@ARTICLE{Kirillov198391,
author={Kirillov, S.V. and Makarov, E.M. and Semenkov, Yu.P.},
title={Quantitative study of interaction of deacylated tRNA with Escherichia coli ribosomes. Role of 50 S subunits in formation of the E site},
journal={FEBS Letters},
year={1983},
volume={157},
number={1},
pages={91-94},
doi={10.1016/0014-5793(83)81122-3},
note={cited By 81},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020534216&doi=10.1016%2f0014-5793%2883%2981122-3&partnerID=40&md5=ab1383a0ed2da9252e2777bd1c40ddb0},
affiliation={B.P. Konstantinov Nuclear Physics Institute, USSR Academy of Sciences, Gatchina, Leningrad district 188350, Russian Federation},
abstract={The 30 S subunit contains 2 sites for tRNA binding (Phe-tRNA, AcPhe-tRNA, tRNA Phe OH ) with the functional properties of D and A sites of the 70 S ribosome after attachment of 50 S subunit. The third (E) site specific for deacylated tRNA is introduced into 70 S ribosome by its 50 S subunit. The E-site binding of tRNA Phe OH is not sensitive to either tetracycline and edeine, and practically codon-independent. The affinity constant of tRNA Phe OH for the E site is 2-3 orders of magnitude lower than that for the D site. © 1983.},
author_keywords={Antibiotic, tetracycline, edeine;  Deacylated tRNA-ribosome interaction;  Ribosome, exit site;  Site distribution, between subunits},
correspondence_address1={Kirillov, S.V.; B.P. Konstantinov Nuclear Physics Institute, USSR Academy of Sciences, Gatchina, Leningrad district 188350, Russian Federation},
issn={00145793},
coden={FEBLA},
pubmed_id={6345196},
language={English},
abbrev_source_title={FEBS Lett.},
document_type={Article},
source={Scopus},
}

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