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pubmed, google, scholar, article, cas, initiation, translation, central, cell, mrna, protein, biol, eukaryotic, ribosomal, nature, eif, mol, factor, rna, subunit, ribosome, pestova, complex, translational, mrnas, repression, regulation, hellen, genes, dev, codon, factors, human, sci, usa, proteins, mammalian, domain, proc, natl, acad, eife, structure, interaction, complexes, eifa, open, binding, access, site,

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nature portfolio permissions reprints privacy policy eif2–gtp–met-trnameti ternary complexes author information authors cap-distal iron-responsive elements advertising research social media sequence-specific rna-binding proteins nature cell biol micro-rna-mediated translation repression nature rev nature struct asp-glu-ala-asp asp-glu-x-asp composite nucleotide-binding sites classical gtpase-activator protein nature 455 nature 394 nature 403 nature 438 nature 447 nature cap-binding complex elf4f post-transcriptional gene expression affect pabp-dependent deadenylation codon–anticodon base pairing codon-anticodon base-pairing cap-independent translation switch hypoxia-controlled cap-dependent protein–protein interaction surfaces normal deadenylation-dependent route canonical scanning-dependent mode met-trnameti cold spring harbor dead-box protein ded1p recapitulate mirna-mediated repression mtor-independent translational upregulation blocks eif4f access post-termination ribosomal complexes springerlink instant access eif4g-pabp interaction increases dead-box rna helicase 'open' conformation open conformation internal ribosomal entry yeast eif4a–eif4g complex cap-binding complex eif4f stem-loop binding protein

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• How do microRNAs regulate gene expression?
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• What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?

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