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Jinwook Seo,Hak Sung Lee,이민전,Mira Kim,신차균 대한약학회 2004 Archives of Pharmacal Research Vol.27 No.1
DA-125, a novel derivative of adriamycin, is known for its anti-cancer activity. In this study, the inhibitory mechanism of DA-125 on topoisomerase was investigated in the simian virus 40 (SV40) replicating CV-1 cell by studying the SV40 DNA replication intermediates and DNAtopoisomerase complexes. DNA-protein complexes that were formed in the drug-treated cells were quantitated by using a glass filter assay. SV40 DNA replication intermediates that were accumulated in the drug-treated CV-1 cell were analyzed in a high resolution gel. DA-125 did not accumulate B-dimers of SV40 DNA replication intermediates which were found in the adriamycin- treated CV-1 cells. DA-125 induced a dose-dependent formation of the DNA-protein complexes, while adriamycin did not. When adriamycin and etoposide (VP16) were added to the SV40-infected cells at the same time, adriamycin blocked the formation of the DNA-protein complexes induced by VP16 in a dose-dependent manner. However, DA-125 blocked the formation of the DNA-protein complexes induced by VP16 up to the maximum level of the DNA-protein complexes that were induced by DA-125 alone. Adriamycin and DA-125 did not inhibit the formation of the DNA-protein complexes that were caused by camptothecin, a known topoisomerase I poison. DA-125 is bifunctional in inhibiting topoisomerase II because it simultaneously has the properties of the topoisomerase II poison and the DNA intercalator. As a topoisomerase II poison, DA-125 alone induced dose-dependent formation of the DNA-protein complexes. However, as a DNA intercalator, it quantitatively inhibited the formation of the DNA-protein complexes induced by a strong topoisomerase II poison VP16. Furthermore considering that the levels of the DNA-protein complex induced by VP16 were decreased by DA- 125 in terms of the topoisomerase II poison, we suggest that DA-125 has a higher affinity to the drug-binding sites of DNA than VP16 has.
MAP4-regulated dynein-dependent trafficking of BTN3A1 controls the TBK1–IRF3 signaling axis
Seo, Minji,Lee, Seong-Ok,Kim, Ji-Hoon,Hong, Yujin,Kim, Seongchan,Kim, Yeumin,Min, Dal-Hee,Kong, Young-Yun,Shin, Jinwook,Ahn, Kwangseog National Academy of Sciences 2016 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.113 No.50
<P>The innate immune system detects viral nucleic acids and induces type I interferon (IFN) responses. The RNA-and DNA-sensing pathways converge on the protein kinase TANK-binding kinase 1 (TBK1) and the transcription factor IFN-regulatory factor 3 (IRF3). Activation of the IFN signaling pathway is known to trigger the redistribution of key signaling molecules to punctate perinuclear structures, but the mediators of this spatiotemporal regulation have yet to be defined. Here we identify butyrophilin 3A1 (BTN3A1) as a positive regulator of nucleic acid-mediated type I IFN signaling. Depletion of BTN3A1 inhibits the cytoplasmic nucleic acid-or virus-triggered activation of IFN-beta production. In the resting state, BTN3A1 is constitutively associated with TBK1. Stimulation with nucleic acids induces the redistribution of the BTN3A1-TBK1 complex to the perinuclear region, where BTN3A1 mediates the interaction between TBK1 and IRF3, leading to the phosphorylation of IRF3. Furthermore, we show that microtubule-associated protein 4 (MAP4) controls the dynein-dependent transport of BTN3A1 in response to nucleic acid stimulation, thereby identifying MAP4 as an upstream regulator of BTN3A1. Thus, the depletion of either MAP4 or BTN3A1 impairs cytosolic DNA- or RNA-mediated type I IFN responses. Our findings demonstrate a critical role for MAP4 and BTN3A1 in the spatiotemporal regulation of TBK1, a central player in the intracellular nucleic acid-sensing pathways involved in antiviral signaling.</P>
Chemical ordering in PtNi nanocrystals
Seo, Okkyun,Lee, Ji Yeon,Kim, Jae Myung,Kim, Jin-Woo,Kang, Hyon Chol,Chung, Jinwook,Noh, Do Young Elsevier 2016 JOURNAL OF ALLOYS AND COMPOUNDS Vol.666 No.-
<P><B>Abstract</B></P> <P>We investigated the chemical ordering in PtNi nanocrystals fabricated on sapphire substrate using <I>in-situ</I> synchrotron X-ray scattering. Nanocrystals with composition close to 1:1 were ordered in the tetragonal L1<SUB>0</SUB> structure at low temperatures. The transition to disordered FCC structure occurred at around 640 °C and substantial hysteresis of about 50 K was observed. Nanocrystals of smaller sizes fabricated under the same conditions were Ni rich and ordered into Cu<SUB>3</SUB>Au type L1<SUB>2</SUB> structure. Significantly higher degree of chemical ordering was observed in L1<SUB>2</SUB> structure than in L1<SUB>0</SUB> structure.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Chemical ordering in aligned PtNi alloy nanoparticles on sapphire was studied. </LI> <LI> L10 structure and order–disorder transition with large hysteresis were observed. </LI> <LI> Nanoparticles smaller than 100 nm became Ni rich and ordered in L12 structure. </LI> </UL> </P>