Evidence map›Paper›PMID 19647434›Full record

ReviewTrends in biochemical sciences2009

Navigating the ribosome's metastable energy landscape.

James B Munro, Kevin Y Sanbonmatsu, Christian M T Spahn, Scott C Blanchard

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
–field-weighted citation impact
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

81 citing papers in PubMed.

  1. Article
  2. 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
  3. Review
  4. Practical Synthesis ofACS chemical biology · 2023
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Getting to the bottom of lncRNA mechanism: structure-function relationships.Mammalian genome : official journal of the International Mammalian Genome Society · 2022
    Review
  11. Assembly factors chaperone ribosomal RNA folding by isolating helical junctions that are prone to misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. POLARIS: Path of Least Action Analysis on Energy Landscapes.Journal of chemical information and modeling · 2020
    Article
  15. Article
  16. New Insights into Ribosome Structure and Function.Cold Spring Harbor perspectives in biology · 2019
    Review
  17. Article
  18. Article
  19. Review
  20. Miscoding-induced stalling of substrate translocation on the bacterial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article

21 more citing papers are in PubMed but not listed here.

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.

James B MunroDepartment of Physiology and Biophysics, Weill Cornell Medical College, 1300 York Avenue, New York, NY 10021, USA.
Kevin Y Sanbonmatsu
Christian M T Spahn
Scott C Blanchard

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 GM 079238NIGMS NIH HHS R01 GM072686NIGMS NIH HHS R01 GM079238
6 · The paper itself

Abstract

The molecular mechanisms by which tRNA molecules enter and transit the ribosome during mRNA translation remains elusive. However, recent genetic, biochemical and structural studies offer important new findings into the ordered sequence of events underpinning the translocation process that help place the molecular mechanism within reach. In particular, new structural and kinetic insights have been obtained regarding tRNA movements through 'hybrid state' configurations. These dynamic views reveal that the macromolecular ribosome particle, like many smaller proteins, has an intrinsic capacity to reversibly sample an ensemble of similarly stable native states. Such perspectives suggest that substrates, factors and environmental cues contribute to translation regulation by helping the dynamic system navigate through a highly complex and metastable energy landscape.

Indexed as

Protein BiosynthesisBinding SitesModels, MolecularNucleic Acid ConformationRibosomesRNA, MessengerRNA, TransferThermodynamicsRNA, MessengerRNA, Transfer

Identifiers

PMID19647434
PMCPMC2914510

What OpenQuestion holds

Textmetadata
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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.