Evidence map›Paper›PMID 28138066›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2017

The translation elongation cycle-capturing multiple states by cryo-electron microscopy.

Joachim Frank

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Machines on Genes through the Computational Microscope.Journal of chemical theory and computation · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Relating Structure and Dynamics in RNA Biology.Cold Spring Harbor perspectives in biology · 2019
    Review
  10. New Insights into Ribosome Structure and Function.Cold Spring Harbor perspectives in biology · 2019
    Review
  11. Review
  12. Perspectives on the ribosome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Article
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

1 author.

Joachim FrankDepartment of Biochemistry and Molecular Biophysics, Columbia University, Black Building, 650 W. 168th Street, New York, NY 10032, USA jf2192@cumc.columbia.edu.ORCID 0000-0001-5449-6943

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
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM055440
6 · The paper itself

Abstract

During the work cycle of elongation, the ribosome, a molecular machine of vast complexity, exists in a large number of states distinguished by constellation of its subunits, its subunit domains and binding partners. Single-particle cryogenic electron microscopy (cryo-EM), developed over the past 40 years, is uniquely suited to determine the structure of molecular machines in their native states. With the emergence, 10 years ago, of unsupervised clustering techniques in the analysis of single-particle data, it has been possible to determine multiple structures from a sample containing ribosomes equilibrating in different thermally accessible states. In addition, recent advances in detector technology have made it possible to reach near-atomic resolution for some of these states. With these capabilities, single-particle cryo-EM has been at the forefront of exploring ribosome dynamics during its functional cycle, along with single-molecule fluorescence resonance energy transfer and molecular dynamics computations, offering insights into molecular architecture uniquely honed by evolution to capitalize on thermal energy in the ambient environment.This article is part of the themed issue 'Perspectives on the ribosome'.

Indexed as

Peptide Chain Elongation, TranslationalCryoelectron MicroscopyRibosomesfree-energy landscapemolecular machinesmRNA–tRNA translocationsingle-particle reconstruction

Identifiers

PMID28138066
PMCPMC5311924

What OpenQuestion holds

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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.