ArticleNature2022
eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining.
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Article in Nature, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51citing papers in PubMed
6.0field-weighted citation impact, top 2% of its field
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Who cites it
51 citing papers in PubMed, 74 citations in OpenAlex.
- Review
- Review
- Translation initiation by the Kozak mRNA sequence is based on a conformational readout on the ribosome.Nature communications · 2026Article
- Remodeling of mRNA by eIF4F in human translation initiation.bioRxiv : the preprint server for biology · 2026Article
- A ribosomal kinetic checkpoint governs selective mRNA recruitment.bioRxiv : the preprint server for biology · 2026Article
- Observing intersubunit dynamics in single yeast ribosomes.Nucleic acids research · 2026Article
- Toward a unifying mechanistic model of eukaryotic translation initiation through integrative single-molecule, structural, and computational insights.Current opinion in structural biology · 2026Review
- Three-color single-molecule fluorescence resonance energy transfer to study macromolecular dynamics.Current opinion in structural biology · 2026Review
- Mechanisms of human mitochondrial leaderless mRNA translation initiation.Nature communications · 2026Article
- The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES.The EMBO journal · 2026Article
- Functional characterization of dynamic nascent RNA folding ensembles in real time.Science advances · 2026Article
- Article
- Structural insights into the role of eIF3 in translation mediated by the HCV IRES.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025Article
- Two dynamically competing factors determine the translation start site.Nature structural & molecular biology · 2025Article
- Canonical translation factors eIF1A and eIF5B modulate the initiation step of repeat-associated non-AUG translation.Nucleic acids research · 2025Article
- Advancing Single-Molecule Biophysics: Next-Generation Organic Fluorophores with Tailored Labeling Strategies.Chemical & biomedical imaging · 2025Review
- FMRP drives mRNP targets into translationally silenced complexes.Molecular cell · 2025Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Christopher P LapointeDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID http://orcid.org/0000-0002-0406-105X
Rosslyn Grosely *Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Masaaki Sokabe *Department of Molecular and Cellular Biology College of Biological Sciences, University of California, Davis, CA, USA.
Carlos AlvaradoDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Jinfan WangDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.ORCID http://orcid.org/0000-0003-4170-9289
Elizabeth MontabanaDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Nancy VillaDepartment of Molecular and Cellular Biology College of Biological Sciences, University of California, Davis, CA, USA.
Byung-Sik ShinSection on Protein Biosynthesis, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Thomas E DeverSection on Protein Biosynthesis, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0001-7120-9678
Christopher S FraserDepartment of Molecular and Cellular Biology College of Biological Sciences, University of California, Davis, CA, USA.
Israel S FernándezDepartment of Structural Biology, St Jude Children's Research Hospital, Memphis, TN, USA. israel.s.fernandez@gmail.com.ORCID http://orcid.org/0000-0001-7218-1603
Joseph D PuglisiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA. puglisi@stanford.edu.ORCID http://orcid.org/0000-0001-9268-5112
Stanford University · USUniversity of California, Davis · USNational Institutes of Health · USSt. Jude Children's Research Hospital · US
Funding
Mechanism and Regulation of Eukaryotic Protein SynthesisZIAHD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 2009 to 2025
$29.4MSTRUCTURAL BASIS FOR RIBOSOME FUNCTIONSR01GM051266 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PUGLISI, JOSEPH D · 1995 to 2021
$7.7MThe mechanism of mRNA recruitment to the human ribosome.R01GM092927 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI FRASER, CHRISTOPHER S · 2010 to 2022
$4.1MDynamics of TranslationR35GM145306 · NIGMS · STANFORD UNIVERSITY · PI JOSEPH D PUGLISI · 2022 to 2026
$3.8MDynamics of eukaryotic translation initiation and its controlR01GM113078 · NIGMS · STANFORD UNIVERSITY · PI PUGLISI, JOSEPH D · 2016 to 2021
$2.9MDefining modifiers and mechanisms of RAN translationRF1AG064690 · NIA · STANFORD UNIVERSITY · PI GITLER, AARON D., PUGLISI, JOSEPH D · 2019 to 2019
$2.8MDefining modifiers and mechanisms of RAN translationR01AG064690 · NIA · STANFORD UNIVERSITY · PI Aaron D. Gitler, JOSEPH D PUGLISI · 2024 to 2026
$2.3MFrom one end to the other: dynamics of human translation initiation and its controlR00GM144678 · NIGMS · FRED HUTCHINSON CANCER CENTER · PI LAPOINTE, CHRISTOPHER PAUL · 2023 to 2024
$498kFrom one end to the other: dynamics of human translation initiation and its controlK99GM144678 · NIGMS · STANFORD UNIVERSITY · PI LAPOINTE, CHRISTOPHER PAUL · 2022 to 2023
$164kNIA NIH HHS R01 AG064690NIA NIH HHS RF1 AG064690NIGMS NIH HHS K99 GM144678NIGMS NIH HHS R00 GM144678NIGMS NIH HHS R01 GM051266NIGMS NIH HHS R01 GM092927NIGMS NIH HHS R01 GM113078NIGMS NIH HHS R35 GM145306NIH HHS AG064690NIH HHS GM011378
Abstract
Translation initiation defines the identity and quantity of a synthesized protein. The process is dysregulated in many human diseases
Indexed as
Eukaryotic Initiation Factor-1Eukaryotic Initiation FactorsRibosome SubunitsRNA, Transfer, MetCryoelectron MicroscopyHumansSingle Molecule ImagingEukaryotic Initiation Factor-1eukaryotic initiation factor-5BEukaryotic Initiation Factorseukaryotic peptide initiation factor-1ARNA, Transfer, Met
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