Identification of Cysteine-10 of Protein S18 as Part of the mRNA-Binding Site of Escherichia coli Ribosomes by Affinity-Labeling Studies with a Chemically Reactive A-U-G Analog
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12742.x/fullpdf
Reference27 articles.
1. Affinity labeling of the ribosomal decoding site with an AUG-substrate analog.
2. The codon binding site of the Escherichia coli ribosome as studied with a chemically reactive A-U-G analog
3. Synthesis of a Chemically Reactive Analog of the Initiation Codon. Its Reaction with Ribosomes of Escherichia coli
4. Comparison of the reactions of chemically reactive analogs of U-G-A and of A-U-G with ribosomes of Escherichia coli
5. 5. H. Noll, M. Noll, B. Hapke, G. Dieijen, E. K. F. Bautz, P. Karlson, and H. Kersten (1973 ) inRegulation of Transcription and Translation in Eucaryotes, 24. Colloquium der Gesellschaft fur Biologische Chemie () pp.257 -311 , Berlin, Heidelberg, New York.
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1. Placement of dinitrophenyl-modified ribosomal proteins in totally reconstituted Escherichia coli 30 S subunits. Localization of proteins S6, S13, S16, and S18 by immune electron microscopy.;Journal of Biological Chemistry;1993-09
2. Affinity labelling of rat liver ribosomal protein S26 by heptauridylate containing a 5?-terminal alkylating group;Molecular Biology Reports;1984-01
3. Dissimilation of methionine in cell suspension cultures from Catharanthus roseus L.;Planta;1983-08
4. Identification of tyrosine residues that are susceptible to lactoperoxidase-catalyzed iodination on the surface of Escherichia coli 30S ribosomal subunit;Biochemistry;1983-05
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