Ki Hun Park

Chonnam National University, Gwangju, Gwangju, South Korea

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Publications (159)370.51 Total impact

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    ABSTRACT: Depletion of abundant proteins is one of the effective ways to improve detection and identification of low-abundance proteins. Our previous study showed that protamine sulfate precipitation (PSP) method can deplete abundant ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) from leaf proteins and is suitable for their in-depth proteome investigation. In this study, we provide evidence that the PSP method can also be effectively used for depletion of abundant seed-storage proteins (SSPs) from the total seed proteins of diverse legume plants including soybean, broad bean, pea, wild soybean, and peanut. The 0.05% PS was sufficient to deplete major SSPs from all legumes tested except for peanut where 0.1% PS was required. SDS-PAGE, Western blotting and 2DE analyses of PS-treated soybean and peanut seed proteins showed enriched spots in PS-supernatant than total proteins. Coefficient of variation percentage (%CV) and principal component analysis of 2DE spots support the reproducibility, suitability, and efficacy of the PSP method for quantitative and comparative seed proteome analysis. MALDI-TOF-TOF successfully identified some protein spots from soybean and peanut. Hence, this simple, reproducible, economical PSP method has a broader application in depleting plant abundant proteins including SSPs in addition to RuBisCO, allowing discussion for comprehensive proteome establishment and parallel comparative studies in plants.This article is protected by copyright. All rights reserved
    Proteomics 01/2015; · 3.97 Impact Factor
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    ABSTRACT: In Korea, soy (Glycine max (L.) Merr.) leaves are eaten as a seasonal vegetable or pickled in soy sauce. Ethyl acetate extracts of soy leaves (EASL) are enriched in pterocarpans and have potent α-glucosidase inhibitory activity. This study investigated the molecular mechanisms underlying the anti-diabetic effect of EASL in C57BL/6J mice with high-fat diet (HFD)-induced type 2 diabetes. Mice were randomly divided into normal diet (ND), HFD (60 kcal% fat diet), EASL (HFD with 0.56% (wt/wt) EASL), and Pinitol (HFD with 0.15% (wt/wt) pinitol) groups. Weight gain and abdominal fat accumulation were significantly suppressed by EASL. Levels of plasma glucose, HbA1c, and insulin in the EASL group were significantly lower than those of the HFD group, and the pancreatic islet of the EASL group had greater size than those of the HFD group. EASL group up-regulated neurogenin 3 (Ngn3), paired box 4 (Pax4), and v-maf musculoaponeurotic fibrosarcoma oncogene homolog A (MafA), which are markers of pancreatic cell development, as well as insulin receptor substrate 1 (IRS1), IRS2, and glucose transporter 4 (GLUT4), which are related to insulin sensitivity. Furthermore, EASL suppressed genes involved in hepatic gluconeogenesis and steatosis. These results suggest that EASL improves plasma glucose and insulin levels in mice with HDF-induced type 2 diabetes by regulating β-cell proliferation and insulin sensitivity.
    Molecules 11/2014; 19(11):18493-510. · 2.10 Impact Factor
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    Bulletin- Korean Chemical Society 06/2014; 35(10):3095-3098. · 0.84 Impact Factor
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    ABSTRACT: A major modification to the QuEChERS (quick, easy, cheap, effective, rugged and safe) method was developed for the analysis of etoxazole in red pepper using gas chromatography coupled with a nitrogen–phosphorus detector. Etoxazole was extracted with acetonitrile, partitioned with magnesium sulfate and purified with a solid-phase extraction cartridge. The method showed good linearity with a determination coefficient (R2) of 0.998 for the 0.02–2.0 mg/L concentration range. The method was validated using blank red pepper spiked at 0.2 and 1.0 mg/kg, and the average recovery rate was 74.4–79.1% with relative standard deviations <5% for intra- and inter-day precision. The limits of detection and quantification were 0.007 and 0.02 mg/kg, respectively. The developed method was successfully applied to field-incurred samples, and the presence of etoxazole residues was confirmed using gas chromatography/mass spectrometry. Copyright © 2014 John Wiley & Sons, Ltd.
