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426 results on '"Wang, En‐Duo"'

101. Cryptosporidium and Toxoplasma Parasites Are Inhibited by a Benzoxaborole Targeting Leucyl-tRNA Synthetase

Author

Palencia, Andrés, primary, Liu, Ru-Juan, additional, Lukarska, Maria, additional, Gut, Jiri, additional, Bougdour, Alexandre, additional, Touquet, Bastien, additional, Wang, En-Duo, additional, Li, Xianfeng, additional, Alley, M. R. K., additional, Freund, Yvonne R., additional, Rosenthal, Philip J., additional, Hakimi, Mohamed-Ali, additional, and Cusack, Stephen, additional

Published
2016
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102. Instability of the mitochondrial alanyl-tRNA synthetase underlies fatal infantile-onset cardiomyopathy.

Author

Sommerville, Ewen W, Zhou, Xiao-Long, Oláhová, Monika, Jenkins, Janda, Euro, Liliya, Konovalova, Svetlana, Hilander, Taru, Pyle, Angela, He, Langping, Habeebu, Sultan, Saunders, Carol, Kelsey, Anna, Morris, Andrew A M, McFarland, Robert, Suomalainen, Anu, Gorman, Gráinne S, Wang, En-Duo, Thiffault, Isabelle, Tyynismaa, Henna, and Taylor, Robert W

Published
2019
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106. Pachytene piRNAs instruct massive mRNA elimination during late spermiogenesis

Author

Gou, Lan-Tao, primary, Dai, Peng, additional, Yang, Jian-Hua, additional, Xue, Yuanchao, additional, Hu, Yun-Ping, additional, Zhou, Yu, additional, Kang, Jun-Yan, additional, Wang, Xin, additional, Li, Hairi, additional, Hua, Min-Min, additional, Zhao, Shuang, additional, Hu, Si-Da, additional, Wu, Li-Gang, additional, Shi, Hui-Juan, additional, Li, Yong, additional, Fu, Xiang-Dong, additional, Qu, Liang-Hu, additional, Wang, En-Duo, additional, and Liu, Mo-Fang, additional

Published
2015
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111. Studying base pair open-close kinetics of tRNALeu by TROSY-based proton exchange NMR spectroscopy

Author

Hao, Zhan Xi, Tan, Min, Liu, Changdong, Feng, Rui, Wang, En Duo, Zhu, Guang, Hao, Zhan Xi, Tan, Min, Liu, Changdong, Feng, Rui, Wang, En Duo, and Zhu, Guang

Abstract

The millisecond conformational flexibility is functionally important for nucleic acids and can be studied through probing the base pair open-close kinetics by proton exchange nuclear magnetic resonance (NMR) spectroscopy. Here, the traditional imino proton exchange NMR experiments were modified with transverse relaxation optimized spectroscopy and were applied to accurately measure imino proton exchange rates of all base pairs in Escherichia coli tRNALeu (CAG), and their dependence on magnesium ion concentration. Finally, we correlated millisecond conformational flexibility with aminoacylation of tRNALeu and proposed that the flexibility of the acceptor stem and the core region might contribute to aminoacylation of tRNALeu. © 2010 Federation of European Biochemical Societies.

Published
2010

121. Escherichia coli tRNA4Arg(UCU) induces a constrained conformation of the crucial Ω-loop of arginyl-tRNA synthetase

Author

Yao, Yong-Neng, Zhang, Qing-Shuo, Yan, Xian-Zhong, Zhu, Guang, Wang, En-Duo, Yao, Yong-Neng, Zhang, Qing-Shuo, Yan, Xian-Zhong, Zhu, Guang, and Wang, En-Duo

Abstract

Previous investigations show that tRNA(Arg)-induced conformational changes of arginyl-tRNA synthetase (ArgRS) Omega-loop region (Escherichia coli (E coli), Ala451-Ala457) may contribute to the productive conformation of the enzyme catalytic core, and E. coli tRNA(2)(Arg)(ICG)-bound and -free conformations of the Omega-loop exchange at an intermediate rate on NMR timescale. Herein, we report that E. coli ArgRS catalyzes tRNA(2)(Arg)(ICG) and tRNA(4)(Arg)(UCU) with similar efficiencies. However, F-19 NMR spectroscopy of 4-fluorotryptophan-labeled E. coli ArgRS reveals that the tRNA(4)(Arg)(UCU)-bound and -free conformations of the Omega-loop region interconvert very slowly and the lifetime of bound conformation is much longer than 0.33ms. Therefore, tRNA(4)(Arg) (UCU) differs from tRNA(2)(Arg)(ICG) in the conformation-exchanging rate of the Omega-loop. Comparative structure model of E. coli ArgRS is presented to rationalize these F-19 NMR data. Our F-19 NMR and catalytic assay results suggest that the tRNA(Arg)-induced conformational changes of Omega-loop little contribute to the productive conformation of ArgRS catalytic core. (C) 2003 Elsevier Inc. All rights reserved.

