Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Narumon, Thongdee"'
Autor:
Thanyaporn Srimahaeak, Narumon Thongdee, Jurairat Chittrakanwong, Sopapan Atichartpongkul, Juthamas Jaroensuk, Kamonwan Phatinuwat, Narumon Phaonakrop, Janthima Jaresitthikunchai, Sittiruk Roytrakul, Skorn Mongkolsuk, Mayuree Fuangthong
Publikováno v:
Frontiers in Microbiology, Vol 13 (2023)
Pseudomonas aeruginosa gidA, which encodes a putative tRNA-modifying enzyme, is associated with a variety of virulence phenotypes. Here, we demonstrated that P. aeruginosa gidA is responsible for the modifications of uridine in tRNAs in vivo. Loss of
Externí odkaz:
https://doaj.org/article/52567aab93074bc0bb7d508bb2f506e3
Autor:
Thanyaporn Srimahaeak, Jurairat Chittrakanwong, Narumon Thongdee, Pimchai Chaiyen, Sopapan Atichartpongkul, Juthamas Jaroensuk, Kamonchanok Chooyoung, Skorn Mongkolsuk, Mayuree Fuangthong, Paiboon Vattanaviboon
Publikováno v:
Nucleic Acids Research
Cellular response to oxidative stress is a crucial mechanism that promotes the survival of Pseudomonas aeruginosa during infection. However, the translational regulation of oxidative stress response remains largely unknown. Here, we reveal a tRNA mod
Autor:
Somchart Maenpuen, Narumon Thongdee, Erin G. Prestwich, Skorn Mongkolsuk, Wenhe Zhong, Abbas El Sahili, Sopapan Atichartpongkul, Yok Hian Chionh, Megan E. McBee, Julien Lescar, Chong Wai Liew, Juthamas Jaroensuk, Pimchai Chaiyen, Yee Hwa Wong, Peter C. Dedon, Michael S. DeMott, Mayuree Fuangthong, Qianhui Nah
Publikováno v:
RNA. 25:1481-1496
The tRNA (m1G37) methyltransferase TrmD catalyzes m1G formation at position 37 in many tRNA isoacceptors and is essential in most bacteria, which positions it as a target for antibiotic development. In spite of its crucial role, little is known about
Autor:
Narumon Thongdee, Julien Lescar, Juthamas Jaroensuk, Michael S. DeMott, Chong Wai Liew, Mayuree Fuangthong, Yee Hwa Wong, Yok Hian Chionh, Sopapan Atichartpongkul, Skorn Mongkolsuk, Peter C. Dedon, Megan E. McBee, Erin G. Prestwich
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩
Oxford University Press
Nucleic Acids Research, Oxford University Press, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩
Nucleic Acids Research, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩
Oxford University Press
Nucleic Acids Research, Oxford University Press, 2016, 44 (22), pp.10834-10848. ⟨10.1093/nar/gkw870⟩
Bacteria respond to environmental stresses using a variety of signaling and gene expression pathways, with translational mechanisms being the least well understood. Here, we identified a tRNA methyltransferase in Pseudomonas aeruginosa PA14, trmJ, wh
Autor:
Juthamas, Jaroensuk, Yee Hwa, Wong, Wenhe, Zhong, Chong Wai, Liew, Somchart, Maenpuen, Abbas E, Sahili, Sopapan, Atichartpongkul, Yok Hian, Chionh, Qianhui, Nah, Narumon, Thongdee, Megan E, McBee, Erin G, Prestwich, Michael S, DeMott, Pimchai, Chaiyen, Skorn, Mongkolsuk, Peter C, Dedon, Julien, Lescar, Mayuree, Fuangthong
Publikováno v:
RNA
The tRNA (m(1)G37) methyltransferase TrmD catalyzes m(1)G formation at position 37 in many tRNA isoacceptors and is essential in most bacteria, which positions it as a target for antibiotic development. In spite of its crucial role, little is known a