    Biomedical Chromatography 06/2014; 28(6). · 1.95 Impact Factor
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    ABSTRACT: Angelica keiskei is used as popular functional food stuff. However, quantitative analysis of this plant’s metabolites has not yet been disclosed. The principal phenolic compounds (1–16) within A. keiskei were isolated, enabling us to quantify the metabolites within different parts of the plant. The specific quantification of metabolites (1–16) was accomplished by multiple reaction monitoring (MRM) using a quadruple tandem mass spectrometer. The limit of detection and limit of quantitation were calculated as 0.4–44 μg/kg and 1.5–148 μg/kg, respectively. Abundance and composition of these metabolites varied significantly across different parts of plant. For example, the abundance of chalcones (12–16) decreased as follows: root bark (10.51 mg/g) > stems (8.52 mg/g) > leaves (2.63 mg/g) > root cores (1.44 mg/g). The chalcones were found to be responsible for the xanthine oxidase (XO) inhibition shown by this plant. The most potent inhibitor, xanthoangelol inhibited XO with an IC50 of 8.5 μM. Chalcones (12–16) exhibited mixed-type inhibition characteristics.
    Food Chemistry 06/2014; 153:20–27. · 3.26 Impact Factor
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    ABSTRACT: Escherichia coli 6-carboxytetrahydropterin synthase (eCTPS), a homologue of 6-pyruvoyltetrahydropterin synthase (PTPS), possesses a much stronger catalytic activity to cleave the side chain of sepiapterin in vitro compared with genuine PTPS activity and catalyzes the conversion of dihydroneopterin triphosphate to 6-carboxy-5,6,7,8-tetrahydropterin in vivo. Crystal structures of wild-type apo eCTPS and of a Cys27Ala mutant eCTPS complexed with sepiapterin have been determined to 2.3 and 2.5 Å resolution, respectively. The structures are highly conserved at the active site and the Zn(2+) binding site. However, comparison of the eCTPS structures with those of mammalian PTPS homologues revealed that two specific residues, Trp51 and Phe55, that are not found in mammalian PTPS keep the substrate bound by stacking it with their side chains. Replacement of these two residues by site-directed mutagenesis to the residues Met and Leu, which are only found in mammalian PTPS, converted eCTPS to the mammalian PTPS activity. These studies confirm that these two aromatic residues in eCTPS play an essential role in stabilizing the substrate and in the specific enzyme activity that differs from the original PTPS activity. These aromatic residues Trp51 and Phe55 are a key signature of bacterial PTPS enzymes that distinguish them from mammalian PTPS homologues.
    Acta Crystallographica Section D Biological Crystallography 05/2014; 70(Pt 5):1212-23. · 7.23 Impact Factor
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    ABSTRACT: Kresoxim-methyl and its two thermolabile metabolites, BF 490-2 and BF 490-9, were analyzed in pear using a pepper leaf matrix protection to maintain the metabolites inside the gas chromatography system. Samples were extracted with a mixture of ethyl acetate and n-hexane (1:1, v/v) and purified and/or separated using a solid phase extraction procedure. The pepper leaf matrix was added and optimized with cleaned pear extract to enhance metabolite sensitivity. Matrix matched calibration was used for kresoxim-methyl in the pear matrix and for metabolites in the pear mixed with pepper leaf matrix. Good linearity was obtained for all analytes with a coefficient of determination, r2 ⩾ 0.992. Limits of detection (LOD) and quantification (LOQ) were 0.006 and 0.02 mg kg−1 and 0.02 and 0.065 mg kg−1 for kresoxim-methyl and the metabolites, respectively. Recoveries were carried out at two concentration levels and were 85.6–97.9% with a relative standard deviation <2.5%. The method was successfully applied to field incurred pear samples, and only kresoxim-methyl was detected at a concentration of 0.03 mg kg−1.
    Journal of Advanced Research 05/2014; 5(3):329–335.
