Evidence map›Paper›PMID 25422471›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Trajectories of the ribosome as a Brownian nanomachine.

Ali Dashti, Peter Schwander, Robert Langlois, Russell Fung, Wen Li, Ahmad Hosseinizadeh, Hstau Y Liao, Jesper Pallesen, Gyanesh Sharma, Vera A Stupina and 4 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing 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

122 citing papers in PubMed.

  1. Article
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  7. Amortized template matching of molecular conformations from cryoelectron microscopy images using simulation-based inference.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
  11. Article
  12. Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Article
  14. Article
  15. End-to-end Training of Latent Space Diffusion Models for Conformational Heterogeneity in Cryo-EM Reconstruction.International Conference Image and Vision Computing New Zealand : [proceedings]. International Conference Image and Vision Computing New Zealand · 2024
    Article
  16. Article
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  18. Article
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62 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

14 authors.

Ali DashtiDepartment of Physics, University of Wisconsin, Milwaukee, WI 53211;
Peter SchwanderDepartment of Physics, University of Wisconsin, Milwaukee, WI 53211;
Robert LangloisDepartment of Biochemistry and Molecular Biophysics, and.
Russell FungDepartment of Physics, University of Wisconsin, Milwaukee, WI 53211;
Wen LiDepartment of Biochemistry and Molecular Biophysics, and.
Ahmad HosseinizadehDepartment of Physics, University of Wisconsin, Milwaukee, WI 53211;
Hstau Y LiaoDepartment of Biochemistry and Molecular Biophysics, and.
Jesper PallesenHoward Hughes Medical Institute, Columbia University, New York, NY 10032; and.
Gyanesh SharmaDepartment of Biochemistry and Molecular Biophysics, and.
Vera A StupinaDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742.
Anne E SimonDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742.
Jonathan D DinmanDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742.
Joachim FrankDepartment of Biochemistry and Molecular Biophysics, and Howard Hughes Medical Institute, Columbia University, New York, NY 10032; and jf2192@columbia.edu ourmazd@uwm.edu.
Abbas OurmazdDepartment of Physics, University of Wisconsin, Milwaukee, WI 53211; jf2192@columbia.edu ourmazd@uwm.edu.

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
Translational Fidelity in EukaryotesR01GM058859 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D · 1999 to 2011
$3.8M
X-linked Dyskeratosis Congenita and Ribosomal FrameshiftingR01HL119439 · NHLBI · UNIV OF MARYLAND, COLLEGE PARK · PI DINMAN, JONATHAN D, RUGGERO, DAVIDE · 2014 to 2017
$2.8M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL119439NIGMS NIH HHS GM55440NIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM058859NIGMS NIH HHS R01 GM29169
6 · The paper itself

Abstract

A Brownian machine, a tiny device buffeted by the random motions of molecules in the environment, is capable of exploiting these thermal motions for many of the conformational changes in its work cycle. Such machines are now thought to be ubiquitous, with the ribosome, a molecular machine responsible for protein synthesis, increasingly regarded as prototypical. Here we present a new analytical approach capable of determining the free-energy landscape and the continuous trajectories of molecular machines from a large number of snapshots obtained by cryogenic electron microscopy. We demonstrate this approach in the context of experimental cryogenic electron microscope images of a large ensemble of nontranslating ribosomes purified from yeast cells. The free-energy landscape is seen to contain a closed path of low energy, along which the ribosome exhibits conformational changes known to be associated with the elongation cycle. Our approach allows model-free quantitative analysis of the degrees of freedom and the energy landscape underlying continuous conformational changes in nanomachines, including those important for biological function.

Indexed as

Protein BiosynthesisBuffersCryoelectron MicroscopyFungal ProteinsKineticsModels, MolecularMolecular Dynamics SimulationMotionNanoparticlesNanotechnologyProtein ConformationRibosomesTemperatureThermodynamicsBuffersFungal Proteinscryo-electron microscopyelongation cyclemanifold embeddingnanomachinestranslation

Identifiers

PMID25422471
PMCPMC4267381

What OpenQuestion holds

Textmetadata
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.