http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Kim, S.G.,Jo, Y.H.,Seong, J.H.,Park, K.B.,Noh, M.Y.,Cho, J.H.,Ko, H.J.,Kim, C.E.,Tindwa, H.,Patnaik, B.B.,Bang, I.S.,Lee, Y.S.,Han, Y.S. Pergamon Press ; Elsevier Science Ltd 2017 Insect biochemistry and molecular biology Vol.89 No.-
Scavenger receptors (SRs) constitute a family of membrane-bound receptors that bind to multiple ligands. The SR family of proteins is involved in removing cellular debris, oxidized low-density lipoproteins, and pathogens. Specifically, class C scavenger receptors (SR-C) have also been reported to be involved in phagocytosis of gram-positive and -negative bacteria in Drosophila and viruses in shrimp. However, reports are unavailable regarding the role of SR-C in antifungal immune mechanisms in insects. In this study, a full-length Tenebrio molitor SR-C (TmSR-C) sequence was obtained by 5'- and 3'-Rapid amplification of cDNA ends-polymerase chain reaction (RACE-PCR). The TmSR-C full-length cDNA comprised 1671 bp with 5'- and 3'-untranslated regions of 23- and 107-bp, respectively. TmSR-C encodes a putative protein of 556 amino acid residues that is constitutively expressed in all tissues of late instar larvae and 2-day-old adults, with the highest transcript levels observed in hemocytes of larvae and adults. TmSR-C mRNA showed a 2.5-fold and 3-fold increase at 24 and 6 h after infection with Candida albicans and β-glucan, respectively. Immunoassay with TmSR-C polyclonal antibody showed induction of the putative protein in the cytosols of hemocytes at 3 h after inoculation of C. albicans. RNA interference (RNAi)-based gene silencing and phagocytosis assays were used to understand the role of TmSR-C in antifungal immunity. Silencing of TmSR-C transcripts reduced the survivability of late instar larvae at 2 days post-inoculation of C. albicans, Escherichia coli, or Staphylococcus aureus. Furthermore, in TmSR-C-silenced larvae, there was a decline in the rate of microorganism phagocytosis. Taken together, results of this study suggest that TmSR-C plays a pivotal role in phagocytosing not only fungi but also gram-negative and -positive bacteria in T. molitor.
Shewanella fodinae sp. nov., isolated from a coal mine and from a marine lagoon
Sravan Kumar, R.,Sasi Jyothsna, T. S.,Sasikala, Ch.,Seong, C. N.,Lim, C. H.,Park, S. C.,Ramana, Ch. V. Microbiology Society 2010 International journal of systematic and evolutiona Vol.60 No.7
<P>Strains JC15<SUP>T</SUP> and JC19 were isolated from samples collected from different locations in India, including a coal mine and a marine lagoon. Both strains were Gram-stain-negative rods, motile by means of a single polar flagellum, catalase- and oxidase-positive, and hydrolysed casein, produced H2S and showed <I>β</I>-haemolysis. Strain JC15<SUP>T</SUP> grew optimally at pH 6 (range pH 5-8) while strain JC19 grew optimally at pH 7 (range pH 6-9) and both had a growth temperature optimum of 30-37 °C (range 22-40 °C). Both strains could grow chemo-organoheterotrophically and chemolithoautotrophically. Neither strain required NaCl for growth and both could tolerate up to 9 % (w/v) NaCl, with optimum growth at 5 % NaCl. Vitamin B12 was required as a growth factor by both strains. The major fatty acids were iso-C15 : 0, C17 : 1<I>ω</I>8<I>c</I> and iso-C13 : 0 3-OH. The DNA G<I>+</I>C contents of strains JC15<SUP>T</SUP> and JC19 were 53.6 and 54.3 mol%, respectively. A phylogenetic tree based on 16S rRNA gene sequence analysis showed that strains JC15<SUP>T</SUP> and JC19 were most closely related to <I>Shewanella haliotis</I> DW01<SUP>T</SUP> (approximately 94 % sequence similarity) and to other members of the genus <I>Shewanella.</I> Genomic relatedness (DNA-DNA hybridization) between strains JC15<SUP>T</SUP> and JC19 is 88 %. On the basis of phenotypic and molecular genetic evidence, strain JC15<SUP>T</SUP> represents a novel species of the genus <I>Shewanella</I>, for which the name <I>Shewanella fodinae</I> sp. nov. is proposed. The type strain is JC15<SUP>T</SUP> (=CCUG 57102<SUP>T</SUP> =NBRC 105216<SUP>T</SUP> =KCTC 22506<SUP>T</SUP>).</P>
Lee, H J,Lee, Y N,Youn, H-N,Lee, D H,Kwak, J H,Seong, B L,Lee, J B,Park, S Y,Choi, I S,Song, C S Poultry Science Association, etc 2012 Poultry science Vol.91 No.1
<P>Polyphenolic compounds present in green tea, particularly catechins, are known to have strong anti-influenza activity. The goal of this study was to determine whether green tea by-products could function as an alternative to common antivirals in animals compared to original green tea. Inhibition of viral cytopathic effects ascertained by neutral red dye uptake was examined with 50% effective (virus-inhibitory) concentrations (EC??)determined. Against the H1N1 virus A/NWS/33, we found the anti-influenza activity of green tea by-products (EC?? = 6.36 ?g/mL) to be equivalent to that of original green tea (EC??= 6.72 ?g/mL). The anti-influenza activity of green tea by-products was further examined in mouse and chicken influenza infection models. In mice, oral administration of green tea by-products reduced viral titers in the lungs in the early phase of infection, but they could not protect these animals from disease and death. In contrast, therapeutic administration of green tea by-products via feed or water supplement resulted in a dose-dependent significant antiviral effect in chickens, with a dose of 10 g/kg of feed being the most effective (P < 0.001). We also demonstrated that unidentified hexane-soluble fractions of green tea by-products possessed strong anti-influenza activity, in addition to ethyl acetate-soluble fractions, including catechins. This study revealed green tea by-product extracts to be a promising novel antiviral resource for animals.</P>
