Evidence map›Paper›PMID 21719661›Full record

ArticleScience (New York, N.Y.)2011

Comment on "The mechanism for activation of GTP hydrolysis on the ribosome".

Anders Liljas, Måns Ehrenberg, Johan Åqvist

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Structural basis of elongation factor 2 switching.Current research in structural biology · 2020
    Article
  3. Review
  4. 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
  5. Review
  6. Article
  7. Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Role of a ribosomal RNA phosphate oxygen during the EF-G-triggered GTP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Structural Insights into tRNA Dynamics on the Ribosome.International journal of molecular sciences · 2015
    Review
  11. Article
  12. Article
  13. Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Translocation at work.Nature structural & molecular biology · 2013
    Article
  15. Structure of EF-G-ribosome complex in a pretranslocation state.Nature structural & molecular biology · 2013
    Article
  16. Article
  17. Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Physical chemistry chemical physics : PCCP · 2013
    Article
  18. Article
  19. Why nature really chose phosphate.Quarterly reviews of biophysics · 2013
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Anders LiljasDepartment of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden. anders.liljas@biochemistry.lu.se
Måns Ehrenberg
Johan Åqvist
Uppsala University · SELund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voorhees et al. (Reports, 5 November 2010, p. 835) determined the structure of elongation factor Tu (EF-Tu) and aminoacyl-transfer RNA bound to the ribosome with a guanosine triphosphate (GTP) analog. However, their identification of histidine-84 of EF-Tu as deprotonating the catalytic water molecule is problematic in relation to their atomic structure; the terminal phosphate of GTP is more likely to be the proper proton acceptor.

Indexed as

GTP PhosphohydrolasesGuanosine TriphosphateHistidineHydrogen BondingHydrolysisHydrophobic and Hydrophilic InteractionsModels, MolecularPeptide Elongation Factor TuPhosphatesProtonsRibosomesRNA, BacterialRNA, Ribosomal, 23SRNA, Transfer, Amino AcylWaterGTP Phosphohydrolasesguanosine 5'-(beta,gamma-methylene)triphosphateGuanosine TriphosphateHistidinePeptide Elongation Factor TuPhosphatesProtonsRNA, BacterialRNA, Ribosomal, 23SRNA, Transfer, Amino AcylWater

Identifiers

PMID21719661
OpenAlexW1999326148

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.