Evidence map›Paper›PMID 24972228›Full record

ArticlePhysical review letters2014

Stochastic ratchet mechanisms for replacement of proteins bound to DNA.

S Cocco, J F Marko, R Monasson

Abstract read
In one paragraph

Article in Physical review letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Facilitated dissociation of transcription factors from single DNA binding sites.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Molecular Mechanism of Facilitated Dissociation of Fis Protein from DNA.Journal of the American Chemical Society · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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.

S Cocco1Laboratoire de Physique Statistique de l'Ecole Normale Supérieure, CNRS and Université Pierre and Marie Curie, 75005 Paris, France.
J F Marko2Department of Molecular Biosciences and Department of Physics and Astronomy, Northwestern University, Evanston, Illinois 60208, USA.
R Monasson3Laboratoire de Physique Théorique de l'Ecole Normale Supérieure, CNRS and Université Pierre and Marie Curie, 75005 Paris, France.

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
NCI NIH HHS 1U54CA143869-01NCI NIH HHS U54 CA143869
6 · The paper itself

Abstract

Experiments indicate that unbinding rates of proteins from DNA can depend on the concentration of proteins in nearby solution. Here we present a theory of multistep replacement of DNA-bound proteins by solution-phase proteins. For four different kinetic scenarios we calculate the dependence of protein unbinding and replacement rates on solution protein concentration. We find (1) strong effects of progressive "rezipping" of the solution-phase protein onto DNA sites liberated by "unzipping" of the originally bound protein, (2) that a model in which solution-phase proteins bind nonspecifically to DNA can describe experiments on exchanges between the nonspecific DNA-binding proteins Fis-Fis and Fis-HU, and (3) that a binding specific model describes experiments on the exchange of CueR proteins on specific binding sites.

Indexed as

Models, ChemicalBinding, CompetitiveDNADNA-Binding ProteinsKineticsSolutionsStochastic ProcessesThermodynamicsDNADNA-Binding ProteinsSolutions

Identifiers

PMID24972228
PMCPMC4131839

What OpenQuestion holds

Textmetadata
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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.