The ternary complex of EF-Tu and its role in protein biosynthesis
- 11 February 1997
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 7 (1) , 110-116
- https://doi.org/10.1016/s0959-440x(97)80014-0
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Elongation in bacterial protein biosynthesisCurrent Opinion in Biotechnology, 1996
- A complex profile of protein elongation: translating chemical energy into molecular movementStructure, 1996
- Direct Visualization of A-, P-, and E-Site Transfer RNAs in the Escherichia coli RibosomeScience, 1996
- The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatusStructure, 1996
- Ribosomal proteins and elongation factorsCurrent Opinion in Structural Biology, 1995
- Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP AnalogScience, 1995
- A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosomeNature, 1995
- The 70S Escherichia coli ribosome at 23 å resolution: fitting the ribosomal RNAStructure, 1995
- Structural aspects of ribonucleoprotein interactions in ribosomesCurrent Opinion in Structural Biology, 1993
- Recognition of tRNAs by aminoacyl-tRNA synthetases.The FASEB Journal, 1993