Evidence map›Paper›PMID 20235828›Full record

ReviewAnnual review of biochemistry2010

Structure and dynamics of a processive Brownian motor: the translating ribosome.

Joachim Frank, Ruben L Gonzalez

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing 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

141 citing papers in PubMed.

  1. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Article
  3. Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025
    Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Taming the ribosome.Biophysical journal · 2024
    Article
  13. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Entropic control of the free-energy landscape of an archetypal biomolecular machine.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Article

81 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

2 authors.

Joachim FrankHoward Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York City, New York 10032, USA. jf2192@columbia.edu
Ruben L Gonzalez

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
The Structural Dynamics of Translation InitiationR01GM084288 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GONZALEZ, RUBEN L · 2009 to 2022
$4.4M
STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLYR37GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2006
$2.8M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM084288NIGMS NIH HHS R01 GM55440NIGMS NIH HHS R37 GM029169NIGMS NIH HHS R37GM29169
6 · The paper itself

Abstract

There is mounting evidence indicating that protein synthesis is driven and regulated by mechanisms that direct stochastic, large-scale conformational fluctuations of the translational apparatus. This mechanistic paradigm implies that a free-energy landscape governs the conformational states that are accessible to and sampled by the translating ribosome. This scenario presents interdependent opportunities and challenges for structural and dynamic studies of protein synthesis. Indeed, the synergism between cryogenic electron microscopic and X-ray crystallographic structural studies, on the one hand, and single-molecule fluorescence resonance energy transfer (smFRET) dynamic studies, on the other, is emerging as a powerful means for investigating the complex free-energy landscape of the translating ribosome and uncovering the mechanisms that direct the stochastic conformational fluctuations of the translational machinery. In this review, we highlight the principal insights obtained from cryogenic electron microscopic, X-ray crystallographic, and smFRET studies of the elongation stage of protein synthesis and outline the emerging themes, questions, and challenges that lie ahead in mechanistic studies of translation.

Indexed as

Peptide Chain Elongation, TranslationalAnimalsCryoelectron MicroscopyCrystallography, X-RayFluorescence Resonance Energy TransferHumansProtein BiosynthesisRibosomesRNA, TransferRNA, Transfer

Identifiers

PMID20235828
PMCPMC2917226

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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.