Iodination of Escherichia coli ribosomal protein L18 abolishes its 5 S RNA binding activity-Reference-Cited by-同舟云学术

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Iodination of Escherichia coli ribosomal protein L18 abolishes its 5 S RNA binding activity

Published:1981-02 Issue:2 Volume:652 Page:256-260
ISSN:0005-2787
Container-title:Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis

Author:

Fanning Thomas G.,Traut Robert R.

Publisher

Elsevier BV

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous)

Reference22 articles.

1. Structure and macromolecular interactions of 5S RNA. 1. Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli

2. Small-Angle X-Ray Titration Study on the Complex Formation between 5-S RNA and the L18 Protein of the Escherichia coli 50-S Ribosome Particle

3. Alteration of 5S RNA conformation by ribosomal proteins L18 and L25

4. Changes in the conformation and stability of 5 S RNA upon the binding of ribosomal proteins.

5. Identification of the nucleotide sequences involved in the interaction between Escherichia coli 5 S RNA and specific 50 S subunit proteins

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. 5S rRNA binding proteins from the hyperthermophilic archaeon,Pyrococcus furiosus;FEBS Letters;2000-12-12

2. Sequence, overproduction and purification of Vibrio proteolyticus ribosomal protein L 18 for in vitro and in vivo studies;Gene;1996-01

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