Evidence map›Paper›PMID 25713070›Full record

ArticleThe Journal of biological chemistry2015

Exploration of the arrest peptide sequence space reveals arrest-enhanced variants.

Florian Cymer, Rickard Hedman, Nurzian Ismail, Gunnar von Heijne

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Translational landscape during seed germination revealed by ribosome profiling.The Plant journal : for cell and molecular biology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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

4 authors at 1 institution in 1 country.

Florian CymerFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden and.
Rickard HedmanFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden and.
Nurzian IsmailFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden and.
Gunnar von HeijneFrom the Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden and the Science for Life Laboratory Stockholm University, Box 1031, 17121 Solna, Sweden gunnar@dbb.su.se.
Stockholm University · SE

Funding

European Research Council 232648
6 · The paper itself

Abstract

Translational arrest peptides (APs) are short stretches of polypeptides that induce translational stalling when synthesized on a ribosome. Mechanical pulling forces acting on the nascent chain can weaken or even abolish stalling. APs can therefore be used as in vivo force sensors, making it possible to measure the forces that act on a nascent chain during translation with single-residue resolution. It is also possible to score the relative strengths of APs by subjecting them to a given pulling force and ranking them according to stalling efficiency. Using the latter approach, we now report an extensive mutagenesis scan of a strong mutant variant of the Mannheimia succiniciproducens SecM AP and identify mutations that further increase the stalling efficiency. Combining three such mutations, we designed an AP that withstands the strongest pulling force we are able to generate at present. We further show that diproline stretches in a nascent protein act as very strong APs when translation is carried out in the absence of elongation factor P. Our findings highlight critical residues in APs, show that certain amino acid sequences induce very strong translational arrest and provide a toolbox of APs of varying strengths that can be used for in vivo force measurements.

Indexed as

Gene Expression Regulation, BacterialAmino Acid SequenceBiomechanical PhenomenaEscherichia coliMannheimiaMolecular Sequence DataMutagenesis, Site-DirectedMutationPeptide Chain Elongation, TranslationalPeptide Elongation FactorsPeptidesRibosomesfactor EF-PPeptide Elongation FactorsPeptidesProtein SecretionRibosome FunctionSecMTranslationTranslation Elongation FactorTranslation Regulation

Identifiers

PMID25713070
PMCPMC4400336
OpenAlexW2092985726

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.