Yeo, C.E.,Kang, W.Y.,Seong, S.J.,Cho, S.,Lee, H.W.,Yoon, Y.R.,Kim, H.J. Academic Press 2017 Experimental cell research Vol.359 No.1
Neuromedin B (NMB), a mammalian bombesin-like peptide, regulates diverse physiological processes, such as energy metabolism, memory and fear behavior, and cellular growth, through its cognate receptor, NMBR. In this study, we report that NMB expression was upregulated during osteoclast development and that silencing NMB or NMBR attenuated osteoclast generation mediated by macrophage colony-stimulating factor (M-CSF) and receptor activator of NF-κB ligand (RANKL). We found that knockdown of NMB or NMBR using a small hairpin RNA suppressed M-CSF-induced proliferation of osteoclast precursor cells without altering osteoclast differentiation. Interestingly, NMB or NMBR knockdown reduced the expression of the M-CSF receptor, c-Fms, which is an important modulator of osteoclast development. Consequently, NMB or NMBR silencing inhibited M-CSF/c-Fms-mediated downstream signaling pathways like activation of ERK and Akt and induction of D-type cyclins, cyclin D1 and D2. Moreover, knockdown of NMB or NMBR accelerated apoptosis in osteoclast lineage cells by inducing caspase-3, caspase-9, and Bim expression. In summary, our study demonstrates that the NMB/NMBR axis plays a pivotal role in osteoclast generation by modulating the proliferation and survival of osteoclast lineage cells.
Kim, C. W.,Han, K. S.,Ryu, K.-S.,Kim, B. H.,Kim, K.-H.,Choi, S. I.,Seong, B. L. Wiley-Blackwell Publishing, Inc. 2007 Protein science Vol. No.
<P>The fusion of soluble partner to the N terminus of aggregation-prone polypeptide has been popularly used to overcome the formation of inclusion bodies in the E. coli cytosol. The chaperone-like functions of the upstream fusion partner in the artificial multidomain proteins could occur in de novo folding of native multidomain proteins. Here, we show that the N-terminal domains of three E. coli multidomain proteins such as lysyl-tRNA synthetase, threonyl-tRNA synthetase, and aconitase are potent solubility enhancers for various C-terminal heterologous proteins. The results suggest that the N-terminal domains could act as solubility enhancers for the folding of their authentic C-terminal domains in vivo. Tandem repeat of N-terminal domain or insertion of aspartic residues at the C terminus of the N-terminal domain also increased the solubility of fusion proteins, suggesting that the solubilizing ability correlates with the size and charge of N-terminal domains. The solubilizing ability of N-terminal domains would contribute to the autonomous folding of multidomain proteins in vivo, and based on these results, we propose a model of how N-terminal domains solubilize their downstream domains.</P>
Tuning microcavities in thermally rearranged polymer membranes for CO<sub>2</sub> capture
Han, S. H.,Kwon, H. J.,Kim, K. Y.,Seong, J. G.,Park, C. H.,Kim, S.,Doherty, C. M.,Thornton, A. W.,Hill, A. J.,Lozano, Á,. E.,Berchtold, K. A.,Lee, Y. M. The Royal Society of Chemistry 2012 Physical Chemistry Chemical Physics Vol.14 No.13
<P>Microporous materials have a great importance in catalysis, delivery, storage and separation in terms of their performance and efficiency. Most microporous materials are comprised of inorganic frameworks, while thermally rearranged (TR) polymers are a microporous organic polymer which is tuned to optimize the cavity sizes and distribution for difficult separation applications. The sub-nano sized microcavities are controlled by <I>in situ</I> thermal treatment conditions which have been investigated by positron annihilation lifetime spectroscopy (PALS). The size and relative number of cavities increased from room temperature to 230 °C resulting in improvements in both permeabilities and selectivities for H<SUB>2</SUB>/CO<SUB>2</SUB> separation due to the significant increase of gas diffusion and decrease of CO<SUB>2</SUB> solubility. The highest performance of the well-tuned TR-polymer membrane was 206 Barrer for H<SUB>2</SUB> permeability and 6.2 of H<SUB>2</SUB>/CO<SUB>2</SUB> selectivity, exceeding the polymeric upper bound for gas separation membranes.</P> <P>Graphic Abstract</P><P>Thermally rearranged polybenzoxazoles with tuned cavities for hydrogen purification and carbon dioxide separation even at high temperature were developed to apply for a syn gas separation. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2cp23729f'> </P>