Identification and Purification of Translation Initiation Factor 2 (IF2) from Thermus thermophilus
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1997.66_1a.x/fullpdf
Reference48 articles.
1. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
2. Crystals of protein L1 from the 50 S ribosomal subunit of Thermus thermophilus
3. Crystal structure of active elongation factor Tu reveals major domain rearrangements
4. Formylmethionyl-tRNA binding to 30 S ribosomes programmed with homopolynucleotides and the effect of translational initiation factor 3
5. The 2.9 Å Crystal Structure of T. thermophilus Seryl-tRNA Synthetase Complexed with tRNA Ser
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1. Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2;International Journal of Molecular Sciences;2023-04-05
2. Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components;Nucleic Acids Research;2012-06-21
3. Multidomain Initiation Factor 2 from Thermus thermophilus Consists of the Individual Autonomous Domains;Biochemistry;2008-04-01
4. Testing the conservation of the translational machinery over evolution in diverse environments: assaying Thermus thermophilus ribosomes and initiation factors in a coupled transcription-translation system from Escherichia coli;Nucleic Acids Research;2004-10-28
5. Development of a High-Throughput Scintillation Proximity Assay for the Identification of C-Domain Translational Initiation Factor 2 Inhibitors;Journal of Biomolecular Screening;2002-12
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