Initiation Factor IF2, Thiostrepton and Micrococcin Prevent the Binding of Elongation Factor G to the Escherichia coli Ribosome
- 24 May 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 319 (1), 27-35
- https://doi.org/10.1016/s0022-2836(02)00235-8
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- RanGAP mediates GTP hydrolysis without an arginine fingerNature, 2002
- Initiation factor IF 2 binds to the α-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNARNA, 2001
- Macromolecular mimicryThe EMBO Journal, 2000
- A Conformational Switch in Escherichia coli 16 S Ribosomal RNA During Decoding of Messenger RNAScience, 1997
- G PROTEIN MECHANISMS: Insights from Structural AnalysisAnnual Review of Biochemistry, 1997
- The GTPase-activating Protein RGS4 Stabilizes the Transition State for Nucleotide HydrolysisPublished by Elsevier ,1996
- The GTPase superfamily: a conserved switch for diverse cell functionsNature, 1990
- Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNANature, 1988
- Influence of Guanine Nucleotides and Elongation Factors on Interaction of Release Factors with the RibosomeProceedings of the National Academy of Sciences, 1973
- Ribosomes Cannot Interact Simultaneously with Elongation Factors EF Tu and EF GProceedings of the National Academy of Sciences, 1972