9 results on '"Ryoo G"'
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2. An effective storage method during a sampling of speech signals.
- Author
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Bae, M., Kim, U., Ryoo, G., and Whang, H.
- Published
- 1992
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3. Ultrafast Synthesis of Hard Carbon Anodes for Sodium-ion Batteries: An Intense-Pulsed-Light-Assisted Approach to Photothermal Carbonization of Polymer/Carbon Nanotube Composite Films.
- Author
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Ryoo G, Kim MJ, Kim MS, Shin S, Lee JW, Kim BG, Lee DG, Kim Y, Seo H, Cho JY, Han JT, Jeong SY, Kim J, Lee DY, Jeong HJ, and Park JH
- Abstract
The conventional carbonization process for synthesizing hard carbons (HCs) requires high-temperature furnace operations exceeding 1000 °C, leading to excessive energy consumption and lengthy processing times, which necessitates the exploration of more efficient synthesis methods. This study demonstrates the rapid preparation of HC anodes using intense pulsed light (IPL)-assisted photothermal carbonization without the prolonged and complex operations typical of traditional carbonization methods. A composite film of microcrystalline cellulose (MCC) and single-walled carbon nanotubes (SWCNTs) is carbonized at high temperatures in less than 1 min. The SWCNTs efficiently absorbed light energy, enabling ultrafast heating and eliminating the need for prolonged, high-energy furnace-based processes. The IPL-assisted HC anodes exhibited excellent electrochemical performance, with an initial desodiation capacity of 260.4 mAh g⁻¹
anode and 97.5% capacity retention after 200 cycles. These results are comparable to those achieved using traditional furnace-based carbonization processes, such as carbonizing HC anodes at 1200 °C, validating the effectiveness of IPL-assisted processes. Additionally, surface and structural analyses revealed the development of pseudo-graphitic domains, crucial for enhanced sodium-ion storage. This research highlights IPL-assisted photothermal carbonization as a viable, time-efficient, and energy-saving alternative to conventional methods, offering a sustainable pathway for the large-scale production of HC anodes for future sodium-ion battery technologies., (© 2025 Wiley‐VCH GmbH.)- Published
- 2025
- Full Text
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4. Energy Storage Performance of Electrode Materials Derived from Manganese Metal-Organic Frameworks.
- Author
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Ryoo G, Kim SK, Lee DK, Kim YJ, Han YS, and Jung KH
- Abstract
Metal-organic frameworks (MOFs) are porous materials assembled using metal and organic linkers, showing a high specific surface area and a tunable pore size. Large portions of metal open sites in MOFs can be exposed to electrolyte ions, meaning they have high potential to be used as electrode materials in energy storage devices such as supercapacitors. Also, they can be easily converted into porous metal oxides by heat treatment. In this study, we obtained high energy storage performance by preparing electrode materials through applying heat treatment to manganese MOFs (Mn-MOFs) under air. The chemical and structural properties of synthesized and thermally treated Mn-MOFs were measured by Fourier-transform infrared spectroscopy (FTIR), Raman spectroscopy, X-ray diffraction (XRD), X-ray photoelectron spectroscopy (XPS), and transmission electron microscopy (TEM). The surface area and porosity were investigated by nitrogen adsorption/desorption isotherms. The electrochemical properties were studied by cyclic voltammetry (CV) and galvanostatic charge-discharge (GCD) using a three-electrode cell. It was found that Mn-MOF electrodes that underwent heat treatment at 400 °C under air consisted of Mn
2 O3 with high specific surface area and porosity. They also showed a superior specific capacitance of 214.0 F g-1 and an energy density value of 29.7 Wh kg-1 (at 0.1 A g-1 ) compared to non-treated Mn-MOFs.- Published
- 2024
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5. Expanding therapeutic utility of carfilzomib for breast cancer therapy by novel albumin-coated nanocrystal formulation.
- Author
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Park JE, Park J, Jun Y, Oh Y, Ryoo G, Jeong YS, Gadalla HH, Min JS, Jo JH, Song MG, Kang KW, Bae SK, Yeo Y, and Lee W
- Subjects
- Animals, Antineoplastic Agents therapeutic use, Biological Transport, Cyclodextrins chemistry, Drug Compounding, Drug Liberation, Drug Stability, Female, Humans, Mice, Mice, Inbred BALB C, Oligopeptides pharmacokinetics, Oligopeptides therapeutic use, Poloxamer chemistry, Proteasome Inhibitors therapeutic use, Solubility, Surface Properties, Tissue Distribution, Albumins chemistry, Antineoplastic Agents chemistry, Breast Neoplasms drug therapy, Drug Carriers chemistry, Nanoparticles chemistry, Oligopeptides chemistry, Proteasome Inhibitors chemistry
- Abstract
Carfilzomib (CFZ) is the second-in-class proteasome inhibitor with much improved efficacy and safety profiles over bortezomib in multiple myeloma patients. In expanding the utility of CFZ to solid cancer therapy, the poor aqueous solubility and in vivo instability of CFZ are considered major drawbacks. We investigated whether a nanocrystal (NC) formulation can address these issues and enhance anticancer efficacy of CFZ against breast cancer. The surface of NC was coated with albumin in order to enhance the formulation stability and drug delivery to tumors via interactions with albumin-binding proteins located in and near cancer cells. The novel albumin-coated NC formulation of CFZ (CFZ-alb NC) displayed improved metabolic stability and enhanced cellular interactions, uptake and cytotoxic effects in breast cancer cells in vitro. Consistently, CFZ-alb NC showed greater anticancer efficacy in a murine 4T1 orthotopic breast cancer model than the currently used cyclodextrin-based formulation. Overall, our results demonstrate the potential of CFZ-alb NC as a viable formulation for breast cancer therapy., (Copyright © 2019 Elsevier B.V. All rights reserved.)
