Evidence map›Paper›PMID 12209000›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2002

Evolutionary conservation of reactions in translation.

M Clelia Ganoza, Michael C Kiel, Hiroyuki Aoki

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors.

M Clelia GanozaC. H. Best Institute, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5G 1L6. mganoza@utoronto.ca
Michael C Kiel
Hiroyuki Aoki

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Current X-ray diffraction and cryoelectron microscopic data of ribosomes of eubacteria have shed considerable light on the molecular mechanisms of translation. Structural studies of the protein factors that activate ribosomes also point to many common features in the primary sequence and tertiary structure of these proteins. The reconstitution of the complex apparatus of translation has also revealed new information important to the mechanisms. Surprisingly, the latter approach has uncovered a number of proteins whose sequence and/or structure and function are conserved in all cells, indicating that the mechanisms are indeed conserved. The possible mechanisms of a new initiation factor and two elongation factors are discussed in this context.

Indexed as

Evolution, MolecularFungal ProteinsProtein BiosynthesisRNA-Binding ProteinsAmino Acid SequenceConserved SequenceDNA-Binding ProteinsEukaryotic Initiation Factor-4AEukaryotic Translation Initiation Factor 5AMolecular Sequence DataPeptide Chain Elongation, TranslationalPeptide Elongation FactorsPeptide Initiation FactorsPeptidyl TransferasesRNA HelicasesSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsEukaryotic Initiation Factor-4AEukaryotic Translation Initiation Factor 5AFungal ProteinsPeptide Elongation FactorsPeptide Initiation FactorsPeptidyl TransferasesRNA-Binding ProteinsRNA HelicasesSaccharomyces cerevisiae ProteinsTranscription FactorsYEF3 protein, S cerevisiae

Identifiers

PMID12209000
PMCPMC120792

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.