2′(3′)-O-N -formylmethionyl)-adenosine-5′-phosphate, a new donor substrate in peptidyl transferase catalyzed reactions
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(73)80455-7/fullpdf
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1. Structural requirements for inhibition of polyphenylalanine synthesis by aminoacyl and nucleotidyl analogues of puromycin
2. Ribosome-catalyzed peptidyl transfer: substrate specificity at the P-site.
3. Peptidyl-Donor Substrates for Ribosomal Peptidyl Transferase. Chemical Synthesis and Biological Activity of N-Acetyl Aminoacyl Di-and Tri-Nucleotides
4. Substrate specificity of ribosomal peptidyl transferase: 2′(3′)-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site
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2. Interaction of fMet-tRNAfMetand fMet-AMP with the C-terminal domain ofThermus thermophilustranslation initiation factor 2;European Journal of Biochemistry;2000-07
3. Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics;FEBS Letters;1997-04-14
4. Conserved Nucleotides of 23 S rRNA Located at the Ribosomal Peptidyltransferase Center;Journal of Biological Chemistry;1996-12
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