- Published
- 2019
- Full Text
- View/download PDF
6. Inhibition of Organic Anion Transporting Polypeptide 1B1 and 1B3 by Betulinic Acid: Effects of Preincubation and Albumin in the Media.
- Author
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Oh Y, Jeong YS, Kim MS, Min JS, Ryoo G, Park JE, Jun Y, Song YK, Chun SE, Han S, Bae SK, Chung SJ, and Lee W
- Subjects
- Animals, Cattle, HEK293 Cells, Humans, Liver-Specific Organic Anion Transporter 1 metabolism, Male, Pentacyclic Triterpenes, Rats, Rats, Sprague-Dawley, Solute Carrier Organic Anion Transporter Family Member 1B3 metabolism, Triterpenes pharmacokinetics, Betulinic Acid, Liver-Specific Organic Anion Transporter 1 antagonists & inhibitors, Serum Albumin metabolism, Solute Carrier Organic Anion Transporter Family Member 1B3 antagonists & inhibitors, Triterpenes chemistry, Triterpenes pharmacology
- Abstract
Betulinic acid (BA), a plant-derived pentacyclic triterpenoid, may interact with the members of the organic anion transporting polypeptide 1B subfamily. Here, we investigated the interactions of BA and its analogs with OATP1B1/3 and rat Oatp1b2 in vitro and in vivo. BA inhibited the activity of OATP1B1/3 and rat Oatp1b2 in vitro. Systemic exposure of atorvastatin was substantially altered with the intravenous co-administration of BA (20 mg/kg). Preincubation (incubation with inhibitors, followed by washout) with BA led to a sustained inhibition of OATP1B3, which recovered rapidly in the media containing 10% fetal bovine serum. The addition of albumin to the media decreased intracellular concentrations of BA and expedited the recovery of OATP1B3 activity following preincubation. For asunaprevir and cyclosporin A (previously known to inhibit OATP1B3 upon preincubation), the addition of albumin to the media shortened recovery time with asunaprevir, but not with cyclosporin A. Overall, our results showed that BA inhibits OATP1B transporters in vitro and may incur hepatic transporter-mediated drug interactions in vivo. Our results identify BA as another OATP1B3 inhibitor with preincubation effect and suggest that the preincubation effect and its duration is impacted by altered equilibrium of inhibitors between intracellular and extracellular space (e.g., albumin in the media)., (Copyright © 2018 American Pharmacists Association®. Published by Elsevier Inc. All rights reserved.)
- Published
- 2018
- Full Text
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7. Alternative Splicing: Expanding Diversity in Major ABC and SLC Drug Transporters.
- Author
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Park JE, Ryoo G, and Lee W
- Subjects
- ATP-Binding Cassette Transporters physiology, Humans, Solute Carrier Proteins physiology, ATP-Binding Cassette Transporters genetics, Alternative Splicing, Solute Carrier Proteins genetics
- Abstract
Alternative splicing is an important mechanism of genetic regulation enhancing diversity and complexity of the transcriptome and proteome from the finite number of genes. Many reported cases demonstrate that alternative splicing events can lead to changes in the expression/function of proteins during disease development and progression. For pharmacogenes that can influence drug disposition and response, the role of alternative splicing has begun to receive increasing attention as an under-explored source of variable drug response. Here, we provide an overview of alternative spliced variants reported for the major drug transporters of SLC and ABC families with their possible implications in disease and drug therapy. As more comprehensive analyses on the abundance and functional outcomes of variably spliced isoforms of major drug transporters become available, it will be possible to utilize the obtained knowledge as novel therapeutic targets for tailored treatment strategies.
- Published
- 2017
- Full Text
- View/download PDF
8. The N-terminal region of organic anion transporting polypeptide 1B3 (OATP1B3) plays an essential role in regulating its plasma membrane trafficking.
