The NMR structure ofEscherichia coliribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases-Reference-Cited by-同舟云学术

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The NMR structure ofEscherichia coliribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases

Published:1998-11-02 Issue:21 Volume:17 Page:6377-6384
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Stoldt Matthias¹,Wöhnert Jens¹,Görlach Matthias¹,Brown Larry R.¹

Affiliation:

1. Abteilung Molekulare Biophysik/NMR Spektroskopie, Institut für Molekulare Biotechnologie e. V., Postfach 100813; 07708 Jena Germany

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference85 articles.

1. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation;Allain;Nature,1996

2. Alpha helix-RNA major groove recognition in an HIV-1 rev peptide-RRE RNA complex;Battiste;Science,1996

3. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules;Bartels;J Biomol NMR,1995

4. Crystal structure of domain A of Thermus flavus 5S rRNA and the contribution of water molecules to its structure;Betzel;FEBS Lett,1994

5. The primary structure of the 5S rRNA binding protein L25 of Escherichia coli ribosomes;Bitar;Hoppe Seylers Z Physiol Chem,1975

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