Evidence map›Paper›PMID 18717565›Full record

ArticleACS chemical biology2008

Chain dynamics of nascent polypeptides emerging from the ribosome.

Jamie P Ellis, Courtney K Bakke, Robert N Kirchdoerfer, Lisa M Jungbauer, Silvia Cavagnero

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-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

27 citing papers in PubMed, 64 citations in OpenAlex.

  1. Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021
    Review
  11. Article
  12. Hijacking Translation Initiation for Synthetic Biology.Chembiochem : a European journal of chemical biology · 2020
    Review
  13. Review
  14. Review
  15. AnThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
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  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Jamie P EllisDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706, USA.
Courtney K Bakke
Robert N Kirchdoerfer
Lisa M Jungbauer
Silvia Cavagnero
University of Wisconsin–Madison · US

Funding

PREDOCTORAL TRAINING IN MOLECULAR BIOPHYSICST32GM008293 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 1989 to 2016
$4.6M
A FRET/LRET Approach to Nascent Polypeptide ConformationR21GM071012 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CAVAGNERO, SILVIA · 2005 to 2006
$295k
NIGMS NIH HHS R21 GM071012NIGMS NIH HHS R21GM071012NIGMS NIH HHS T32 GM008293NIGMS NIH HHS T32 GM08293
6 · The paper itself

Abstract

Very little is known about the conformation of polypeptides emerging from the ribosome during protein biosynthesis. Here, we explore the dynamics of ribosome-bound nascent polypeptides and proteins in Escherichia coli by dynamic fluorescence depolarization and assess the population of cotranslationally active chaperones trigger factor (TF) and DnaK. E. coli cell-free technology and fluorophore-linked E. coli Met-tRNA f Met enable selective site-specific labeling of nascent proteins at the N-terminal methionine. For the first time, direct spectroscopic evidence captures the generation of independent nascent chain motions for a single-domain protein emerging from the ribosome (apparent rotational correlation time approximately 5 ns), during the intermediate and late stages of polypeptide elongation. Such motions are detected only for a sequence encoding a globular protein and not for a natively unfolded control, suggesting that the independent nascent chain dynamics may be a signature of folding-competent sequences. In summary, we observe multicomponent, severely rotationally restricted, and strongly chain length/sequence-dependent nascent chain dynamics.

Indexed as

Protein BiosynthesisApoproteinsEscherichia coliEscherichia coli ProteinsFluorescence PolarizationMyoglobinPeptidesPeptidylprolyl IsomeraseProtein ConformationRibosomesapomyoglobinApoproteinsEscherichia coli ProteinsMyoglobinPeptidesPeptidylprolyl Isomerasetrigger factor, E coli

Identifiers

PMID18717565
PMCPMC2572860
OpenAlexW2033926064

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.