDI and the interaction period was extended compared to the normal folding process. In terms of the temperature effect on PDI-lactoferrin interaction, PDI binds to lactoferrin polypeptides longer at a lower temperature (here, $25^{\circ}C$) than $37^{\circ}C$. The lactoferrin-PDI interaction was also studied in vitro. According to the in vitro experiment data, PDI was still functional in cell lysates assisting lactoferrin folding into the mature form. PDI interacts with lactoferrin polypeptides for an extended period during the folding in vitro. During the refolding process in vitro, intermolecular aggregates and refolding oligomers matured into a functional form after PDI binds to the lactoferrin. These results suggest that PDI provides a prolonged chaperoning activity in the refolding processes and that there appears to be a greater requirement for PDI chaperone activity in the refolding of lactoferrin polypeptides.

• The Journal of Natural Sciences
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• v.17 no.1
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• pp.13-29
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• 2006

Most redox-active proteins have thiol-bearing cysteine residues that are sensitive to oxidation. Cysteine thiols oxidized to sulfenic acid are generally unstable, either forming a disulfide with a nearby thiol or being further oxidized to a stable sulfinic acid, which have been viewed as an irreversible protein modification. However, recent studies showed that cysteine residues of certain thiol peroxidases (Prxs) undergo reversible oxidation to sulfinic acid and the reduction reaction is catalyzed by sulfiredoxin (Srx1). Specific Cys residues of various other proteins are also oxidized to sulfinic acid ($Cys-So_2H$). Srxl is considered one of the oxidant proteins with a role in signaling through catalytic reduction of oxidative modification like in the reduction of glutathionylation, a post-translational, oxidative modification that occurs on numerous proteins. In this study, the role of sulfiredoxin in cellular processes, was investigated by studying its interaction with other proteins. Through the yeast two-hybrid system (Y2HS) technique, we have found that Ams1 is a potential and novel interacting protein partner of Srxl. $\alpha$-mannosidase (Ams1) is a resident vacuolar hydrolase which aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing $\alpha$-D-mannose residues. It forms an oligomer in the cytoplasm and under nutrient rich condition and is delivered to the vacuole by the Cytoplasm to Vacuole (Cvt) pathway. Aside from the role of Srxl as a catalyst in the reduction of cysteine sulfenic acid groups, it may play a completely new function in the cellular process as indicated by its interaction with Ams1 of the yeast Saccharomyces cerevisiae.

• Development and Reproduction
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• v.21 no.4
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• pp.449-456
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• 2017

The germline stem cells of the Drosophila ovary continuously produce eggs throughout the life-span. Intricate regulation of stemness and differentiation is critical to this continuous production. The translational regulator Nos is an intrinsic factor that is required for maintenance of stemness in germline stem cells. Nos expression is reduced in differentiating cells at the post-transcriptional level by diverse translational regulators. However, molecular mechanisms underlying Nos repression are not completely understood. Through three distinct protein-protein interaction experiments, we identified specific molecular interactions between translational regulators involved in Nos repression. Our findings suggest a model in which protein complexes assemble on the 3' untranslated region of Nos mRNA in order to regulate Nos expression at the post-transcriptional level.

• Journal of the Korea Society of Computer and Information
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• v.14 no.5
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• pp.175-182
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• 2009

We extracted protein signal delivery path from protein interaction data, using location information and weight of protein. We obtained the protein interaction data by experimenting in two-hybrid system using Yeast. We simulated function's data of Hypotonic Shock comparing to signal delivery path provided in KEGG from the results. We measured process running period as well. In future, this research can be key to discover the origin of various genetic diseases and develop treatment.