- Author
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Chun SE, Thakkar N, Oh Y, Park JE, Han S, Ryoo G, Hahn H, Maeng SH, Lim YR, Han BW, and Lee W
- Subjects
- Amino Acid Sequence, Animals, Cell Line, Cell Membrane metabolism, Humans, Mice, Organic Anion Transporters, Sodium-Independent chemistry, Organic Anion Transporters, Sodium-Independent genetics, Phosphorylation, Point Mutation, Protein Transport, Rats, Sequence Homology, Amino Acid, Solute Carrier Organic Anion Transporter Family Member 1B3, Subcellular Fractions metabolism, Organic Anion Transporters, Sodium-Independent physiology
- Abstract
Organic anion transporting polypeptide 1B3 (OATP1B3) is a major influx transporter mediating the hepatic uptake of various endogenous substrates as well as clinically important drugs such as statins and anticancer drugs. However, molecular mechanisms controlling the membrane trafficking of OATP1B3 have been largely unknown. Several reports recently indicated the presence of a distinct, cancer-type OATP1B3 variant lacking the N-terminal 28 amino acids compared to OATP1B3 expressed in non-malignant hepatocytes. Interestingly, the cancer-type OATP1B3 variant is located predominantly in the cytoplasm, implicating the involvement of the N-terminal region of OATP1B3 in its membrane trafficking. In the current study, we set out to experimentally validate the importance of the N-terminal region of OATP1B3 and to identify responsible sequence motif(s) in that region. A number of truncation or point mutants of OATP1B3 were transiently expressed in HEK293T, HCT-8 or MDCK II cells and their expression in cytoplasmic and surface membrane fractions were analyzed by immunoblotting. Our results indicated that the N-terminal sequence of OATP1B3, in particular, at the amino acid positions between 12 and 28, may be indispensable in its membrane trafficking. Moreover, our results using a fusion construct indicated that the first 50 amino acids of OATP1B3 are sufficient for its membrane localization. The importance of the N-terminal region in membranous localization was shared among the other OATP1B subfamily members, OATP1B1 and rat Oatp1b2. Our efforts to identify the responsible amino acid(s) or structure motif(s) in the N-terminal region did not pinpoint individual amino acids or motifs with putative secondary structures. Our current findings however demonstrate that the N-terminal region is important for the membrane localization of the OATP1B subfamily members and should facilitate future investigations of the mechanisms involved in the regulation and membrane trafficking of these important transporter proteins., (Copyright © 2017 Elsevier Inc. All rights reserved.)
- Published
- 2017
- Full Text
- View/download PDF
9. Polymer micelle formulation for the proteasome inhibitor drug carfilzomib: Anticancer efficacy and pharmacokinetic studies in mice.
- Author
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Park JE, Chun SE, Reichel D, Min JS, Lee SC, Han S, Ryoo G, Oh Y, Park SH, Ryu HM, Kim KB, Lee HY, Bae SK, Bae Y, and Lee W
- Subjects
- Animals, Cell Line, Tumor, Disease Models, Animal, Drug Compounding, Drug Design, Lung Neoplasms drug therapy, Lung Neoplasms metabolism, Lung Neoplasms pathology, Male, Mice, Mice, Inbred NOD, Mice, SCID, Proteasome Endopeptidase Complex metabolism, Xenograft Model Antitumor Assays, Antineoplastic Agents administration & dosage, Antineoplastic Agents pharmacokinetics, Micelles, Oligopeptides administration & dosage, Oligopeptides pharmacokinetics, Polymers, Proteasome Inhibitors administration & dosage, Proteasome Inhibitors pharmacokinetics
- Abstract
Carfilzomib (CFZ) is a peptide epoxyketone proteasome inhibitor approved for the treatment of multiple myeloma (MM). Despite the remarkable efficacy of CFZ against MM, the clinical trials in patients with solid cancers yielded rather disappointing results with minimal clinical benefits. Rapid degradation of CFZ in vivo and its poor penetration to tumor sites are considered to be major factors limiting its efficacy against solid cancers. We previously reported that polymer micelles (PMs) composed of biodegradable block copolymers poly(ethylene glycol) (PEG) and poly(caprolactone) (PCL) can improve the metabolic stability of CFZ in vitro. Here, we prepared the CFZ-loaded PM, PEG-PCL-deoxycholic acid (CFZ-PM) and assessed its in vivo anticancer efficacy and pharmacokinetic profiles. Despite in vitro metabolic protection of CFZ, CFZ-PM did not display in vivo anticancer efficacy in mice bearing human lung cancer xenograft (H460) superior to that of the clinically used cyclodextrin-based CFZ (CFZ-CD) formulation. The plasma pharmacokinetic profiles of CFZ-PM were also comparable to those of CFZ-CD and the residual tumors that persisted in xenograft mice receiving CFZ-PM displayed an incomplete proteasome inhibition. In summary, our results showed that despite its favorable in vitro performances, the current CFZ-PM formulation did not improve in vivo anticancer efficacy and accessibility of active CFZ to solid cancer tissues over CFZ-CD. Careful consideration of the current results and potential confounding factors may provide valuable insights into the future efforts to validate the potential of CFZ-based therapy for solid cancer and to develop effective CFZ delivery strategies that can be used to treat solid cancers.
- Published
- 2017
- Full Text
- View/download PDF
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