Institution
Pukyong National University
Education•Busan, South Korea•
About: Pukyong National University is a education organization based out in Busan, South Korea. It is known for research contribution in the topics: Phosphor & Luminescence. The organization has 6689 authors who have published 14681 publications receiving 233751 citations. The organization is also known as: PKNU.
Topics: Phosphor, Luminescence, Photoluminescence, Olive flounder, Thin film
Papers published on a yearly basis
Papers
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TL;DR: The insertion of PbX2 into Cs4Pb X6 provides a means of accessing CsPbX3 nanocrystals in a wide variety of sizes, shapes, and compositions, an important aspect for the development of precisely tuned perovskite nanocrystal inks.
Abstract: We have developed a colloidal synthesis of nearly monodisperse nanocrystals of pure Cs4PbX6 (X = Cl, Br, I) and their mixed halide compositions with sizes ranging from 9 to 37 nm. The optical absorption spectra of these nanocrystals display a sharp, high energy peak due to transitions between states localized in individual PbX64– octahedra. These spectral features are insensitive to the size of the particles and in agreement with the features of the corresponding bulk materials. Samples with mixed halide composition exhibit absorption bands that are intermediate in spectral position between those of the pure halide compounds. Furthermore, the absorption bands of intermediate compositions broaden due to the different possible combinations of halide coordination around the Pb2+ ions. Both observations are supportive of the fact that the [PbX6]4– octahedra are electronically decoupled in these systems. Because of the large band gap of Cs4PbX6 (>3.2 eV), no excitonic emission in the visible range was observed...
453 citations
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TL;DR: The results show that APTBP significantly inhibited lipid peroxidation in linoleic acid emulsion system and also quenched free radicals (DPPH, hydroxyl and superoxide) in a dose-dependent manner and did not show any cytotoxic effect against MRC-5 and ECV304 cell lines.
450 citations
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TL;DR: Low molecular weight peptides obtained from ultrafiltration of giant squid muscle protein exhibited their antioxidant potential to act as chain-breaking antioxidants by inhibiting radical-mediated peroxidation of linoleic acid, and their activities were closer to highly active synthetic antioxidant, butylated hydroxytoluene.
Abstract: Low molecular weight peptides obtained from ultrafiltration (UF) of giant squid (Dosidicus gigas) muscle protein were studied for their antioxidative effects in different in vitro oxidative systems. The most potent two peptides, Asn-Ala-Asp-Phe-Gly-Leu-Asn-Gly-Leu-Glu-Gly-Leu-Ala (1307 Da) and Asn-Gly-Leu-Glu-Gly-Leu-Lys (747 Da), exhibited their antioxidant potential to act as chain-breaking antioxidants by inhibiting radical-mediated peroxidation of linoleic acid, and their activities were closer to highly active synthetic antioxidant, butylated hydroxytoluene. Addition of these peptides could enhance the viability of cytotoxic embryonic lung fibroblasts significantly (P<.05) at a low concentration of 50 microg/ml, and it was presumed due to the suppression of radical-induced oxidation of membrane lipids. Electron spin trapping studies revealed that the peptides were potent scavengers of free radicals in the order of carbon-centered (IC(50) 396.04 and 304.67 microM), hydroxyl (IC(50) 497.32 and 428.54 microM) and superoxide radicals (IC(50) 669.34 and 573.83 microM). Even though the exact molecular mechanism for scavenging of free radicals was unclear, unusually high hydrophobic amino acid composition (more than 75%) of giant squid muscle peptides was presumed to be involved in the observed activities.
438 citations
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TL;DR: APHPH decreased t-butylhydroperoxide-induced cytotoxicity on human embryonic lung fibroblasts and efficiently protected free-radical-induced DNA damage and inhibited lipid peroxidation higher than that of alpha-tocopherol as positive control.
Abstract: To extract antioxidant peptide from hoki frame protein hydrolysate (APHPH), we employed six proteases (pepsin, trypsin, papain, α-chymotrypsin, Alcalase and Neutrase) for enzymatic hydrolysis, and the antioxidant activities of their hydrolysates were investigated using both lipid peroxidation inhibition assay and free radical scavenging assay by electron spin resonance spin-trapping technique. Among hydrolysates, peptic hydrolysate, having the highest antioxidant activity, further separated into four groups using ultrafiltration membranes and purified consecutive chromatographic methods. Finally, the purified peptide had a molecular mass of 1801 Da, and amino acid sequence was identified as Glu-Ser-Thr-Val-Pro-Glu-Arg-Thr-His-Pro-Ala-Cys-Pro-Asp-Phe-Asn. APHPH inhibited lipid peroxidation higher than that of α-tocopherol as positive control and efficiently quenched different sources of free radical: 1,1-diphenyl-2-pycryl-hydrazyl (IC 50 =41.37 μM), hydroxyl (IC 50 =17.77 μM), peroxyl (IC 50 =18.99 μM) and superoxide radicals (IC 50 =172.10 μM). Furthermore, APHPH decreased t -butylhydroperoxide-induced cytotoxicity on human embryonic lung fibroblasts and efficiently protected free-radical-induced DNA damage.
425 citations
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TL;DR: This contribution focuses on biological activities of marine algae-derived NPs and emphasizing their potential applications in foods as well as pharmaceuticals areas.
413 citations
Authors
Showing all 6752 results
Name | H-index | Papers | Citations |
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Se-Kwon Kim | 102 | 763 | 39344 |
Rangasamy Jayakumar | 74 | 289 | 21042 |
Hae Young Chung | 72 | 529 | 21126 |
You-Jin Jeon | 70 | 573 | 20967 |
Chin-Pao Huang | 69 | 307 | 17355 |
Wan Mohd Ashri Wan Daud | 68 | 290 | 18767 |
Ho Won Jang | 64 | 493 | 15645 |
Sang Yeol Lee | 61 | 258 | 12344 |
Shuang Wang | 60 | 983 | 17802 |
Alan J. Lough | 60 | 666 | 14689 |
Jae Sue Choi | 59 | 443 | 13677 |
Sher Bahadar Khan | 59 | 405 | 10507 |
Ho Nam Chang | 56 | 308 | 11890 |
Dae Sung Lee | 56 | 403 | 10361 |
Yoon-Bo Shim | 55 | 298 | 10080 |