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Biochemistry|November 18, 1986
Reaction of some macrolide antibiotics with the ribosome. Labeling of the binding site componentsF Tejedor, J P BallestaThe Journal of Biological Chemistry|September 1, 1995
The highly conserved protein P0 carboxyl end is essential for ribosome activity only in the absence of proteins P1 and P2C Santos, J P BallestaEuropean Journal of Biochemistry|July 15, 1994
Mechanism of resistance to the antibiotic trichothecin in the producing fungiM Iglesias, J P BallestaJournal of Bacteriology|April 1, 1972
Dependence of the rate of synthesis of phosphatidylethanolamine and phosphatidylglycerol on the rate of growth of Escherichia coliJ P Ballesta, M SchaechterThe Journal of Antimicrobial Chemotherapy|July 1, 1985
Components of the macrolide binding site on the ribosomeF Tejedor, J P BallestaJournal of Bacteriology|June 1, 1971
Resistance of Zygorhynchus species to lysisJ P Ballesta, M AlexanderProceedings of the National Academy of Sciences of the United States of America|October 1, 1972
Elongation factor T-dependent hydrolysis of guanosine triphosphate resistant to thiostreptonJ P Ballesta, D VazquezArchives of Biochemistry and Biophysics|February 23, 2000
Ribosomal stalk protein phosphorylating activities in Saccharomyces cerevisiaeG Bou, M Remacha, J P BallestaMolecular and Cellular Biology|May 1, 1990
Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiaeM Remacha, C Santos, J P BallestaThe Journal of Biological Chemistry|February 5, 1993
The activity-controlling phosphorylation site is not the same in the four acidic ribosomal proteins from Saccharomyces cerevisiaeT Naranda, M Remacha, J P BallestaPageof 11