A Covariant Change of the Two Highly Conserved Bases in the GTPase-associated Center of 28 S rRNA in Silkworms and Other Moths

This publication has 32 references indexed in Scilit:

• Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome
  Proceedings of the National Academy of Sciences, 1999
• A Detailed View of a Ribosomal Active Site: The Structure of the L11–RNA Complex
  Cell, 1999
• Crystal Structure of a Conserved Ribosomal Protein-RNA Complex
  Science, 1999
• The ribosome-in-pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA
  Proceedings of the National Academy of Sciences, 1997
• A Base Substitution within the GTPase-associated Domain of Mammalian 28 S Ribosomal RNA Causes High Thiostrepton Accessibility
  Published by Elsevier ,1995
• Stabilization of a ribosomal RNA tertiary structure by ribosomal protein L11
  Journal of Molecular Biology, 1995
• RIBOSOMAL RNA AND TRANSLATION
  Annual Review of Biochemistry, 1991
• The conserved GTPase center and variable region V9 from Saccharomyces cerevisiae 26S rRNA can be replaced by their equivalents from other prokaryotes or eukaryotes without detectable loss of ribosomal function.
  Proceedings of the National Academy of Sciences, 1991
• Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA
  Nature, 1988
• Ribosomal proteins EL11 from Escherichia coli and L15 from Saccharomyces cerevisiae bind to the same site in both yeast 26 S and mouse 28 S rRNA
  Journal of Molecular Biology, 1987