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Recognition of γ-Subunit by β-Subunit in Translation Initiation Factor 2. Stabilization of the GTP-Bound State of I/F 2 in Archaea and Eukaryotes.
- Published in:
- Biochemistry (00062979), 2023, v. 88, n. 2, p. 221, doi. 10.1134/S0006297923020062
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- Article
Structure and Function of Archaeal Translation Initiation Factor 2 Fragments Containing Cys2‑Cys2 Motifs.
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- Biochemistry (00062979), 2021, v. 86, n. 8, p. 1003, doi. 10.1134/S0006297921080101
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- Article
The third structural switch in the archaeal translation initiation factor 2 (aIF2) molecule and its possible role in the initiation of GTP hydrolysis and the removal of aIF2 from the ribosome.
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- Acta Crystallographica: Section D, Structural Biology, 2019, v. 75, n. 4, p. 392, doi. 10.1107/S2059798319002304
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- Article
Crystal Structure of the 23S rRNA Fragment Specific to r-Protein L1 and Designed Model of the Ribosomal L1 Stalk from Haloarcula marismortui.
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- Crystals (2073-4352), 2017, v. 7, n. 2, p. 37, doi. 10.3390/cryst7020037
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Disruption of shape complementarity in the ribosomal protein L1-RNA contact region does not hinder specific recognition of the RNA target site.
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- Journal of Molecular Recognition, 2011, v. 24, n. 4, p. 524, doi. 10.1002/jmr.1063
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- Article
Domain I of ribosomal protein L1 is sufficient for specific RNA binding.
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- Nucleic Acids Research, 2007, v. 35, n. 21, p. 7389, doi. 10.1093/nar/gkm898
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- Article
Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.
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- Nucleic Acids Research, 2005, v. 33, n. 2, p. 478, doi. 10.1093/nar/gki194
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- Article
Structure of the L1 protuberance in the ribosome.
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- Nature Structural Biology, 2003, v. 10, n. 2, p. 104, doi. 10.1038/nsb886
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- Article
Crystal structure of the S15?rRNA complex.
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- Nature Structural Biology, 2000, v. 7, n. 4, p. 273
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- Article