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Van Noort, J. M., Kraal, B., Bosch, L. (1985) A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome. Proceedings of the National Academy of Sciences, 82 (10) 3212-3216 doi:10.1073/pnas.82.10.3212

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Reference TypeJournal (article/letter/editorial)
TitleA second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome.
JournalProceedings of the National Academy of Sciences
AuthorsVan Noort, J. M.Author
Kraal, B.Author
Bosch, L.Author
Year1985 (May 1)Volume82
Issue10
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.82.10.3212Search in ResearchGate
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Mindat Ref. ID1441454Long-form Identifiermindat:1:5:1441454:1
GUID0
Full ReferenceVan Noort, J. M., Kraal, B., Bosch, L. (1985) A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome. Proceedings of the National Academy of Sciences, 82 (10) 3212-3216 doi:10.1073/pnas.82.10.3212
Plain TextVan Noort, J. M., Kraal, B., Bosch, L. (1985) A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome. Proceedings of the National Academy of Sciences, 82 (10) 3212-3216 doi:10.1073/pnas.82.10.3212
In(1985, May) Proceedings of the National Academy of Sciences Vol. 82 (10) Proceedings of the National Academy of Sciences

See Also

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Van Noort, J. M., Kraal, B., Bosch, L. (1986) GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site. Proceedings of the National Academy of Sciences, 83 (13) 4617-4621 doi:10.1073/pnas.83.13.4617
Van Noort, J. M., Kraal, B., Bosch, L., La Cour, T. F., Nyborg, J., Clark, B. F. (1984) Cross-linking of tRNA at two different sites of the elongation factor Tu. Proceedings of the National Academy of Sciences, 81 (13) 3969-3972 doi:10.1073/pnas.81.13.3969
Gagnon, Matthieu G., Lin, Jinzhong, Steitz, Thomas A. (2016) Elongation factor 4 remodels the A-site tRNA on the ribosome. Proceedings of the National Academy of Sciences, 113 (18) 4994-4999 doi:10.1073/pnas.1522932113
Janosi, L., Shimizu, I., Kaji, A. (1994) Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth. Proceedings of the National Academy of Sciences, 91 (10) 4249-4253 doi:10.1073/pnas.91.10.4249
Cabrer, B., Vazquez, D., Modolell, J. (1972) Inhibition by Elongation Factor EF G of Aminoacyl-tRNA Binding to Ribosomes. Proceedings of the National Academy of Sciences, 69 (3) 733-736 doi:10.1073/pnas.69.3.733
(1979) Correction: A Factor in Serum and Amniotic Fluid is a Substrate for the tRNA-Modifying Enzyme tRNA-Guanine Transferase. Proceedings of the National Academy of Sciences, 76 (10) 5411 doi:10.1073/pnas.76.10.5411-b
Lake, J. A. (1977) Aminoacyl-tRNA binding at the recognition site is the first step of the elongation cycle of protein synthesis. Proceedings of the National Academy of Sciences, 74 (5) 1903-1907 doi:10.1073/pnas.74.5.1903
March, P. E., Inouye, M. (1985) GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and G. Proceedings of the National Academy of Sciences, 82 (22) 7500-7504 doi:10.1073/pnas.82.22.7500
Rolland, N., Janosi, L., Block, M. A., Shuda, M., Teyssier, E., Miege, C., Cheniclet, C., Carde, J.-P., Kaji, A., Joyard, J. (1999) Plant ribosome recycling factor homologue is a chloroplastic protein and is bactericidal in Escherichia coli carrying temperature-sensitive ribosome recycling factor. Proceedings of the National Academy of Sciences, 96 (10) 5464-5469 doi:10.1073/pnas.96.10.5464
Schrader, J. M., Chapman, S. J., Uhlenbeck, O. C. (2011) Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding. Proceedings of the National Academy of Sciences, 108 (13) 5215-5220 doi:10.1073/pnas.1102128108
Georgiou, T., Yu, Y.- T. N., Ekunwe, S., Buttner, M. J., Zuurmond, A.- M., Kraal, B., Kleanthous, C., Snyder, L. (1998) Specific peptide-activated proteolytic cleavage of Escherichia coli elongation factor Tu. Proceedings of the National Academy of Sciences, 95 (6) 2891-2895 doi:10.1073/pnas.95.6.2891
 
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