Aminoacyl and Peptidyl Analogs of Chloramphenicol as Slow-Binding Inhibitors of Ribosomal Peptidyltransferase: A New Approach for Evaluating Their Potency-Reference-Cited by-同舟云学术

Aminoacyl and Peptidyl Analogs of Chloramphenicol as Slow-Binding Inhibitors of Ribosomal Peptidyltransferase: A New Approach for Evaluating Their Potency

Published:1997-01-01 Issue:1 Volume:51 Page:139-146
ISSN:0026-895X
Container-title:Molecular Pharmacology
language:en
Short-container-title:Mol Pharmacol

Author:

Michelinaki Maria,Mamos Petros,Coutsogeorgopoulos Charalambos,Kalpaxis Dimitrios L.

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference32 articles.

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2. Gale E. F. Cundliffe E. Reynolds P. E. Richmond M. H. Waring M. J. (1981) The Molecular Basis of Antibiotic Action. (John Wiley & Sons, New York).

3. Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA

4. Identification of a rRNA/chloramphenicol interaction site within the peptidyltransferase center of the 50S subunit of the Escherichia coli ribosome.;Marconi;J. Biol. Chem.,1990

5. Fine Structure of the Peptidyl Transferase Centre on 23 S-like rRNAs Deduced from Chemical Probing of Antibiotic-Ribosome Complexes

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