Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids
Microbiological ReviewsPublished 1 December 1983Open access
Carl R. Woese, Robin R. Gutell, Ramesh C. Gupta, Harry F. Noller
Citations649
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The 180 to 220 Region is considered, as well as other Models, with the aim of determining the most effective and efficient approach to mountain bike mountaineering.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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A model is suggested for protein synthesis which depends upon conformational changes in tRNA and allosteric transitions in place of translocation.
Nature New BiologyRibosomal Discrimination of tRNAs
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PubMed[Nucleotide sequence of the gene for the mitochondrial 15S ribosomal RNA of yeast].
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42 Citations1973Henry W. Schaup, Mitchell L. Sogin +2 more
A region of 16S ribosomal ribonucleic acid that binds Escherichia coli Ribosomal protein S8 has been isolated and characterized and corresponds to what has been designated as fragment C of the ribon nucleic acid.
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40 Citations1976Vasilenko Sk, Ryte Vc
Dialysis, gel-chromatography on Sephadex G-75 (superfine) and chromatography on sulphoethylcellulose give high yield (68 per cent) of 162-fold purified ribonuclease from cobra venom.
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38 Citations1980Chantal Ehresmann, Patrick Stiegler +3 more
A ribonucleoprotein prepared by strong ribonuclease digestion of a complex of 16-S ribosomal RNA and proteins S4 and S20 from Escherichia coli has been characterized, and its nucleotide sequence, the positions of enzyme cuts and the sequence excisions have been placed in the completed sequence of16-S RNA.
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34 Citations1981Reinhard Lührmann, Marina Stöffler-Meilicke +1 more
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32 Citations1975Carl R. Woese, Cheryl D. Pribula +2 more
The sequence for 5S ribosomal RNA from Photobacter strain 8265 is eighteen base replacements removed from that of Escherichia coli, raising the prospect of a 5S RNA molecule that undergoes conformational transitions as part of the overall state changes that constitute the function of the ribosome.
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The location of protein S4 in the small ribosomal subunit has been identified by immunoelectron microscopy and it is located at a single site on the exterior (cytoplasmic) side of the subunit, at the partition that separates the one-third, or head, from two-thirds, or base, of thesubunit.
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Early in the assembly of Escherichia coli ribosomes, complexes between ribosomal protein S4 or S8 and 16S RNA were fixed gently with formaldehyde and then denatured for protein-free spreading to preserve an easily recognized configuration in the RNA that allows the sites of protein binding to be determined.
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21 Citations1982Seán Turner, John F. Thompson +2 more
The identification of a site for HMT crosslinking within positions 434 and 497 of 16S rRNA of E. coli ribosomal RNA is reported.
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The quantitative changes in tRNAVal are interpreted to indicate that C-17 spends a large portion of its lifetime in an unstacked conformation, consistent with the folded cloverleaf models that have been proposed from x-ray diffraction studies of yeast tRNAPhe.
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