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Nomanbhoy, T. K., Schimmel, P. R. (2000) Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase. Proceedings of the National Academy of Sciences, 97 (10) 5119-5122 doi:10.1073/pnas.090102197

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Reference TypeJournal (article/letter/editorial)
TitleMisactivated amino acids translocate at similar rates across surface of a tRNA synthetase
JournalProceedings of the National Academy of Sciences
AuthorsNomanbhoy, T. K.Author
Schimmel, P. R.Author
Year2000 (May 9)Volume97
Issue10
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.090102197Search in ResearchGate
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Mindat Ref. ID1639612Long-form Identifiermindat:1:5:1639612:4
GUID0
Full ReferenceNomanbhoy, T. K., Schimmel, P. R. (2000) Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase. Proceedings of the National Academy of Sciences, 97 (10) 5119-5122 doi:10.1073/pnas.090102197
Plain TextNomanbhoy, T. K., Schimmel, P. R. (2000) Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase. Proceedings of the National Academy of Sciences, 97 (10) 5119-5122 doi:10.1073/pnas.090102197
In(2000, May) Proceedings of the National Academy of Sciences Vol. 97 (10) Proceedings of the National Academy of Sciences

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Bishop, A. C., Nomanbhoy, T. K., Schimmel, P. (2002) Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase. Proceedings of the National Academy of Sciences, 99 (2) 585-590 doi:10.1073/pnas.012611299
Bishop, A. C., Beebe, K., Schimmel, P. R. (2003) Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase. Proceedings of the National Academy of Sciences, 100 (2) 490-494 doi:10.1073/pnas.0237335100
Swairjo, M. A., Schimmel, P. R. (2005) Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase. Proceedings of the National Academy of Sciences, 102 (4) 988-993 doi:10.1073/pnas.0409024102
Chihade, J. W., Brown, J. R., Schimmel, P. R., Ribas de Pouplana, L. (2000) Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase. Proceedings of the National Academy of Sciences, 97 (22) 12153-12157 doi:10.1073/pnas.220388797
Beebe, K., Merriman, E., de Pouplana, L. R., Schimmel, P. (2004) A domain for editing by an archaebacterial tRNA synthetase. Proceedings of the National Academy of Sciences, 101 (16) 5958-5963 doi:10.1073/pnas.0401530101
Miller, W. T., Schimmel, P. (1992) A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition. Proceedings of the National Academy of Sciences, 89 (6) 2032-2035 doi:10.1073/pnas.89.6.2032
Beuning, P. J., Musier-Forsyth, K. (2000) Hydrolytic editing by a class II aminoacyl-tRNA synthetase. Proceedings of the National Academy of Sciences, 97 (16) 8916-8920 doi:10.1073/pnas.97.16.8916
Steer, B. A., Schimmel, P. (1999) Domain-domain communication in a miniature archaebacterial tRNA synthetase. Proceedings of the National Academy of Sciences, 96 (24) 13644-13649 doi:10.1073/pnas.96.24.13644
Frugier, M., Giege, R., Schimmel, P. (2003) RNA recognition by designed peptide fusion creates "artificial" tRNA synthetase. Proceedings of the National Academy of Sciences, 100 (13) 7471-7475 doi:10.1073/pnas.1332771100
Liu, D. R., Magliery, T. J., Pastrnak, M., Schultz, P. G. (1997) Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo. Proceedings of the National Academy of Sciences, 94 (19) 10092-10097 doi:10.1073/pnas.94.19.10092
Schmidt, E., Schimmel, P. (1993) Dominant lethality by expression of a catalytically inactive class I tRNA synthetase. Proceedings of the National Academy of Sciences, 90 (15) 6919-6923 doi:10.1073/pnas.90.15.6919
 
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