Evidence map›Paper›PMID 10200264›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2.

J H Lee, S K Choi, A Roll-Mecak, S K Burley, T E Dever

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. A Novel Inhibitor of Translation Initiation Factor eIF5B inJournal of microbiology and biotechnology · 2024
    Article
  4. Article
  5. Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

J H LeeLaboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2716, USA.
S K Choi
A Roll-Mecak
S K Burley
T E Dever
Rockefeller University · USHoward Hughes Medical Institute · USNational Institutes of Health · 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
$29.4M
REGULATION OF EUKARYOTIC PROTEIN SYNTHESISZ01HD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 1995 to 2008
$2.6M
6 · The paper itself

Abstract

Binding of initiator methionyl-tRNA to ribosomes is catalyzed in prokaryotes by initiation factor (IF) IF2 and in eukaryotes by eIF2. The discovery of both IF2 and eIF2 homologs in yeast and archaea suggested that these microbes possess an evolutionarily intermediate protein synthesis apparatus. We describe the identification of a human IF2 homolog, and we demonstrate by using in vivo and in vitro assays that human IF2 functions as a translation factor. In addition, we show that archaea IF2 can substitute for its yeast homolog both in vivo and in vitro. We propose a universally conserved function for IF2 in facilitating the proper binding of initiator methionyl-tRNA to the ribosomal P site.

Indexed as

Peptide Initiation FactorsAmino Acid SequenceArchaeaArchaeal ProteinsBacterial ProteinsConserved SequenceEukaryotic Initiation Factor-2HumansKineticsMolecular Sequence DataPhylogenyProkaryotic Initiation Factor-2Protein BiosynthesisSaccharomyces cerevisiaeArchaeal ProteinsBacterial ProteinsEukaryotic Initiation Factor-2IF2 protein, archaealPeptide Initiation FactorsProkaryotic Initiation Factor-2

Identifiers

PMID10200264
PMCPMC16334
OpenAlexW2049223383

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.