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Gao, Y.G., Selmer, M., Dunham, C.M., Weixlbaumer, A., Kelley, A.C. and Ramakrishnan, V. (2009) The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State. Science, 326, 694-699.
http://dx.doi.org/10.1126/science.1179709

has been cited by the following article:

• TITLE: Structural Implications of Universal Complementarities in Translation—High Accuracy at the Decoding Site

  AUTHORS: Kozo Nagano

  KEYWORDS: Ribosomal RNA, Transfer RNA, Spectinomycin, Universal Rule, U33-Folded Form, U33-Extended Form, GTP Hydrolysis, Cognate, Near-Cognate

  JOURNAL NAME: Advances in Biological Chemistry, Vol.5 No.2, April 17, 2015

  ABSTRACT: X-ray structures of transfer RNAs (tRNAs) bound to the whole ribosome do not fully explain the mechanism of translation. The cause of the failure seems to come mainly from a high Mg2+ ion concentration compared to that in the living cells. There exists a wide range of nucleotide sequence conservation in tRNA and ribosomal RNAs (rRNAs) of small and large subunits as well as sequence complementarities, that seems to explain how high accuracy in translation can be achieved at the decoding site. Conformational transition between U33-folded and U33-extended forms of anticodon loops of tRNAs and G-C pair formation and disruption between C1399 and G1504 of 16S rRNA, etc. play the central role in explaining why E-site tRNA can automatically be expelled when an aminoacyl-tRNA at the A site turns out to be cognate.