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    ABSTRACT: Sialidase catalyzes the removal of a terminal sialic acid from glycoconjugates and plays a pivotal role in nutrition, cellular interactions and pathogenesis mediating various infectious diseases including cholera, influenza and sepsis. An array of antiviral sialidase agents have been developed and are commercially available, such as zanamivir and oseltamivir for treating influenza. However, the development of bacterial sialidase inhibitors has been much less successful. Here, natural polyphenolic geranylated flavonoids which show significant inhibitory effects against Cp-NanI, a sialidase from Clostridium perfringens, are reported. This bacterium causes various gastrointestinal diseases. The crystal structure of the Cp-NanI catalytic domain in complex with the best inhibitor, diplacone, is also presented. This structure explains how diplacone generates a stable enzyme-inhibitor complex. These results provide a structural framework for understanding the interaction between sialidase and natural flavonoids, which are promising scaffolds on which to discover new anti-sialidase agents.
    Acta Crystallographica Section D Biological Crystallography 05/2014; 70(Pt 5):1357-65. · 7.23 Impact Factor
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    ABSTRACT: Anti-rotaviral activities of Sophora flavescens extract (SFE) and stevioside (SV) from Stevia rebaudiana Bertoni either singly or in various combinations were examined in vitro and in vivo using a porcine rotavirus G5[P7] strain. Combination of SFE and SV inhibited in vitro virus replication more efficiently than each single treatment. In the piglet model, SV had no effect on rotavirus enteritis, whereas SFE improved but did not completely cure rotaviral enteritis. Interestingly, combination therapy of SFE and SV alleviated diarrhea, and markedly improved small intestinal lesion score and fecal virus shedding. Acute toxicity tests including the piglet lethal dose 50, and body weight, organ weight and pathological changes for the combination therapy did not show any adverse effect on the piglets. These preliminary data suggest that the combination therapy of SV and SFE is a potential curative medication for rotaviral diarrhea in pigs. Determination of the efficacy of this combination therapy in other species including humans needs to be addressed in the future.
    Research in Veterinary Science 04/2014; · 1.51 Impact Factor
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    ABSTRACT: The present work was reported on investigation of saponin profiles in nine different legume seeds, including soybean, adzuki bean, cowpea, common bean, scarlet runner bean, lentil, chick pea, hyacinth bean, and broad bean using ultra performance liquid chromatography with photodiode array detector and electrospray ionisation/mass spectrometry (UPLC-PDA-ESI/MS) technique. A total of twenty saponins were characterised under rapid and simple conditions within 15min by the 80% methanol extracts of all species. Their chemical structures were elucidated as soyasaponin Ab (1), soyasaponin Ba (2), soyasaponin Bb (3), soyasaponin Bc (4), soyasaponin Bd (5), soyasaponin αg (6), soyasaponin βg (7), soyasaponin βa (8), soyasaponin γg (9), soyasaponin γa (10), azukisaponin VI (11), azukisaponin IV (12), azukisaponin II (13), AzII (14), AzIV (15), lablaboside E (16), lablaboside F (17), lablaboside D (18), chikusetusaponin IVa (19), and lablab saponin I (20). The individual and total saponin compositions exhibited remarkable differences in all legume seeds. In particular, soyasaponin βa (8) was detected the predominant composition in soybean, cowpea, and lentil with various concentrations. Interestingly, soybean, adzuki bean, common bean, and scarlet runner bean had high saponin contents, while chick pea and broad bean showed low contents.
