Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Sopapan, Atichartpongkul"'
Autor:
Kamonwan Phatinuwat, Sopapan Atichartpongkul, Watthanachai Jumpathong, Skorn Mongkolsuk, Mayuree Fuangthong
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-11 (2024)
Abstract Ribosomal RNA (rRNA) modifications are involved in multiple biological processes. KsgA is a 16S rRNA adenine dimethyltransferase that methylates at the adenines 1518 and 1519 (A1518/1519) positions, which are located near the ribosome decodi
Externí odkaz:
https://doaj.org/article/3186c65f72604dc8abb7c133c16dfcf5
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:
Juthamas Jaroensuk, Chalermroj Sutthaphirom, Jittima Phonbuppha, Wachirawit Chinantuya, Chatchai Kesornpun, Nattanon Akeratchatapan, Narongyot Kittipanukul, Kamonwan Phatinuwat, Sopapan Atichartpongkul, Mayuree Fuangthong, Thunyarat Pongtharangkul, Frank Hollmann, Pimchai Chaiyen
Cofactor imbalance obstructs the productivities of metabolically engineered cells. Herein, we employed a minimally perturbing system, xylose reductase and lactose (XR/lactose), to increase levels of a pool of sugar-phosphates which are connected to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de01366b00cf709e91745e68c692b68e
https://doi.org/10.1101/2023.01.08.523081
https://doi.org/10.1101/2023.01.08.523081
Autor:
Warunya Panmanee, Nisanart Charoenlap, Sopapan Atichartpongkul, Aekkapol Mahavihakanont, Matthew D Whiteside, Geoff Winsor, Fiona S L Brinkman, Skorn Mongkolsuk, Daniel J Hassett
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0189066 (2017)
The LysR member of bacterial transactivators, OxyR, governs transcription of genes involved in the response to H2O2 and organic (alkyl) hydroperoxides (AHP) in the Gram-negative pathogen, Pseudomonas aeruginosa. We have previously shown that organism
Externí odkaz:
https://doaj.org/article/9ea0183f8d074db3a9b15de238c777a0
Autor:
Siriwan Boonma, Adisak Romsang, Jintana Duang-Nkern, Sopapan Atichartpongkul, Wachareeporn Trinachartvanit, Paiboon Vattanaviboon, Skorn Mongkolsuk
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0172071 (2017)
Pseudomonas aeruginosa has two genes encoding ferredoxin NADP(+) reductases, denoted fprA and fprB. We show here that P. aeruginosa fprA is an essential gene. However, the ΔfprA mutant could only be successfully constructed in PAO1 strains containin
Externí odkaz:
https://doaj.org/article/d30ebaf396424adc85f30273729991fd
Autor:
Sopapan Atichartpongkul, Paiboon Vattanaviboon, Ratiphorn Wisitkamol, Juthamas Jaroensuk, Skorn Mongkolsuk, Mayuree Fuangthong
Publikováno v:
PLoS ONE, Vol 11, Iss 8, p e0161982 (2016)
Pseudomonas aeruginosa ohrR and ospR are gene homologs encoding oxidant sensing transcription regulators. OspR is known to regulate gpx, encoding a glutathione peroxidase, while OhrR regulates the expression of ohr that encodes an organic peroxide sp
Externí odkaz:
https://doaj.org/article/60f698c033f149e99f760bcaa3f34b95
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da12b70a826a32302d1628fac448dc34
https://doi.org/10.1093/nar/gkz702
https://doi.org/10.1093/nar/gkz702
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::10d0f9510160f0ccf682b4a455242e3b
https://doi.org/10.1261/rna.066746.118
https://doi.org/10.1261/rna.066746.118
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3ca8694e4caaaaf4dfd2356adbe83a5
https://doi.org/10.1093/nar/gkw870
https://doi.org/10.1093/nar/gkw870
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1452c72bf354e9cc2f9aceedcfafbc2e
https://pubmed.ncbi.nlm.nih.gov/31399541
https://pubmed.ncbi.nlm.nih.gov/31399541