Evidence map›Paper›PMID 19433506›Full record

ArticleNucleic acids research2009

Analyzing the forces binding a restriction endonuclease to DNA using a synthetic nanopore.

B Dorvel, G Sigalov, Q Zhao, J Comer, V Dimitrov, U Mirsaidov, A Aksimentiev, G Timp

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Electrical unfolding of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Dynamics of a Molecular Plug Docked onto a Solid-State Nanopore.The journal of physical chemistry letters · 2018
    Article
  4. Article
  5. Graphene Nanopores for Protein Sequencing.Advanced functional materials · 2016
    Article
  6. Article
  7. Article
  8. Watching single proteins using engineered nanopores.Protein and peptide letters · 2014
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Molecular diagnostics for personal medicine using a nanopore.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology
    Review
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

8 authors at 1 institution in 1 country.

B DorvelBeckman Institute, University of Illinois, Urbana, IL 61801, USA.
G Sigalov
Q Zhao
J Comer
V Dimitrov
U Mirsaidov
A Aksimentiev
G Timp
University of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI STONE, JOHN H · 1990 to 2011
$19.8M
NEW APPROACHES TO DNA MAPPING--ELECTRONIC IMAGINGR01HG000371 · NHGRI · ASSOCIATED UNIV-BROOKHAVEN NATL LAB · PI SUTHERLAND, JOHN C · 1990 to 1992
–
NCRR NIH HHS 5 P41-RR05969NHGRI NIH HHS R01 HG003713A
6 · The paper itself

Abstract

Restriction endonucleases are used prevalently in recombinant DNA technology because they bind so stably to a specific target sequence and, in the presence of cofactors, cleave double-helical DNA specifically at a target sequence at a high rate. Using synthetic nanopores along with molecular dynamics (MD), we have analyzed with atomic resolution how a prototypical restriction endonuclease, EcoRI, binds to the DNA target sequence--GAATTC--in the absence of a Mg(2+) ion cofactor. We have previously shown that there is a voltage threshold for permeation of DNA bound to restriction enzymes through a nanopore that is associated with a nanonewton force required to rupture the complex. By introducing mutations in the DNA, we now show that this threshold depends on the recognition sequence and scales linearly with the dissociation energy, independent of the pore geometry. To predict the effect of mutation in a base pair on the free energy of dissociation, MD is used to qualitatively rank the stability of bonds in the EcoRI-DNA complex. We find that the second base in the target sequence exhibits the strongest binding to the protein, followed by the third and first bases, with even the flanking sequence affecting the binding, corroborating our experiments.

Indexed as

Computer SimulationDeoxyribonuclease EcoRIDNADNA-Binding ProteinsModels, MolecularNanostructuresProtein BindingDeoxyribonuclease EcoRIDNADNA-Binding Proteins

Identifiers

PMID19433506
PMCPMC2709577
OpenAlexW2125639965

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.