Ribosomal Protein L27 Participates in both 50 S Subunit Assembly and the Peptidyl Transferase Reaction

This publication has 41 references indexed in Scilit:

• Peptide Environment of the Peptidyl Transferase Center from Escherichia coli 70 S Ribosomes as Determined by Thermoaffinity Labeling with Dihydrospiramycin
  Journal of Biological Chemistry, 1995
• RIBOSOMAL RNA AND TRANSLATION
  Annual Review of Biochemistry, 1991
• Localization of a series of RNA-protein cross-link sites in the 23S and 5S ribosomal RNA fromEscherichia coli, induced by treatment of 50S subunits with three different bifunctional reagents
  Nucleic Acids Research, 1990
• Synthesis and biological activity of photoactive derivatives of erythromycin
  Journal of Medicinal Chemistry, 1989
• RNA-protein cross-linking inEscherichia coli50S ribosontal subunits; determination of sites on 23S RNA that are cross-linked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane
  Nucleic Acids Research, 1988
• Localization of ribosomal protein L27 at the peptidyl transferase centre of the 50 S subunit, as determined by immuno-electron microscopy
  Molecular Genetics and Genomics, 1987
• Ribosome structure: binding site of macrolides studied by photoaffinity labeling
  Biochemistry, 1985
• The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29
  Nucleic Acids Research, 1981
• The primary structure of protein L27 from the peptidyl‐tRNA binding site of Escherichia coli ribosomes
  FEBS Letters, 1975
• Mapping of Escherichia coli Ribosomal Components Involved in Peptidyl Transferase Activity
  Proceedings of the National Academy of Sciences, 1973