The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes
- 15 December 1977
- journal article
- Published by Wiley in FEBS Letters
- Vol. 84 (2), 342-346
- https://doi.org/10.1016/0014-5793(77)80721-7
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Predictions for secondary structures of six proteins from the 50 S subunit of the Escherichia coli ribosomeFEBS Letters, 1977
- N-trimethylalanine, a novel blocking group, found in E. coli ribosomal protein L11Biochemical and Biophysical Research Communications, 1977
- The identification of new RNA‐binding proteins in the Escherichia coli ribosomeFEBS Letters, 1977
- Determination of the Amino‐Acid Sequence of the Ribosomal Protein S8 of Escherichia coliEuropean Journal of Biochemistry, 1976
- Studies on the significance of sequence homologies among proteins fromEscherichia coliribosomesFEBS Letters, 1976
- The Primary Structure of the 5S rRNA Binding Protein L25 of Escherichia coli RibosomesHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- Interdependence of E. coli ribosomal proteins at the peptidyltransferase centreFEBS Letters, 1974
- Properties of ribosomes and RNA synthesized by Escherichia coli grown in the presence of ethionine: III. Methylated proteins in 50 S ribosomes of E. coli EA2Journal of Molecular Biology, 1974
- Solid phase sequential analysis: Specific linking of acidic peptides by their carboxyl ends to insoluble resinsFEBS Letters, 1973
- SELECTIVE CLEAVAGE OF THE METHIONYL PEPTIDE BONDS IN RIBONUCLEASE WITH CYANOGEN BROMIDE1Journal of the American Chemical Society, 1961