Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation

By Joon-Hwa Lee, T. Pestova, B. Shin, C. Cao, S. Choi, T. Dever. 2002

123 citations recorded by the source corpus.

Subfields: Molecular Biology

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In Molecular Biology

1. Bridget Y. Huang
2. I. S. Fernández
3. M. Kozak
4. B. Kuhle
5. R. Ficner
6. G. Pavitt
7. W. Merrick

Citations in the corpus

• Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, background): “A second GTP-regulated step is then required for the recruitment of the large (60S) ribosomal subunit (14).”
• eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining (2014, background): “…of eIF5B GDP from the 80S ribosome In accordance with the function of G proteins as molecular switches, the formation of the elongation-competent 80S ribosome by eIF5B GTP results in GTP hydrolysis and Pi release, followed by the dissociation of eIF5B GDP (Lee et al, 2002; Pestova et al, 2000).”
• Regulation of translation via mRNA structure in prokaryotes and eukaryotes. (2005, background): “requires yet another protein factor (Lee et al., 2002; Shin et al., 2002).”