Published
2004

146. Cryptosporidiumand ToxoplasmaParasites Are Inhibited by a Benzoxaborole Targeting Leucyl-tRNA Synthetase

Author

Palencia, Andrés, Liu, Ru-Juan, Lukarska, Maria, Gut, Jiri, Bougdour, Alexandre, Touquet, Bastien, Wang, En-Duo, Li, Xianfeng, Alley, M. R. K., Freund, Yvonne R., Rosenthal, Philip J., Hakimi, Mohamed-Ali, and Cusack, Stephen

Abstract

ABSTRACTThe apicomplexan parasites Cryptosporidiumand Toxoplasmaare serious threats to human health. Cryptosporidiosis is a severe diarrheal disease in malnourished children and immunocompromised individuals, with the only FDA-approved drug treatment currently being nitazoxanide. The existing therapies for toxoplasmosis, an important pathology in immunocompromised individuals and pregnant women, also have serious limitations. With the aim of developing alternative therapeutic options to address these health problems, we tested a number of benzoxaboroles, boron-containing compounds shown to be active against various infectious agents, for inhibition of the growth of Cryptosporidiumparasites in mammalian cells. A 3-aminomethyl benzoxaborole, AN6426, with activity in the micromolar range and with activity comparable to that of nitazoxanide, was identified and further characterized using biophysical measurements of affinity and crystal structures of complexes with the editing domain of Cryptosporidiumleucyl-tRNA synthetase (LeuRS). The same compound was shown to be active against Toxoplasmaparasites, with the activity being enhanced in the presence of norvaline, an amino acid that can be mischarged by LeuRS. Our observations are consistent with AN6426 inhibiting protein synthesis in both Cryptosporidiumand Toxoplasmaby forming a covalent adduct with tRNALeuin the LeuRS editing active site and suggest that further exploitation of the benzoxaborole scaffold is a valid strategy to develop novel, much needed antiparasitic agents.

Published
2016
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149. Pachytene piRNAs instruct massive mRNA elimination during late spermiogenesis.

Author

Gou, Lan-Tao, Dai, Peng, Yang, Jian-Hua, Xue, Yuanchao, Hu, Yun-Ping, Zhou, Yu, Kang, Jun-Yan, Wang, Xin, Li, Hairi, Hua, Min-Min, Zhao, Shuang, Hu, Si-Da, Wu, Li-Gang, Shi, Hui-Juan, Li, Yong, Fu, Xiang-Dong, Qu, Liang-Hu, Wang, En-Duo, and Liu, Mo-Fang

Subjects
MAMMAL reproduction, SPERMATOGENESIS, PIWI genes, GENE silencing, GENE expression in mammals, DEADENYLATION, MESSENGER RNA
Abstract

Spermatogenesis in mammals is characterized by two waves of piRNA expression: one corresponds to classic piRNAs responsible for silencing retrotransponsons and the second wave is predominantly derived from nontransposon intergenic regions in pachytene spermatocytes, but the function of these pachytene piRNAs is largely unknown. Here, we report the involvement of pachytene piRNAs in instructing massive mRNA elimination in mouse elongating spermatids (ES). We demonstrate that a piRNA-induced silencing complex (pi-RISC) containing murine PIWI (MIWI) and deadenylase CAF1 is selectively assembled in ES, which is responsible for inducing mRNA deadenylation and decay via a mechanism that resembles the action of miRNAs in somatic cells. Such a highly orchestrated program appears to take full advantage of the enormous repertoire of diversified targeting capacity of pachytene piRNAs derived from nontransposon intergenic regions. These findings suggest that pachytene piRNAs are responsible for inactivating vast cellular programs in preparation for sperm production from ES. [ABSTRACT FROM AUTHOR]

Published
2014
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