Evidence map›Paper›PMID 26926435›Full record

ArticleNature structural & molecular biology2016

Multiperspective smFRET reveals rate-determining late intermediates of ribosomal translocation.

Michael R Wasserman, Jose L Alejo, Roger B Altman, Scott C Blanchard

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. 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
10.3field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 128 citations in OpenAlex.

  1. eLife · 2026
    Article
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  5. Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025
    Article
  6. Simulating biomolecules for physiological timescales.Current opinion in structural biology · 2025
    Review
  7. Article
  8. Article
  9. Article
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  12. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
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  15. Article
  16. Article
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  18. Article
  19. The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. 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 at 2 institutions in 1 country.

Michael R WassermanDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Jose L AlejoDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Roger B AltmanDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Scott C BlanchardDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Cornell University · USTri-Institutional PhD Program in Chemical Biology · 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
Next-generation Fluorescent Probes for Biological ResearchR01GM098859 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI BLANCHARD, SCOTT C · 2012 to 2019
$2.9M
smFRET Investigation of Aminoglycoside-induced OtotoxicityF31DC012026 · NIDCD · WEILL MEDICAL COLL OF CORNELL UNIV · PI WASSERMAN, MICHAEL R · 2011 to 2013
$126k
NIDCD NIH HHS F31 DC012026NIGMS NIH HHS 2R01GM079238NIGMS NIH HHS 5R01GM098859NIGMS NIH HHS R01 GM079238NIGMS NIH HHS R01 GM098859
6 · The paper itself

Abstract

Directional translocation of the ribosome through the mRNA open reading frame is a critical determinant of translational fidelity. This process entails a complex interplay of large-scale conformational changes within the actively translating particle, which together coordinate the movement of tRNA and mRNA substrates with respect to the large and small ribosomal subunits. Using pre-steady state, single-molecule fluorescence resonance energy transfer imaging, we tracked the nature and timing of these conformational events within the Escherichia coli ribosome from five structural perspectives. Our investigations revealed direct evidence of structurally and kinetically distinct late intermediates during substrate movement, whose resolution determines the rate of translocation. These steps involve intramolecular events within the EF-G-GDP-bound ribosome, including exaggerated, reversible fluctuations of the small-subunit head domain, which ultimately facilitate peptidyl-tRNA's movement into its final post-translocation position.

Indexed as

Escherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferGuanosine DiphosphateModels, MolecularPeptide Elongation Factor GProtein TransportRibosomesRNA, BacterialRNA, Transfer, Amino AcylEscherichia coli ProteinsGuanosine DiphosphatePeptide Elongation Factor GRNA, BacterialRNA, Transfer, Amino AcyltRNA, peptidyl-

Identifiers

PMID26926435
PMCPMC4821728
OpenAlexW2294416498

What OpenQuestion holds

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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.