Evidence map›Paper›PMID 26593721›Full record

ArticleMolecular cell2015

Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis.

Angelica Ferguson, Leyi Wang, Roger B Altman, Daniel S Terry, Manuel F Juette, Benjamin J Burnett, Jose L Alejo, Randall A Dass, Matthew M Parks, C Theresa Vincent and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.3field-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

61 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  7. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
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  11. Review
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  20. 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

1 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

11 authors at 2 institutions in 2 countries.

Angelica FergusonDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA; Tri-Institutional Training Program in Chemical Biology, Weill Cornell Medical College, Rockefeller University, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Leyi WangDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Roger B AltmanDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Daniel S TerryDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Manuel F JuetteDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Benjamin J BurnettDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Jose L AlejoDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Randall A DassDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
Matthew M ParksDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
C Theresa VincentDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA; Department of Pharmacology and Physiology, Karolinska Institute, 171 77 Stockholm, Sweden.
Scott C BlanchardDepartment of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA; Tri-Institutional Training Program in Chemical Biology, Weill Cornell Medical College, Rockefeller University, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA. Electronic address: scb2005@med.cornell.edu.
Cornell University · USMemorial Sloan Kettering Cancer Center · 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
NIGMS NIH HHS GM 079238NIGMS NIH HHS R01 GM079238
6 · The paper itself

Abstract

The regulation of protein synthesis contributes to gene expression in both normal physiology and disease, yet kinetic investigations of the human translation mechanism are currently lacking. Using single-molecule fluorescence imaging methods, we have quantified the nature and timing of structural processes in human ribosomes during single-turnover and processive translation reactions. These measurements reveal that functional complexes exhibit dynamic behaviors and thermodynamic stabilities distinct from those observed for bacterial systems. Structurally defined sub-states of pre- and post-translocation complexes were sensitive to specific inhibitors of the eukaryotic ribosome, demonstrating the utility of this platform to probe drug mechanism. The application of three-color single-molecule fluorescence resonance energy transfer (smFRET) methods further revealed a long-distance allosteric coupling between distal tRNA binding sites within ribosomes bearing three tRNAs, which contributed to the rate of processive translation.

Indexed as

Protein BiosynthesisAllosteric RegulationFluorescence Resonance Energy TransferHumansRibosomesRNA, TransferRNA, Transfer

Identifiers

PMID26593721
PMCPMC4660248
OpenAlexW2180353088

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.