Photoaffinity reaction between polyuridylic acid and protein S1 on the Escherichia coli ribosome
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)80825-8/fullpdf
Reference17 articles.
1. Functional heterogeneity of the 30S ribosomal subunit of E. coli
2. Chemical modification of the transfer RNA and polyuridylic acid binding sites of Escherichia coli 30 s ribosomal subunits
3. Polyuridylic acid binding and translating by Escherichia coli ribosomes: Stimulation by Protein 1, inhibition by aurintricarboxylic acid
4. Reaction of ribosomal sulfhydryl groups with 5,5′-dithiobis(2-nitrobenzoic acid)
5. Use of Protection of 30S Ribosomal Proteins by tRNA for Functional Mapping of the E. coli Ribosome
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1. Formation of protein conjugates of phosphorothioate nucleoside diphosphate beta-S;Nucleic Acids Research;1993
2. Messenger RNA Path Through the Procaryotic Ribosome;The Translational Apparatus;1993
3. Ribosome-mRNA contact sites at different stages of translation initiation as revealed by cross-linking of model mRNAs;Biochimie;1991-12
4. Photoaffinity labelling of Escherichia coli ribosomes;Pharmacology & Therapeutics;1987-01
5. Substitution of uridine in vivo by the intrinsic photoactivable probe 4-thiouridine in Escherichia coli RNA. Its use for E. coli ribosome structural analysis;European Journal of Biochemistry;1986-11
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