Evidence map›Paper›PMID 21368145›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1.

Aymen S Yassin, Md Emdadul Haque, Partha P Datta, Kevin Elmore, Nilesh K Banavali, Linda L Spremulli, Rajendra K Agrawal

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Transplantation ofMicrobiology (Reading, England) · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Evolution: Mitochondrial Ribosomes Across Species.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Assembly of the Mitochondrial Translation Initiation Complex.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  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

7 authors at 2 institutions in 2 countries.

Aymen S YassinWadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY 12201-0509, USA.
Md Emdadul Haque
Partha P Datta
Kevin Elmore
Nilesh K Banavali
Linda L Spremulli
Rajendra K Agrawal
Wadsworth Center · USUniversity of North Carolina at Chapel Hill · US

Funding

Structural Aspects of Protein Synthesis in the Mammalian MitochondriaR01GM061576 · NIGMS · WADSWORTH CENTER · PI AGRAWAL, RAJENDRA K · 2001 to 2018
$6.4M
NIGMS NIH HHS R01 GM061576NIGMS NIH HHS R01 GM61576
6 · The paper itself

Abstract

Mitochondria have their own translational machineries for the synthesis of thirteen polypeptide chains that are components of the complexes that participate in the process of oxidative phosphorylation (or ATP generation). Translation initiation in mammalian mitochondria requires two initiation factors, IF2(mt) and IF3(mt), instead of the three that are present in eubacteria. The mammalian IF2(mt) possesses a unique 37 amino acid insertion domain, which is known to be important for the formation of the translation initiation complex. We have obtained a three-dimensional cryoelectron microscopic map of the mammalian IF2(mt) in complex with initiator fMet-tRNA(iMet) and the eubacterial ribosome. We find that the 37 amino acid insertion domain interacts with the same binding site on the ribosome that would be occupied by the eubacterial initiation factor IF1, which is absent in mitochondria. Our finding suggests that the insertion domain of IF2(mt) mimics the function of eubacterial IF1, by blocking the ribosomal aminoacyl-tRNA binding site (A site) at the initiation step.

Indexed as

Amino AcidsAnimalsCattleCryoelectron MicroscopyEubacteriumEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-2Models, MolecularOxidative PhosphorylationRibosomesAmino AcidsEukaryotic Initiation Factor-1Eukaryotic Initiation Factor-2

Identifiers

PMID21368145
PMCPMC3053986
OpenAlexW2025329004

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.