Evidence map›Paper›PMID 20117091›Full record

ReviewBiochemical and biophysical research communications2010

Divergent stalling sequences sense and control cellular physiology.

Koreaki Ito, Shinobu Chiba, Kit Pogliano

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  5. Article
  6. Review
  7. Structural insight into co-translational membrane protein folding.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Resistance to Macrolide Antibiotics in Public Health Pathogens.Cold Spring Harbor perspectives in medicine · 2016
    Review
  14. The ribosome in action: Tuning of translational efficiency and protein folding.Protein science : a publication of the Protein Society · 2016
    Review
  15. Ribosomal Antibiotics: Contemporary Challenges.Antibiotics (Basel, Switzerland) · 2016
    Review
  16. Amino acid sequence repertoire of the bacterial proteome and the occurrence of untranslatable sequences.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. How do bacteria tune translation efficiency?Current opinion in microbiology · 2015
    Review
  20. Review
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 at 3 institutions in 2 countries.

Koreaki ItoFaculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita-Ku, Kyoto 603-8555, Japan. kito@cc.kyoto-su.ac.jp
Shinobu Chiba
Kit Pogliano
Kyoto Sangyo University · JPKyoto University · JPUniversity of California, San Diego · US

Funding

FORESPORE ENGULFMENT DURING B SUBTILIS SPORULATIONR01GM057045 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI POGLIANO, KIT J · 1998 to 2021
$6.1M
NIGMS NIH HHS R01 GM057045
6 · The paper itself

Abstract

Recent studies have identified several amino acid sequences that interact with the ribosomal interior components and arrest their own elongation. Whereas stalling of the inducible class depends on specific low-molecular weight compounds, that of the intrinsic class is released when the nascent chain is transported across or inserted into the membrane. The stalled ribosome alters messenger RNA secondary structure and thereby contributes to regulation of the cis-located target gene expression at different levels. The stalling sequences are divergent but likely to utilize non-uniform nature of the peptide bond formation reactions and are recruited relatively recently to different biological systems, possibly including those to be identified in forthcoming studies.

Indexed as

Amino Acid SequencePeptide Chain Elongation, TranslationalAnti-Bacterial AgentsDirected Molecular EvolutionEscherichia coli ProteinsGene Expression RegulationNucleic Acid ConformationProtein Sorting SignalsRibosomesRNA, MessengerTranscription FactorsTryptophanAnti-Bacterial AgentsEscherichia coli ProteinsProtein Sorting SignalsRNA, MessengerSecM protein, E colitnaC protein, E coliTranscription FactorsTryptophan

Identifiers

PMID20117091
PMCPMC2885147
OpenAlexW2061225259

What OpenQuestion holds

Textmetadata
LicenceTDM
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.