Evidence map›Paper›PMID 27016205›Full record

ArticleJournal of molecular biology2016

Structural Dynamics and Mechanochemical Coupling in DNA Gyrase.

Aakash Basu, Angelica C Parente, Zev Bryant

Abstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural and Computational Analysis ofbioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
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  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Single-Molecule Magnetic Tweezer Analysis of Topoisomerases.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  19. Article
  20. 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

3 authors.

Aakash BasuDepartment of Physics, University of Illinois at Urbana-Champaign,Urbana, IL 61801, USA.
Angelica C ParenteProgram in Biophysics, Stanford University, Stanford, CA 94305, USA; Department of Bioengineering, Stanford University, Stanford, CA 94305, USA.
Zev BryantDepartment of Bioengineering, Stanford University, Stanford, CA 94305, USA; Department of Structural Biology, Stanford University Medical Center, Stanford, CA 94305, USA. Electronic address: zevry@stanford.edu.

Funding

Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Structural Dynamics and Mechanochemical Coupling in Nucleoprotein MachinesR01GM106159 · NIGMS · STANFORD UNIVERSITY · PI Zev Bryant · 2014 to 2026
$3.2M
NIGMS NIH HHS R01 GM106159NIGMS NIH HHS T32 GM008294
6 · The paper itself

Abstract

Gyrase is a molecular motor that harnesses the free energy of ATP hydrolysis to perform mechanical work on DNA. The enzyme specifically introduces negative supercoiling in a process that must coordinate fuel consumption with DNA cleavage and religation and with numerous conformational changes in both the protein and DNA components of a large nucleoprotein complex. Here we present a current understanding of mechanochemical coupling in this essential molecular machine, with a focus on recent diverse biophysical approaches that have revealed details of molecular architectures, new conformational intermediates, structural transitions modulated by ATP binding, and the influence of mechanics on motor function. Recent single-molecule assays have also illuminated the reciprocal relationships between supercoiling and transcription, an illustration of mechanical interactions between gyrase and other molecular machines at the heart of chromosomal biology.

Indexed as

Adenosine TriphosphateDNADNA GyraseHydrolysisModels, BiologicalModels, MolecularMolecular Motor ProteinsNucleic Acid ConformationProtein ConformationAdenosine TriphosphateDNADNA GyraseMolecular Motor ProteinsFRETmagnetic tweezersmolecular motorsingle-moleculetopoisomerase

Identifiers

PMID27016205
PMCPMC5083069

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.