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We are analyzing https://www.nature.com/articles/nrm2838.

Title:
The mechanism of eukaryotic translation initiation and principles of its regulation | Nature Reviews Molecular Cell Biology
Description:
Protein synthesis is regulated at the initiation stage. Determining the structures and activities of initiation factors, and mapping their interactions in ribosomal initiation complexes, has advanced our understanding of translation initiation and provided a foundation for studying its regulation. Protein synthesis is principally regulated at the initiation stage (rather than during elongation or termination), allowing rapid, reversible and spatial control of gene expression. Progress over recent years in determining the structures and activities of initiation factors, and in mapping their interactions in ribosomal initiation complexes, have advanced our understanding of the complex translation initiation process. These developments have provided a solid foundation for studying the regulation of translation initiation by mechanisms that include the modulation of initiation factor activity (which affects almost all scanning-dependent initiation) and through sequence-specific RNA-binding proteins and microRNAs (which affect individual mRNAs).
Website Age:
30 years and 10 months (reg. 1994-08-11).

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

Content Management System {📝}

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Custom-built

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What is the average monthly size of nature.com audience?

🌆 Monumental Traffic: 20M - 50M visitors per month


Based on our best estimate, this website will receive around 42,194,993 visitors per month in the current month.

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$531,700 per month
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Keywords {🔍}

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,

Topics {✒️}

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

Questions {❓}

  • How do microRNAs regulate gene expression?
  • Supplementary information S5 (box) | Does the "closed loop" configuration resulting from PABP-eIF4G interaction promote ribosome recycling?
  • What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?

Schema {🗺️}

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