    Food Chemistry 03/2014; 146:270-7. · 3.26 Impact Factor
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    ABSTRACT: Stilbene urea derivatives as a novel and competitive class of non-glycosidic α-glucosidase inhibitors are effective for the treatment of type II diabetes and obesity. The main purposes of our molecular modeling study are to explore the most suitable binding poses of stilbene derivatives with analyzing the binding affinity differences and finally to develop a pharmacophore model which would represents critical features responsible for α-glucosidase inhibitory activity. Three-dimensional structure of S. cerevisiae α-glucosidase was built by homology modeling method and the structure was used for the molecular docking study to find out the initial binding mode of compound 12, which is the most highly active one. The initial structure was subjected to molecular dynamics (MD) simulations for protein structure adjustment at compound 12-bound state. Based on the adjusted conformation, the more reasonable binding modes of the stilbene urea derivatives were obtained from molecular docking and MD simulations. The binding mode of the derivatives was validated by correlation analysis between experimental Ki value and interaction energy. Our results revealed that the binding modes of the potent inhibitors were engaged with important hydrogen bond, hydrophobic, and π-interactions. With the validated compound 12-bound structure obtained from combining approach of docking and MD simulation, a proper four featured pharmacophore model was generated. It was also validated by comparison of fit values with the Ki values. Thus, these results will be helpful for understanding the relationship between binding mode and bioactivity and for designing better inhibitors from stilbene derivatives.
    PLoS ONE 01/2014; 9(1):e85827. · 3.53 Impact Factor
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    ABSTRACT: Enzyme binding affinity has been recently introduced as a selective screening method to identify bioactive substances within complex mixtures. We used an assay which identified small molecule binders of acetylcholinesterase (AChE) using the following series of steps: incubation of enzyme with extract; centrifugation and filtration; identification of small molecule content in the flow through. The crude extract contained 10 peaks in the UPLC chromatogram. However after incubation the enzyme, six peaks were reduced, indicating these compounds bound AChE. All these isolated compounds (2, 3, and 5-8) significantly inhibited human AChE with IC50s = 5.4-15.0 υM and butyrylcholinsterase (IC50s = 0.7-11.0 υM). All compounds exhibited reversible mixed kinetics. Consistent with the binding screen and fluorescence quenching, gamma-mangostin 6 had a much higher affinity for AChE than 9-hydroxycalabaxanthone 9. This validates this screening protocol as a rapid method to identify inhibitors of AChE.
    Journal of Agricultural and Food Chemistry 01/2014; · 3.11 Impact Factor
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    ABSTRACT: Tribulus terrestris fruits are well known for their usage in pharmaceutical preparations and food supplements. The methanol extract of T. terrestris fruits showed potent inhibition against the papain-like protease (PLpro), an essential proteolylic enzyme for protection to pathogenic virus and bacteria. Subsequent bioactivity-guided fractionation of this extract led to six cinnamic amides (1-6) and ferulic acid (7). Compound 6 emerged as new compound possessing the very rare carbinolamide motif. These compounds (1-7) were evaluated for severe acute respiratory syndrome coronavirus (SARS-CoV) PLpro inhibitory activity to identify their potencies and kinetic behavior. Compounds (1-6) displayed significant inhibitory activity with IC50 values in the range 15.8-70.1 µM. The new cinnamic amide 6 was found to be most potent inhibitor with an IC50 of 15.8 µM. In kinetic studies, all inhibitors exhibited mixed type inhibition. Furthermore, the most active PLpro inhibitors (1-6) were proven to be present in the native fruits in high quantities by HPLC chromatogram and liquid chromatography with diode array detection and electrospray ionization mass spectrometry (LC-DAD-ESI/MS).
    Biological & Pharmaceutical Bulletin 01/2014; 37(6):1021-8. · 1.78 Impact Factor
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    ABSTRACT: Flemingia philippinensis is used as a foodstuff or medicinal plant in the tropical regions of China. The methanol (95%) extract of the roots of this plant showed potent tyrosinase inhibition (80% inhibition at 30μg/ml). Activity-guided isolation yielded six polyphenols that inhibited both the monophenolase (IC50=1.01-18.4μM) and diphenolase (IC50=5.22-84.1μM) actions of tyrosinase. Compounds 1-6 emerged to be three new polyphenols and three known flavanones, flemichin D, lupinifolin and khonklonginol H. The new compounds (1-3) were identified as dihydrochalcones which we named fleminchalcones (A-C), respectively. The most potent inhibitor, dihydrochalcone (3) showed significant inhibitions against both the monophenolase (IC50=1.28μM) and diphenolase (IC50=5.22μM) activities of tyrosinase. Flavanone (4) possessing a resorcinol group also inhibited monophenolase (IC50=1.79μM) and diphenolase (IC50=7.48μM) significantly. In kinetic studies, all isolated compounds behaved as competitive inhibitors. Fleminchalcone A was found to have simple reversible slow-binding inhibition against monophenolase.
