Probing the functional role and localization of Escherichia coli ribosomal protein L16 with a monoclonal antibody
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference46 articles.
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2. Identification of a ribosomal protein essential for peptidyl transferase activity.
3. The peptidyltransferase centre of the Escherichia coli ribosome. The histidine of protein L16 affects the reconstitution and control of the active centre but is not essential for release-factor-mediated peptidyl-tRNA hydrolysis and peptide bond formation
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1. Gene expression modulation by chalcopyrite and bornite in Acidithiobacillus ferrooxidans;Archives of Microbiology;2010-05-18
2. Solution Structure of Ribosomal Protein L16 from Thermus thermophilus HB8;Journal of Molecular Biology;2004-12
3. Mutations in Ribosomal Protein L16 Conferring Reduced Susceptibility to Evernimicin (SCH27899): Implications for Mechanism of Action;Antimicrobial Agents and Chemotherapy;2000-03
4. Incorporation of dinitrophenyl derivatives of proteins S6, S13, S16, and S18 into the 30 S subunit of Escherichia coli ribosomes by total reconstitution.;Journal of Biological Chemistry;1993-09
5. Monoclonal antibodies to Escherichia coli ribosomal proteins L9 and L10. Effects on ribosome function and localization of L9 on the surface of the 50 S ribosomal subunit.;Journal of Biological Chemistry;1991-11
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