Three-dimensional localization of the NH2- and carboxyl-terminal domain of ribosomal protein S1 on the surface of the 30 S subunit from Escherichia coli.-Reference-Cited by-同舟云学术

Three-dimensional localization of the NH2- and carboxyl-terminal domain of ribosomal protein S1 on the surface of the 30 S subunit from Escherichia coli.

Published:1990-07 Issue:19 Volume:265 Page:11338-11344
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Walleczek J,Albrecht-Ehrlich R,Stöffler G,Stöffler-Meilicke M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. Electron microscopy study of Qβreplicase

2. Comparative electron microscopic study on the location of ribosomal proteins S3 and S7 on the surface of the E. coli 30S subunit using monoclonal and conventional antibody

3. Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli

4. Segmental flexibility in Escherichia coli ribosomal protein S1 as studied by fluorescence polarization

5. Mobile domains in ribosomes revealed by proton nuclear magnetic resonance.

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1. Multiple activities of RNA-binding proteins S1 and Hfq;Biochimie;2012-07

2. Direct Interaction of the N-Terminal Domain of Ribosomal Protein S1 with Protein S2 in Escherichia coli;PLoS ONE;2012-03-07

3. Ribosomal protein S1 induces a conformational change of the 30S ribosomal subunit;FEBS Letters;2006-11-27

4. Diverse molecular mechanisms of translation initiation in prokaryotes;Molecular Biology;2006-07

5. Ribosomal Proteins in the Spotlight;Critical Reviews in Biochemistry and Molecular Biology;2005-01