    Bioorganic & medicinal chemistry 12/2013; · 2.82 Impact Factor
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    ABSTRACT: Bacterial neuraminidase (NA) is one of the key enzymes involved in pathogenesis of inflammation during infection. The organic extract of the roots of Flemingia philippinensis showed high bacterial NA inhibitory activity with an IC50 of around 5μg/mL. Activity-guided separation of the methanol extract yielded nine prenylated isoflavones together with the novel species isoflavone (2) which was given the name flemingsin. Isolated prenylated isoflavones (1-9) were evaluated for NA inhibition and their IC50 values were determined to range between 0.30 and 56.8μM. The most potent inhibitor 4 (IC50=300nM, Ki=130nM) features a catechol motif in the B-ring and a furan in the A-ring. Structure-activity analysis also showed a 4-hydroxyl group within the B-ring was essential for NA inhibitory activity, because isoflavone (9) having protected 4-hydroxyl group was much less potent than its hydroxylated counterpart. All neuraminidase compounds screened were found to be reversible noncompetitive inhibitors. Furthermore, the most active NA inhibitors (1-9) were proven to be present in the native roots in high quantities by HPLC and LC-DAD-ESI/MS.
    Bioorganic & medicinal chemistry 09/2013; · 2.82 Impact Factor
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    ABSTRACT: This paper describes a comparison of the properties of the three versions of the QuEChERS method (quick, easy, cheap, effective, rugged and safe) - the original (unbuffered), acetate-buffered, and citrate-buffered methods - for the determination of fenobucarb residues in beef muscles via liquid chromatography-electrospray ionisation tandem mass spectrometry (LC-ESI(+)-MS/MS). The recovery results were good for all the versions; however, the acetate-buffered version gave higher and more consistent recoveries for fenobucarb than the other versions. Performance characteristics, such as linearity, accuracy, and precision were determined. Matrix-matched standard calibration was used for quantification, obtaining recoveries in the range of 83.7-93.4% with relative standard deviations of <5%, at two spiking levels: 10 and 40μg/kg. The limits of detection (LOD) and quantification (LOQ) were estimated to be 1.5 and 5μg/kg, respectively. Finally, the method was applied to the analysis of 15 market samples, and no residues were found over the limit of quantification. The method developed was found able to determine the analyte with satisfactory intensity and accuracy.
    Food Chemistry 06/2013; 138(4):2306-11. · 3.26 Impact Factor
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    ABSTRACT: The pre-harvest residue limit (PHRL) of abamectin (abamectin B1a and B1b) in Perilla frutescens leaves grown under greenhouse conditions were investigated using high-performance liquid chromatography with a fluorescence detector. Samples were extracted with acetonitrile. The extract was purified through a solid phase extraction procedure. Then the purified extract was derivatized with trifluoroacetic anhydride and N-methylimidazole to form a strong stable fluorescent derivative of abamectin. Finally, derivatized abamectins were conveyed to the detector via an Atlantis C18 column, with water and methanol as a mobile phase. Calibration curves were linear over the calibration ranges with coefficients of determinants r (2) ≥ 0.999. The limits of detection and quantification were 0.0033 and 0.01 mg kg(-1) for abamectin B1a and B1b, respectively. Recovery was assessed in a control matrix at two different fortification concentrations, with three replicates for each concentration. Good recoveries were obtained for the target analytes and ranged from 82.11 to 93.03 %, with relative standard deviations of less than 8 %. The rate of disappearance of total abamectin on perilla leaves for recommended and double the recommended doses was described as first-order kinetics with a half-life of 0.7 days. Using the PHRL curve, we could predict the residue level of total abamectin to be 0.92 mg kg(-1) at 7 days before harvest or 0.26 mg kg(-1) at 4 days before harvest, which would be below the provisional MRL designed by the Korea Food and Drug Administration.
