Evidence map›Paper›PMID 23853096›Full record

ArticleThe Journal of biological chemistry2013

ADP-ribosylation of translation elongation factor 2 by diphtheria toxin in yeast inhibits translation and cell separation.

Maria K Mateyak, Terri Goss Kinzy

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Plasma cell-free RNA signatures of inflammatory syndromes in children.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  17. Article
  18. Article
  19. Developing anti-neoplastic biotherapeutics against eIF4F.Cellular and molecular life sciences : CMLS · 2017
    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 at 1 institution in 1 country.

Maria K MateyakDepartment of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA.
Terri Goss Kinzy
Rutgers, The State University of New Jersey · US

Funding

TRANSCRIPTIONAL PROFILINGP30CA072720 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI Chang S Chan · 1997 to 2026
$94.5M
Mechanism of Translation Elongation Factor 2 Inhibition by Bacterial ToxinsR21AI076245 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI KINZY, TERRI GOSS · 2009 to 2010
$420k
NCI NIH HHS P30 CA072720NIAID NIH HHS R21 AI076245
6 · The paper itself

Abstract

Eukaryotic translation elongation factor 2 (eEF2) facilitates the movement of the peptidyl tRNA-mRNA complex from the A site of the ribosome to the P site during protein synthesis. ADP-ribosylation (ADP(R)) of eEF2 by bacterial toxins on a unique diphthamide residue inhibits its translocation activity, but the mechanism is unclear. We have employed a hormone-inducible diphtheria toxin (DT) expression system in Saccharomyces cerevisiae which allows for the rapid induction of ADP(R)-eEF2 to examine the effects of DT in vivo. ADP(R) of eEF2 resulted in a decrease in total protein synthesis consistent with a defect in translation elongation. Association of eEF2 with polyribosomes, however, was unchanged upon expression of DT. Upon prolonged exposure to DT, cells with an abnormal morphology and increased DNA content accumulated. This observation was specific to DT expression and was not observed when translation elongation was inhibited by other methods. Examination of these cells by electron microscopy indicated a defect in cell separation following mitosis. These results suggest that expression of proteins late in the cell cycle is particularly sensitive to inhibition by ADP(R)-eEF2.

Indexed as

Cell CycleGene ExpressionProtein BiosynthesisAdenosine DiphosphateDiphtheria ToxinDNA, FungalEukaryotic Initiation Factor-2PolyribosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine DiphosphateDiphtheria ToxinDNA, FungalEukaryotic Initiation Factor-2Saccharomyces cerevisiae ProteinsADP-ribosylationBacterial ToxinsCell CycleDiphthamideProtein SynthesisTranslation Elongation Factors

Identifiers

PMID23853096
PMCPMC3750162
OpenAlexW1980812314

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.