Evidence map›Paper›PMID 21617092›Full record

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

Converting structural information into an allosteric-energy-based picture for elongation factor Tu activation by the ribosome.

Andrew J Adamczyk, Arieh Warshel

Abstract 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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Structural basis of elongation factor 2 switching.Current research in structural biology · 2020
    Article
  8. Review
  9. Review
  10. Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  11. Article
  12. EF-Tu and EF-G are activated by allosteric effects.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Review
  15. Ribosome dynamics during decoding.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

2 authors.

Andrew J AdamczykDepartment of Chemistry, 418 Seeley G Mudd Building, University of Southern California, 3620 McClintock Avenue, Los Angeles, CA 90089-1062, USA.
Arieh Warshel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crucial process of aminoacyl-tRNA delivery to the ribosome is energized by the GTPase reaction of the elongation factor Tu (EF-Tu). Advances in the elucidation of the structure of the EF-Tu/ribosome complex provide the rare opportunity of gaining a detailed understanding of the activation process of this system. Here, we use quantitative simulation approaches and reproduce the energetics of the GTPase reaction of EF-Tu with and without the ribosome and with several key mutants. Our study provides a novel insight into the activation process. It is found that the critical H84 residue is not likely to behave as a general base but rather contributes to an allosteric effect, which includes a major transition state stabilization by the electrostatic effect of the P loop and other regions of the protein. Our findings have general relevance to GTPase activation, including the processes that control signal transduction.

Indexed as

Allosteric RegulationBinding SitesCatalytic DomainEnzyme ActivationGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisModels, MolecularMolecular StructureMutationPeptide Elongation Factor TuProtein Structure, TertiaryRibosomesStatic ElectricityThermodynamicsGTP PhosphohydrolasesGuanosine TriphosphatePeptide Elongation Factor Tu

Identifiers

PMID21617092
PMCPMC3116401

What OpenQuestion holds

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Registered trials

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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.