The Modification of the Peptidyltransferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Pyridoxal Phosphate
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb04851.x/fullpdf
Reference19 articles.
1. The Modification of the Peptidyl Transferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Ethoxyformic Anhydride
2. The Photochemical Inactivation of Peptidyl Transferase Activity
3. Photosensitization of specific histidine residues of rabbit muscle and spinach leaf aldolases by pyridoxal phosphate
4. Identification of a ribosomal protein essential for peptidyl transferase activity.
5. Modification of Essential Histidyl Residues of the β2 Subunit of Tryptophan Synthetase by Photo-oxidation in the Presence of Pyridoxal 5′-Phosphate and l-Serine and by Diethylpyrocarbonate
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2. Affinity labelling in situ of the bL12 protein on E. coli 70S ribosomes by means of a tRNA dialdehyde derivative;The Journal of Biochemistry;2017-08-16
3. Probing the functional role and localization of Escherichia coli ribosomal protein L16 with a monoclonal antibody;Journal of Biological Chemistry;1991-06
4. Reconstruction of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16;European Journal of Biochemistry;1987-03
5. Reconstitution of Escherichia coli ribosomes containing puromycin-modified S14: functional effects of the photoaffinity labeling of a protein essential for tRNA binding;Biochemistry;1986-12-01
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