Evidence map›Paper›PMID 21941250›Full record

ArticleNature chemistry2011

A single-molecule platform for investigation of interactions between G-quadruplexes and small-molecule ligands.

Deepak Koirala, Soma Dhakal, Beth Ashbridge, Yuta Sannohe, Raphaël Rodriguez, Hiroshi Sugiyama, Shankar Balasubramanian, Hanbin Mao

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

108 citing papers in PubMed, 221 citations in OpenAlex.

  1. Article
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  3. Mechanozyme: An Artificial Enzyme With a Mechanophore Framework.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  5. Comprehensive analysis and validation of mBMC veterinary research · 2026
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  6. Article
  7. Article
  8. Review
  9. Cell reports. Physical science · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Dynamic Structures and Fast Transition Kinetics of Oxidized G-Quadruplexes.Small (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

48 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Deepak KoiralaDepartment of Chemistry and Biochemistry and School of Biomedical Sciences, Kent State University, Kent, Ohio 44242, USA.
Soma Dhakal
Beth Ashbridge
Yuta Sannohe
Raphaël Rodriguez
Hiroshi Sugiyama
Shankar Balasubramanian
Hanbin Mao
Kent State University · USUniversity of Cambridge · GBKyoto University · JP

Funding

Effect of G-rich Higher Order Structures on Insulin Linked Polymorphism RegionR15DK081191 · NIDDK · KENT STATE UNIVERSITY · PI MAO, HANBIN · 2008 to 2010
$262k
Biotechnology and Biological Sciences Research Council BB/G008337/1Cancer Research UK 11961Cancer Research UK A11951NIDDK NIH HHS R15 DK081191NIDDK NIH HHS R15 DK081191-01
6 · The paper itself

Abstract

Ligands that stabilize the formation of telomeric DNA G-quadruplexes have potential as cancer treatments, because the G-quadruplex structure cannot be extended by telomerase, an enzyme over-expressed in many cancer cells. Understanding the kinetic, thermodynamic and mechanical properties of small-molecule binding to these structures is therefore important, but classical ensemble assays are unable to measure these simultaneously. Here, we have used a laser tweezers method to investigate such interactions. With a force jump approach, we observe that pyridostatin promotes the folding of telomeric G-quadruplexes. The increased mechanical stability of pyridostatin-bound G-quadruplex permits the determination of a dissociation constant K(d) of 490 ± 80 nM. The free-energy change of binding obtained from a Hess-like process provides an identical K(d) for pyridostatin and a K(d) of 42 ± 3 µM for a weaker ligand RR110. We anticipate that this single-molecule platform can provide detailed insights into the mechanical, kinetic and thermodynamic properties of liganded bio-macromolecules, which have biological relevance.

Indexed as

G-QuadruplexesLigandsAminoquinolinesDNAHumansKineticsOxazolesPicolinic AcidsTelomeraseTelomereThermodynamicsAminoquinolinesDNALigandsN2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamideOxazolesPicolinic AcidspyridostatinTelomerasetelomestatin

Identifiers

PMID21941250
PMCPMC3277938
OpenAlexW2126398144

What OpenQuestion holds

Textmetadata
LicenceTDM
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.