    Environmental Monitoring and Assessment 06/2013; · 1.68 Impact Factor
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    ABSTRACT: Chelidonium majus L. is an herbal plant that is commonly used in Western phytotherapy and traditional Chinese medicine for diuretic, antitussive, eye-regenerative, anti-osteoporotic, and radioprotective purposes. In this study, we purified 6-acetonyl-5,6-dihydrosanguinarine (ADS) from C. majus and investigated its immune-stimulatory effect. We found that ADS has the potential to induce the inflammatory cytokines TNF-α, IL-6, and IL-8 in macrophages and dendritic cells (DCs), that NFκB activation is a critical mediator of ADS-induced cytokine production, and that the activation of NFκB was dependent on reactive oxygen species (ROS). ADS induced phosphorylation of ERK and JNK, which was also associated with NFκB activation; phosphorylarion and cytokine production were inhibited by ROS scavenger and by specific MAPK inhibitors. Taken together, the results suggest that ADS from C. majus, as a positive immune modulator, induces inflammatory cytokines that might improve immunity, via the ROS-ERK/JNK-NFκB pathway.
    Food and chemical toxicology: an international journal published for the British Industrial Biological Research Association 05/2013; · 2.99 Impact Factor
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    ABSTRACT: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the most abundant plant leaf protein, hampering deep analysis of the leaf proteome. Here, we describe a novel protamine sulfate precipitation (PSP) method for the depletion of RuBisCO. For this purpose, soybean leaf total proteins were extracted using Tris-Mg/NP-40 extraction buffer. Obtained clear supernatant was subjected to the PSP method, followed by 13% SDS-PAGE analysis of total, PS-supernatant and -precipitation derived protein samples. In a dose-dependent experiment, 0.1% (w/v) PS was found to be sufficient for precipitating RuBisCO large and small subunits (LSU and SSU). Western-blot analysis confirmed no detection of RuBisCO LSU in the PS-supernatant proteins. Application of this method to Arabidopsis, rice, and maize leaf proteins revealed results similar to soybean. Furthermore, 2-DE analyses of PS-treated soybean leaf displayed enriched protein profile for the protein sample derived from the PS-supernatant than total proteins. Some enriched 2-D spots were subjected to MALDI-TOF-TOF analysis and were successfully assigned for their protein identity. Hence, the PSP method is: (i) simple, fast, economical, and reproducible for RuBisCO precipitation from the plant leaf sample; (ii) applicable to both dicot and monocot plants; and (iii) suitable for down-stream proteomics analysis.
    Proteomics 04/2013; · 3.97 Impact Factor

Publication Stats

1k Citations
370.51 Total Impact Points


  • 2012–2014
    • Chonnam National University
      • College of Agriculture and Life Sciences
      Gwangju, Gwangju, South Korea
    • University of Dhaka
      Mujib City, Dhaka, Bangladesh
  • 1994–2014
    • Gyeongsang National University
      • • Institute of Agriculture and Life Science
      • • Department of Agricultural Chemistry
      • • Division of Applied Life Science
      • • Department of Chemistry
      Shinshū, South Gyeongsang, South Korea
  • 2008–2011
    • Seoul National University
      • • Department of Pharmacy
      • • Cancer Research Institute
      Seoul, Seoul, South Korea
  • 2006–2011
    • Korea Research Institute of Bioscience and Biotechnology KRIBB
      • National Research Laboratory of Lipid Metabolism and Atherosclerosis
      Anzan, Gyeonggi Province, South Korea
  • 2010
    • Korea Institute of Radiological & Medical Sciences
      Sŏul, Seoul, South Korea
  • 2002
    • University of California, Berkeley
      • Department of Chemistry
      Berkeley, California, United States