Evidence map›Paper›PMID 18286627›Full record

ReviewBiopolymers2008

A new view of protein synthesis: mapping the free energy landscape of the ribosome using single-molecule FRET.

James B Munro, Andrea Vaiana, Kevin Y Sanbonmatsu, Scott C Blanchard

Open access · greenAbstract readReview
In one paragraph

Review in Biopolymers, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Impacts of ribosomal RNA sequence variation on gene expression and phenotype.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Computational studies of molecular machines: the ribosome.Current opinion in structural biology · 2012
    Review
  14. Functional dynamics of proteins.Computational and mathematical methods in medicine · 2012
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  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

4 authors at 2 institutions in 1 country.

James B MunroDepartment of Physiology and Biophysics, Weill Cornell Medical College of Cornell University, NY, USA.
Andrea Vaiana
Kevin Y Sanbonmatsu
Scott C Blanchard
Los Alamos National Laboratory · USCornell University · US

Funding

Imaging Protein Synthesis on the Ribosome using Single-Molecule FRETR01GM079238 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2006 to 2023
$7.0M
Large-Scale Simulations of Ribosomal DecodingR01GM072686 · NIGMS · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI SANBONMATSU, KARISSA Y · 2005 to 2024
$5.5M
NIGMS NIH HHS R01 GM072686NIGMS NIH HHS R01 GM079238
6 · The paper itself

Abstract

This article reviews the application of single-molecule fluorescence resonance energy transfer (smFRET) methods to the study of protein synthesis catalyzed by the ribosome. smFRET is a powerful new technique that can be used to investigate dynamic processes within enzymes spanning many orders of magnitude. The application of wide-field smFRET imaging methods to the study of dynamic processes in the ribosome offers a new perspective on the mechanism of protein synthesis. Using this technique, the structural and kinetic parameters of tRNA motions within wild-type and specifically mutated ribosome complexes have been obtained that provide valuable new insights into the mechanism and regulation of translation elongation. The results of these studies are discussed in the context of current knowledge of the ribosome mechanism from both structural and biophysical perspectives.

Indexed as

ThermodynamicsBinding SitesComputer SimulationFluorescence Resonance Energy TransferMutagenesis, Site-DirectedProtein BiosynthesisRibosomesRNA, TransferRNA, Transfer

Identifiers

PMID18286627
PMCPMC2930612
OpenAlexW2009556295

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.