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Sung, Dae Dong,Koo, In Sun,Yang, Kiyull,Lee, Ikchoon Elsevier 2006 Chemical physics letters Vol.426 No.4
<P><B>Graphical abstract</B></P><P>DFT Studies are carried out on the structure and stability of Zwitterionic intermediates in the aminolysis of phenyl acetate with ammonia in water. At least five explicit water molecules are needed for the Zwitterion.</P><ce:figure id='figure.0010'></ce:figure> <P><B>Abstract</B></P><P>The structure and stability of putative zwitterionic complexes in the aminolysis of phenyl acetate with ammonia are examined using density functional and ab initio methods by applying the explicit, up to 7 H<SUB>2</SUB>O, and implicit, PCM, solvation models. The stability of the zwitterionic tetrahedral intermediate required an explicit solvation by at least five water molecules with stabilization energy of approximately 35kcalmol<SUP>−1</SUP>. The explicit water molecules are inter-connected by cyclic hydrogen bonding networks terminating at the negatively charged carbonyl oxygen and one of the hydrogen atoms on the positively charged ammonium ion.</P>
Design and fabrication of the low conversion loss Self Oscillating Mixer for Q-band
Sang-Jin Lee,Dan An,Mun-Kyo Lee,Jin-Man Jin,Du-Hyun Ko,Chang-Sik Cho,Seong-Dae Lee,Tae-Jong Baek,Seong-Chan Kim,Hyung-Moo Park,Jin-Koo Rhee 대한전자공학회 2005 ITC-CSCC :International Technical Conference on Ci Vol.2005 No.1
Inhibitory effects of polyphenols isolated from Rhus verniciflua on Aldo-keto reductase family 1 B10
( Dae Geun Song ),( Joo Young Lee ),( Eun Ha Lee ),( Sang Hoon Jung ),( Chu Won Nho ),( Kwang Hyun Cha ),( Song Yi Koo ),( Cheol Ho Pan ) 한국생화학분자생물학회 (구 한국생화학회) 2010 BMB Reports Vol.43 No.4
Aldo-keto reductase family 1 B10 (AKR1B10) is a member of the NADPH-dependent aldo-keto reductase (AKR) superfamily, and has been considered to be a potential cancer therapeutic target. Total extract from the bark of Rhus verniciflua (Toxico-dendron vernicifluum (Stokes)) showed AKR1B10 inhibitory activity. To identify the active compounds from R. verniciflua responsible for AKR1B10 inhibition, nine compounds were isolated via bioactivity-guided isolation and tested for their effects against recombinant human AKR1B10 (rhAKR1B10). Results showed that butein, isolated from the ethyl acetate fraction, was most able to inhibit rhAKR1B10. The inhibitory rate of butein against rhAKR1B10 was 42.86% at 1 μM with an IC50 value of 1.47 μM, and enzyme kinetic analysis revealed its inhibition mode to be uncompetitive. [BMB reports 2010; 43(4): 268-272]
Pn-AMP1, a Plant Defense Protein, Induces Actin Depolarization in Yeasts
Koo, Ja Choon,Lee, Boyoung,Young, Michael E.,Koo, Sung Chul,Cooper, John A.,Baek, Dongwon,Lim, Chae Oh,Lee, Sang Yeol,Yun, Dae-Jin,Cho, Moo Je Oxford University Press 2004 Plant & cell physiology Vol.45 No.11
<P>Pn-AMP1, <I>Pharbitis nil</I> antimicrobial peptide 1, is a small cysteine-rich peptide implicated in host-plant defense. We show here that Pn-AMP1 causes depolarization of the actin cytoskeleton in <I>Saccharomyces cerevisiae</I> and <I>Candida albicans</I>. Pn-AMP1 induces rapid depolarization of actin cables and patches within 15 min. Increased osmolarity or temperature induces transient actin depolarization and results in increased sensitivity to Pn-AMP1, while cells conditioned to these stresses show less sensitivity. Mutations in components of a cell wall integrity pathway (Wsc1p, Rom2p, Bck1p and Mpk1p), which regulate actin repolarization, result in increased sensitivity to Pn-AMP1. A genetic screen reveals that mutations in components of the α-1,6-mannosyltransferase complex (Mnn10p, Mnn11p and Och1p), which regulate mannosylation of cell wall proteins, confer resistance to Pn-AMP1. FITC-conjugated Pn-AMP1 localizes to the outer surface of the cell with no significant staining observed in spheroplasts. Taken together, these results indicate that cell wall proteins are determinants of resistance to Pn-AMP1, and the ability of a plant defense protein to induce actin depolarization is important for its antifungal activity.</P>