eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining

By B. Kuhle, R. Ficner. 2014

57 citations recorded by the source corpus.

Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Bridget Y. Huang
2. I. S. Fernández
3. G. Pavitt
4. W. Merrick
5. C. Fraser
6. M. Sokabe

In Radiology, Nuclear Medicine and Imaging

1. G. Pavitt
2. W. Merrick

Citations in the corpus

• Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, background): “The current model for how eIF5B works involves a “domain release” mechanism, which is induced by an initial, off-ribosome GTP-binding event (19).”
• Protein Synthesis Initiation in Eukaryotic Cells. (2018, methodology): “A recent “remodeling” performed by Kuhle and Ficner (2014) places theMet-tRNAi 30 CCA end and the methionine in domain IV of eIF5B in a position equivalent to that seen with either IF2 or EF1A (EF-Tu) and their aminoacyl-tRNAs.”