Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation.
By A. Hinnebusch. 2017
281 citations recorded by the source corpus.
Subfields: Molecular Biology
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In Molecular Biology
- I. S. Fernández
- M. Sokabe
- Joseph D. Puglisi
- Jinfan Wang
- Y. Hashem
- Joachim Frank
- Christopher P. Lapointe
- Bridget Y. Huang
Citations in the corpus
- Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation (2020, background): “The eIFs make extensive contacts with the 40S subunit, including the ribosomal A and P sites (23, 24).”
- Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation (2020, background): “The 48S complex, formed after mRNA recruitment by the 43S-PIC, dynamically scans the mRNA from the 5′ end for an AUG codon in a favorable context (10, 11).”
- Toward a Kinetic Understanding of Eukaryotic Translation. (2018, methodology): “The power of this combination has been highlighted by the successful test of start site selection models in yeast (reviewed inHinnebusch and Lorsch 2012; Hinnebusch 2014, 2017).”
- The Jigsaw Puzzle of mRNA Translation Initiation in Eukaryotes: A Decade of Structures Unraveling the Mechanics of the Process (2018, background): “The purpose of this review is not to revisit the field of eukaryotic translation initiation, as recent excellent and exhaustive reviews already exist in the literature (57), but rather to highlight the quintessential contribution of the field of structural biology to the understanding of this very c”
- mRNA-based therapeutics: powerful and versatile tools to combat diseases (2022, unknown): “eIF4F renders mRNA circularization by interacting with the 5′ cap through eIF4E and the PABP that binds with the poly(A) tail.(22) 40S ribosomal scans the 5′-UTR and recognizes initiation codon with the help of eIF4A to unwind the secondary structure of the 5′-UTR, subsequent, 40S ribosomal subunit ”