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Ibba, M., Francklyn, C. (2004) Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis. Proceedings of the National Academy of Sciences, 101 (20) 7493-7494 doi:10.1073/pnas.0402276101

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Reference TypeJournal (article/letter/editorial)
TitleTurning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis
JournalProceedings of the National Academy of Sciences
AuthorsIbba, M.Author
Francklyn, C.Author
Year2004 (May 18)Volume101
Issue20
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0402276101Search in ResearchGate
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Mindat Ref. ID1699404Long-form Identifiermindat:1:5:1699404:1
GUID0
Full ReferenceIbba, M., Francklyn, C. (2004) Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis. Proceedings of the National Academy of Sciences, 101 (20) 7493-7494 doi:10.1073/pnas.0402276101
Plain TextIbba, M., Francklyn, C. (2004) Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis. Proceedings of the National Academy of Sciences, 101 (20) 7493-7494 doi:10.1073/pnas.0402276101
In(2004, May) Proceedings of the National Academy of Sciences Vol. 101 (20) Proceedings of the National Academy of Sciences

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Minajigi, A., Francklyn, C. S. (2008) RNA-assisted catalysis in a protein enzyme: The 2'-hydroxyl of tRNAThr A76 promotes aminoacylation by threonyl-tRNA synthetase. Proceedings of the National Academy of Sciences, 105 (46) 17748-17753 doi:10.1073/pnas.0804247105
Korencic, D., Ahel, I., Schelert, J., Sacher, M., Ruan, B., Stathopoulos, C., Blum, P., Ibba, M., Soll, D. (2004) A freestanding proofreading domain is required for protein synthesis quality control in Archaea. Proceedings of the National Academy of Sciences, 101 (28) 10260-10265 doi:10.1073/pnas.0403926101
Arnez, J. G., Augustine, J. G., Moras, D., Francklyn, C. S. (1997) The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase. Proceedings of the National Academy of Sciences, 94 (14) 7144-7149 doi:10.1073/pnas.94.14.7144
Francklyn, C., Schimmel, P. (1990) Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proceedings of the National Academy of Sciences, 87 (21) 8655-8659 doi:10.1073/pnas.87.21.8655
Francklyn, C. (2003) tRNA synthetase paralogs: Evolutionary links in the transition from tRNA-dependent amino acid biosynthesis to de novo biosynthesis. Proceedings of the National Academy of Sciences, 100 (17) 9650-9652 doi:10.1073/pnas.1934245100
Pace, B., Matthews, E. A., Johnson, K. D., Cantor, C. R., Pace, N. R. (1982) Conserved 5S rRNA complement to tRNA is not required for protein synthesis. Proceedings of the National Academy of Sciences, 79 (1) 36-40 doi:10.1073/pnas.79.1.36
Arita, M. (2004) The metabolic world of Escherichia coli is not small. Proceedings of the National Academy of Sciences, 101 (6) 1543-1547 doi:10.1073/pnas.0306458101
Hanson, B. L. (2004) Getting protein solvent structures down cold. Proceedings of the National Academy of Sciences, 101 (47) 16393-16394 doi:10.1073/pnas.0407452101
Lipman, R. S. A., Hou, Y.-M. (1998) Aminoacylation of tRNA in the evolution of an aminoacyl-tRNA synthetase. Proceedings of the National Academy of Sciences, 95 (23) 13495-13500 doi:10.1073/pnas.95.23.13495
Carter, Charles W., Wolfenden, Richard (2015) tRNA acceptor stem and anticodon bases form independent codes related to protein folding. Proceedings of the National Academy of Sciences, 112 (24) 7489-7494 doi:10.1073/pnas.1507569112
Steiner, Rebecca E., Kyle, Amanda M., Ibba, Michael (2019) Oxidation of phenylalanyl-tRNA synthetase positively regulates translational quality control. Proceedings of the National Academy of Sciences, 116 (20) 10058-10063 doi:10.1073/pnas.1901634116
 
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