Evidence map›Paper›PMID 25245944›Full record

ArticleNucleic acids research2014

Strong DNA deformation required for extremely slow DNA threading intercalation by a binuclear ruthenium complex.

Ali A Almaqwashi, Thayaparan Paramanathan, Per Lincoln, Ioulia Rouzina, Fredrik Westerlund, Mark C Williams

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Hydrophobic catalysis and a potential biological role of DNA unstacking induced by environment effects.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

6 authors at 4 institutions in 2 countries.

Ali A AlmaqwashiDepartment of Physics, Northeastern University, Boston, MA 02115, USA.
Thayaparan ParamanathanDepartment of Physics, Northeastern University, Boston, MA 02115, USA Department of Physics, Bridgewater State University, Bridgewater, MA 02324, USA.
Per LincolnDepartment of Chemical and Biological Engineering, Chalmers University of Technology, Gothenburg SE-41296, Sweden.
Ioulia RouzinaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Fredrik WesterlundDepartment of Chemical and Biological Engineering, Chalmers University of Technology, Gothenburg SE-41296, Sweden.
Mark C WilliamsDepartment of Physics, Northeastern University, Boston, MA 02115, USA mark@neu.edu.
Chalmers University of Technology · SENortheastern University · USBridgewater State University · USUniversity of Minnesota · US

Funding

Single Molecule HIV-1 Replication InteractionsR01GM072462 · NIGMS · NORTHEASTERN UNIVERSITY · PI WILLIAMS, MARK C · 2004 to 2018
$3.9M
NIGMS NIH HHS GM072462
6 · The paper itself

Abstract

DNA intercalation by threading is expected to yield high affinity and slow dissociation, properties desirable for DNA-targeted therapeutics. To measure these properties, we utilize single molecule DNA stretching to quantify both the binding affinity and the force-dependent threading intercalation kinetics of the binuclear ruthenium complex Δ,Δ-[μ-bidppz-(phen)4Ru2]4+ (Δ,Δ-P). We measure the DNA elongation at a range of constant stretching forces using optical tweezers, allowing direct characterization of the intercalation kinetics as well as the amount intercalated at equilibrium. Higher forces exponentially facilitate the intercalative binding, leading to a profound decrease in the binding site size that results in one ligand intercalated at almost every DNA base stack. The zero force Δ,Δ-P intercalation Kd is 44 nM, 25-fold stronger than the analogous mono-nuclear ligand (Δ-P). The force-dependent kinetics analysis reveals a mechanism that requires DNA elongation of 0.33 nm for association, relaxation to an equilibrium elongation of 0.19 nm, and an additional elongation of 0.14 nm from the equilibrium state for dissociation. In cells, a molecule with binding properties similar to Δ,Δ-P may rapidly bind DNA destabilized by enzymes during replication or transcription, but upon enzyme dissociation it is predicted to remain intercalated for several hours, thereby interfering with essential biological processes.

Indexed as

Base PairingBinding SitesCoordination ComplexesDNAIntercalating AgentsKineticsCoordination ComplexesDNAIntercalating Agents

Identifiers

PMID25245944
PMCPMC4191423
OpenAlexW2142907809

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.