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Cho, Byoung Ok,Ryu, Hyung Won,Jin, Chang Hyun,Choi, Dae Seong,Kang, Si Yong,Kim, Dong Sub,Byun, Myung-Woo,Jeong, Il Yun American Chemical Society 2011 Journal of agricultural and food chemistry Vol.59 No.21
<P>The aim of this study was to investigate the protective ability of blackberry extract (BE) against oxidative stress in carbon tetrachloride (CCl<SUB>4</SUB>)-treated rats. The results showed that treatment with BE attenuated lipid peroxidation that was increased by CCl<SUB>4</SUB> and also markedly recovered the activity of antioxidant enzymes, such as superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and glutathione reductase (GR), that were decreased by CCl<SUB>4</SUB>. BE also elevated the protein expression levels of NF-E2-related factor-2 (Nrf2), CuZnSOD, MnSOD, GPx-1/2, and heme oxygenase-1 (HO-1), but not that of catalase. Furthermore, the administration of BE significantly attenuated the levels of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) that were increased by CCl<SUB>4</SUB>. Therefore, the present study suggests that BE possesses significant protective effects against in vivo oxidative stress.</P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/jf2021804'>ACS Electronic Supporting Info</A></P>
<i>Fryl</i> deficiency is associated with defective kidney development and function in mice
Byun, Yong-Sub,Kim, Eun-Kyoung,Araki, Kimi,Yamamura, Ken-ichi,Lee, Kihoon,Yoon, Won-Kee,Won, Young-Suk,Kim, Hyoung-Chin,Choi, Kyung-Chul,Nam, Ki-Hoan SAGE Publications 2018 Experimental biology and medicine Vol.243 No.5
<P> FRY like transcription coactivator ( Fryl) gene located on chromosome 5 is a paralog of FRY microtubule binding protein ( Fry) in vertebrates. It encodes a protein with unknown functions. Fryl gene is conserved in various species ranging from eukaryotes to human. Although there are several reports on functions of Fry gene, functions of Fryl gene remain unclear. A mouse line containing null mutation in Fryl gene by gene trapping was produced in this study for the first time. The survival and growth of Fryl<SUP>−/−</SUP> mice were observed. Fryl gene expression levels in mouse tissues were determined and histopathologic analyses were conducted. Most Fryl<SUP>−/−</SUP> mice died soon after birth. Rare Fryl<SUP>−/−</SUP> survivors showed growth retardation with significantly lower body weight compared to their littermate controls. Although they could breed, more than half of Fryl<SUP>−/−</SUP> survivors died of hydronephrosis before age 1. No abnormal histopathologic lesion was apparent in full-term embryo or adult tissues except the kidney. Abnormal lining cell layer detachments from walls of collecting and convoluted tubules in kidneys were apparent in Fryl<SUP>−/−</SUP> neonates and full-term embryos. Fryl gene was expressed in renal tubular tissues including the glomeruli and convoluted and collecting tubules. This indicates that defects in tubular systems are associated with Fryl functions and death of Fryl<SUP>−/−</SUP> neonates. Fryl protein is required for normal development and functional maintenance of kidney in mice. This is the first report of in vivo Fryl gene functions. </P><B>Impact statement</B><P> FRY like transcription coactivator ( Fryl) gene is conserved in various species ranging from eukaryotes to human. It expresses a protein with unknown function. We generated a Fryl gene mutant mouse line and found that most homozygous mice died soon after their birth. Rare Fryl<SUP>−/−</SUP> survivors showed growth retardation with significantly lower body weight compared to their littermate controls. Although they could breed, more than half of Fryl<SUP>−/−</SUP> survivors died of hydronephrosis before age 1. Full-term mutant embryos showed abnormal collecting and convoluted tubules in kidneys where Fryl gene was expressed. Collectively, these results indicate that Fryl protein is required for normal development and functional maintenance of kidney in mice. To the best of our knowledge, this is the first report on in vivo Fryl gene functions. </P>
The deficiency of Fryl gene induces neonatal lethality
Yong Sub Byun,Eun Kyoung Kim,Hae Rim Kim,Ju Sung Kang,Yu Rim Kim,Ju Young Lee,Min Young Lee,Sang Mi Cho,Ho Young Ghang,Ki Hoon Lee,Won Kee Yoon,Young Suk Won,Hyoung Chin Kim,Kyung Chul Choi,Ki Hoan Na 한국실험동물학회 2015 한국실험동물학회 학술발표대회 논문집 Vol.2015 No.8
Pyun, Sang-Yong,Byun, Woong-Sub,Cho, Bong-Rae Korean Chemical Society 2011 Bulletin of the Korean Chemical Society Vol.32 No.6
Nitrile-forming eliminations from $(E)-2,4,6-(NO_2)_3C_6H_2CH=NOC_6H_4-2-X-4-NO_2$ (1) promoted by $R_3NH/R_3NH^+$ in 70 mol % MeCN(aq) have been studied kinetically. When X = $NO_2$, the reactions exhibited second-order kinetics as well as Br$\"{o}$nsted ${\beta}$ = 0.63 and ${\mid}{\beta}_{lg}{\mid}$ = 0.34-0.46, and an E2 mechanism is evident. As the leaving group was made poorer (X = H, Cl, and $CF_3$), Br$\"{o}$nsted ${\beta}$ value increased from 0.63 to 0.85-0.89 without much change in the ${\mid}{\beta}_{lg}{\mid}$ value E2, indicating that structure of the transition state changed to an E1cb-like with extensive $C_{\beta}-H$ bond cleavage, significant negative charge development at the ${\beta}$-carbon, and limited $C_{\alpha}$-OAr bond cleavage.