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    <link>https://repository.kopri.re.kr/handle/201206/9813</link>
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    <pubDate>Mon, 06 Apr 2026 08:06:36 GMT</pubDate>
    <dc:date>2026-04-06T08:06:36Z</dc:date>
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      <title>Antiinflammatory lanostane triterpenoids from Ganoderma lucidum</title>
      <link>https://repository.kopri.re.kr/handle/201206/13607</link>
      <description>Title: Antiinflammatory lanostane triterpenoids from Ganoderma lucidum
Authors: Koo, Man Hyung; Chae, Hae-Jung; Lee, Jun Hyuck; Suh, Sung-Suk; Youn, Ui Joung
Abstract: Phytochemical and biological studies of the methanolic extracts from Ganoderma lucidum (Polyporaceae) have led to the identification and isolation of a new lanostane triterpenoid, ganosidone A (1), and its eight known derivatives (2-9). The structure of new compound was determined by HREIMS, 1 D and 2 D NMR experiments and by comparing the acquired physicochemical data with the published values. All the compounds were evaluated for cancer chemopreventive potential based on their ability to inhibit nitric oxide (NO) production induced by lipopolysaccharides (LPS) in mouse macrophage RAW 264.7 cells in vitro. Notably, at a concentration of 50 mu M, compounds 4 and 7 inhibited NO production by 86.5% and 88.2%, respectively.</description>
      <pubDate>Thu, 18 Nov 2021 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">https://repository.kopri.re.kr/handle/201206/13607</guid>
      <dc:date>2021-11-18T00:00:00Z</dc:date>
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    <item>
      <title>Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase</title>
      <link>https://repository.kopri.re.kr/handle/201206/12085</link>
      <description>Title: Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase
Authors: Hwang, Jisub; Jeong, Chang Sook; Lee, Chang Woo; Shin, Seung Chul; Kim, Han-Woo; Lee, Sung Gu; Youn, Ui Joung; Lee, Chang Sup; Oh, Tae-Jin; Kim, Hak Jun; Park, Hyun; Park, Hyun Ho; Lee, Jun Hyuck
Abstract: Crystal structures of enoyl-coenzyme A (CoA) isomerase from Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase from Hymenobacter sp. PAMC 26628 (HyECH) were determined at 2.35 and 2.70 A resolution, respectively. BoECI and HyECH are members of the crotonase superfamily and are enzymes known to be involved in fatty acid degradation. Structurally, these enzymes are highly similar except for the orientation of their C-terminal helix domain. Analytical ultracentrifugation was performed to determine the oligomerization states of BoECI and HyECH revealing they exist as trimers in solution. However, their putative ligand-binding sites and active site residue compositions are dissimilar. Comparative sequence and structural analysis revealed that the active site of BoECI had one glutamate residue (Glu135), this site is occupied by an aspartate in some ECIs, and the active sites of HyECH had two highly conserved glutamate residues (Glu118 and Glu138). Moreover, HyECH possesses a salt bridge interaction between Glu98 and Arg152 near the active site. This interaction may allow the catalytic Glu118 residue to have a specific conformation for the ECH enzyme reaction. This salt bridge interaction is highly conserved in known bacterial ECH structures and ECI enzymes do not have this type of interaction. Collectively, our comparative sequential and structural studies have provided useful information to distinguish and classify two similar bacterial crotonase superfamily enzymes.</description>
      <pubDate>Wed, 01 Jul 2020 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">https://repository.kopri.re.kr/handle/201206/12085</guid>
      <dc:date>2020-07-01T00:00:00Z</dc:date>
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    <item>
      <title>Enzymatic synthesis of anabolic steroids glycosides by glucosyltransferase from Terribacillus sp. PAMC 23288</title>
      <link>https://repository.kopri.re.kr/handle/201206/12092</link>
      <description>Title: Enzymatic synthesis of anabolic steroids glycosides by glucosyltransferase from Terribacillus sp. PAMC 23288
Authors: Yu, Eun-Ji; Yamaguchi, Tokutaro; Lee, Joo-Ho; Lim, A-Rang; Lee, Jun Hyuck; Park, Hyun; Oh, Tae-Jin
Abstract: To date, the use of steroid drugs has been steadily thanks to its effects, but due to severe side effects, studies on the derivative activity of steroids are being conducted. Nandrolone, a breast cancer drug, cortisone and prednisone which reduce inflammation, pain, and edema used in this study are not known as sugar derivatives. O-glucose was successfully linked using UDP-glucosyltransferase (UGT-1), and bioactivity was tested in vitro. NMR analysis found that those products produced by the nandrolone and testosterone were 17β-nandrolone β-D-glucose and 17β-testosterone β-D-glucose, respectively. In addition, testosterone derivatives in rotenone-treated PC12 cells showed higher cell viability and no cytotoxicity compared to control. In the presence of H2O2 in SH-SY5Y cells, nandrolone derivatives showed cell viability and attenuated cytotoxicity. Both derivatives also increased the renal protective effect and cellular ATP.</description>
      <pubDate>Wed, 01 Apr 2020 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">https://repository.kopri.re.kr/handle/201206/12092</guid>
      <dc:date>2020-04-01T00:00:00Z</dc:date>
    </item>
    <item>
      <title>A New Chlorinated Phenolic Compound From the Antarctic Lichen, Pertusaria dactylina</title>
      <link>https://repository.kopri.re.kr/handle/201206/12091</link>
      <description>Title: A New Chlorinated Phenolic Compound From the Antarctic Lichen, Pertusaria dactylina
Authors: Koo, Man Hyung; Kim, Min Ju; So, Jae Eun; Kim, Ji Hee; Han, Se Jong; Kim, Il-Chan; Lee, Jun Hyuck; Youn, Ui Joung
Abstract: A new chlorinated phenolic compound, methyl-3-chloro-2-hydroxy-4-methoxy-6-pentylbenzoate (1) and four known compounds (2-5) were isolated from the Antarctic lichen, Pertusaria dactylina (Pertusariaceae). The structure of the new compound was determined by means of 1D and 2D NMR and HRFABMS experiments. The antimicrobial activities of compounds 15 against Staphylococcus aureus and Candida albicans were evaluated. The results showed that compound 1 exhibited a weak inhibitory effect against C. albicans with an IC50 value of 67 ± 7 μg/mL.</description>
      <pubDate>Sun, 01 Mar 2020 00:00:00 GMT</pubDate>
      <guid isPermaLink="false">https://repository.kopri.re.kr/handle/201206/12091</guid>
      <dc:date>2020-03-01T00:00:00Z</dc:date>
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